Proteopedia - User contributions [en]

G13secL03Tpc3

2012-08-16T02:58:29Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/New_ospb/2' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/2'/>

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that reside in the gut of hard- bodied deer tick of the family ''Ixodidae''. They are transmitted in humans by the bite of this tick. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref> The structure and stability of Osp B is affected by this antibody causing the bacteria to lyse.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

===Interactions===
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. The loop forms electrostatic interaction and hydrogen bond interactions with the antibody's heavy chain. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. The Lysine interacts with the antibody by forming hydrogen bonds with the glutamine and histidine on the heavy chain of H6831. Loop 1, residues 231-233, also interacts with the Fab heavy chain forming two hydrogen bonds. Loop 3, residues 272-276, interact with the light chain, of the antibody with two hydrogen bonds. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the outer surface protein and make the bacteria more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly. The proteolytic activity of the antibody on the bacteria is presumably similar to a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. <ref name=Article4> PMID: 15128807 </ref> Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines for Osp B have not yet been discovered due to the increased variability in the epitope, as the vaccine wouldn’t be able to counteract a wide variety of strains of “Borrelia.” However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research as it is still currently misunderstood.

References: {{reflist}}

G13secL03Tpc3

2012-08-16T02:48:20Z

Enida Zekovic: /* Interactions */

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/New_ospb/2' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/2'/>

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that reside in the gut of hard- bodied deer tick of the family ''Ixodidae''. They are transmitted in humans by the bite of this tick. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref> The structure and stability of Osp B is affected by this antibody causing the bacteria to lyse.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

===Interactions===
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. The loop forms electrostatic interaction and hydrogen bond interactions with the antibody's heavy chain. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. The Lysine interacts with the antibody by forming hydrogen bonds with the glutamine and histidine on the heavy chain of H6831. Loop 1, residues 231-233, also interacts with the Fab heavy chain forming two hydrogen bonds. Loop 3, residues 272-276, interact with the light chain, of the antibody with two hydrogen bonds. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the outer surface protein and make the bacteria more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly. The proteolytic activity of the antibody on the bacteria is presumably similar to a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines for Osp B have not yet been discovered due to the increased variability in the epitope, as the vaccine wouldn’t be able to counteract a wide variety of strains of “Borrelia.” However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research as it is still currently misunderstood.

References: {{reflist}}

G13secL03Tpc3

2012-08-16T02:36:05Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/New_ospb/2' />
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Beta_sheet/2'/>

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that reside in the gut of hard- bodied deer tick of the family ''Ixodidae''. They are transmitted in humans by the bite of this tick. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref> The structure and stability of Osp B is affected by this antibody causing the bacteria to lyse.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

===Interactions===
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. The loop forms electrostatic interaction and hydrogen bond interactions with the antibody's heavy chain. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. The Lysine forms a hydrogen bond with a glutamine and histidine on the heavy chain on H6831. Loop 1, residues 231-233, also interacts with the Fab heavy chain forming two hydrogen bonds. Loop 3, residues 272-276, interact with the light chain, of the antibody with two hydrogen bonds. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the outer surface protein and make the bacteria more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly. The proteolytic activity of the antibody on the bacteria is presumably similar to a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease. Vaccines for Osp B have not yet been discovered due to the increased variability in the epitope, as the vaccine wouldn’t be able to counteract a wide variety of strains of “Borrelia.” However, the ability of H6381 and CB2 to make the bacteria subject to increased proteolytic activity is a possibility for future research as it is still currently misunderstood.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T16:46:00Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/1/1' />

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831. <ref name=Article1> PMID:7513309 </ref>

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.<ref name=Article2> PMID:15713683 </ref>

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain. <ref name=Article2> PMID:15864264 </ref>

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell. <ref name=Article3> PMID:15864264 </ref>
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

==Application==
OspB is capable of existing in various forms, with a different amino acid in place of Lysine-253, responsible for recognition of the antibody. Mutations occur in the residue of Lysine, which prevent it from being recognized and lysed by bactericidal Fabs such as H6381. The study of this structure of Osp B is important to combat future mechanisms of curing Lyme disease.

References: {{reflist}}

G13secL03Tpc3

2012-08-14T16:27:02Z

Enida Zekovic:

G13secL03Tpc3

2012-08-14T15:18:09Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/1/1' />

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

G13secL03Tpc3

2012-08-14T15:15:31Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

==Introduction==
<Structure load='1RJL' size='500' frame='true' align='right' scene='G13secL03Tpc3/Ospb/1' />

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

G13secL03Tpc3

2012-08-14T15:14:52Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

<Structure load='1RJL' size='500' frame='true' align='right'scene='G13secL03Tpc3/Ospb/1' />
==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

G13secL03Tpc3

2012-08-14T15:03:06Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/Ospb/1' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

G13secL03Tpc3

2012-08-14T15:01:57Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/Ospb/1' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

G13secL03Tpc3

2012-08-14T14:56:24Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|Mechanism of destruction by MAC on the bacteria, ''Borrelia burgdorferi'']]

G13secL03Tpc3

2012-08-14T14:54:16Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|]]

G13secL03Tpc3

2012-08-14T14:53:50Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='G13secL03Tpc3/' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. [http://en.wikipedia.org/wiki/Lyme_disease Lyme disease], caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is [http://iai.asm.org/content/76/11/5228.full Osp B]. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.
[[Image:Mac attack.PNG‎|thumb|400px|]]

File:Mac attack.PNG

2012-08-14T14:11:09Z

Enida Zekovic: uploaded a new version of "Image:Mac attack.PNG": Taken from Wikipedia, uploaded by Brazucs.

File:Mac attack.PNG

2012-08-14T14:04:06Z

Enida Zekovic:

G13secL03Tpc3

2012-08-14T13:55:07Z

Enida Zekovic:

== Outer Surface Protein B of ''Borrelia burgdorferi'' ==

Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

<Structure load='1RJL' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

==Introduction==

[http://en.wikipedia.org/wiki/Borrelia_burgdorferi ''Borrelia burgdorferi'']are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13secL03Tpc3

2012-08-14T13:44:18Z

Enida Zekovic:

G13SecL03Tpc3

2012-08-14T13:33:43Z

Enida Zekovic:

== Osp B of Borrelia burgdorferi ==
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

==Introduction==

''Borrelia burgdorferi'' are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by ''Borrelia burgdorferi'', is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13SecL03Tpc3

2012-08-14T13:32:50Z

Enida Zekovic:

== Osp B of Borrelia burgdorferi ==
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

==Introduction==

Borrelia burgdorferi are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by Borrelia burgdorferi, is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13SecL03Tpc3

2012-08-14T13:31:39Z

Enida Zekovic:

== Your Heading Here (maybe something like 'Structure') ==
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

==Introduction==

Borrelia burgdorferi are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by Borrelia burgdorferi, is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.
=== Destruction===
The bacteria lyses indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and disrupting it and causing death to the cell.

G13SecL03Tpc3

2012-08-14T13:27:05Z

Enida Zekovic: New page: == Your Heading Here (maybe something like 'Structure') == <StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry 1dq8)' scene=''> Any...

== Your Heading Here (maybe something like 'Structure') ==
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>

==Introduction==

Borrelia burgdorferi are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease, caused by Borrelia burgdorferi, is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that recognizes the destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis. This occurs indirectly, by a membrane attack complex (MAC). The complement system activates the classical pathway, activating effector proteins which insert themselves in the outer membrane of the bacteria and lyse it.

User:Enida Zekovic

2012-08-13T19:13:12Z

Enida Zekovic:

* Full Real Name: Enida Zekovic

* Position: Student

* Institution (NO ABBREVIATIONS):Stony Brook University

* City, State/Province, Country: Medford, NY, USA

* Field of Expertise or Study: Biology

==Introduction==

Borrelia burgdorferi are motile spirochetes that are carried by a hard- bodied deer tick of the family Ixodidae. Lyme disease is involved in many serious disorders of the skin, nervous and cardiac system. The bacterium consists of outer surface proteins that play an important role in helping the bacteria colonize and survive in the tick. Of these, a major lipoprotein is Osp B. This outer surface protein has a property of becoming lysed without a direct complement with the antibody. Specifically, the C terminus on the Osp B contains a Lysine residue that is a target for a destructive IgG antibody, H6831.

==Structure==

Osp B extends from Serine- 157 to Lysine- 296. It consists of twelve anti parallel beta sheets and one alpha helix. Sheets 1- 4 form a freestanding sheet, where sheets 5-12 form a barrel like domain. The Fab binding domain is in the center of the central beta sheet, residues 152-296.

==Interactions==
The structure of Osp B shows that there are three exposed loops in which are affected by the antibody, H6831. The majority of interaction comes between the antibody’s heavy chain and loop 2 on the lipoprotein, residues 250-254. Lysine 253, which resides on loop 2 play an important role in the recognition of the antibody, thus the antibody having the most interaction with loop 2. Loop 1, residues 231-233, also interacts with the Fab heavy chain as well as loop 3, residues 272-276, interacting with the light chain.

==Structural changes==
The more significant change that occurs from the bactericidal antibody is in the first four beta sheets. This sheet could have been proteolytically removed for reasons that are not certain. They may be due to autoproteolytic activity or proteolysis during crystallization. The surrounding sheets shift and overlap to replace the missing sheets. The removal of these sheets can affect the structure and stability of the outer surface protein making it more susceptible to lysis.