G14secL04Tpc3: Difference between revisions
From Proteopedia
Jump to navigationJump to search
| Line 22: | Line 22: | ||
and <scene name='G14secL04Tpc3/8-12_beta_strands_showing5/1'>8-12 </scene>form two sheets that bend, along with the final <scene name='G14secL04Tpc3/Alpha_helix2/1'>alpha helix </scene> | and <scene name='G14secL04Tpc3/8-12_beta_strands_showing5/1'>8-12 </scene>form two sheets that bend, along with the final <scene name='G14secL04Tpc3/Alpha_helix2/1'>alpha helix </scene> | ||
that comes over the top into the <scene name='G14secL04Tpc3/C-terminal_barrel_domain/5'>C terminal barrel domain</scene> | that comes over the top into the <scene name='G14secL04Tpc3/C-terminal_barrel_domain/5'>C terminal barrel domain</scene> | ||
. It has been shown that OspB deficient spirochetes lack the ability to bind to the tick gut <ref name ="critical" />. Further studies suggest that the structural barrel domain is what gives OspB the ability to adhere to the tick gut wall. The barrel domain cavity could serve as the binding site for an exposed protein loop, small peptide, or linear saccharide hanging off the tick gut wall<ref name="1rjl_pdb" />. <scene name='G14secL04Tpc3/1-4_beta_strands_showing3/2'>Beta strands 1-4</scene> on free OspB's N-terminus are cleaved when OspB is bound to antibody fragment H6831, suggesting that they're removed by the proteolysis in the H6831-bound complex<ref name = "1rjl_pdb" />. The OspB protein is an integral membrane lipoprotein, with its lipidated N-terminus imbedded in the outer membrane of the spirochete and its C-terminus directed away from the membrane<ref>M E Brandt, B S Riley, J D Radolf and M V Norgard. Immunogenic integral membrane proteins of ''Borrelia burgdorferi'' are lipoproteins Infect. Immun. 1990, 58(4):983. http://iai.asm.org/content/58/4/983.short</ref>. Therefore, it is speculated that proteolytic action on these N-terminus beta strands somehow cause lysis of the spirochete. Studies have shown that when complement-independent antibodies such as H6831 act on OspB, the result is blebbing of the outer membrane of the bacteria <ref name="Blebbing">Timothy J. LaRocca, David J. Holthausen, Chyongere Hsieh, Christian Renken, Carmen A. Mannella, Jorge L. Benach and Arturo Casadevall | . It has been shown that OspB deficient spirochetes lack the ability to bind to the tick gut <ref name ="critical" />. Further studies suggest that the structural barrel domain is what gives OspB the ability to adhere to the tick gut wall <ref name="1rjl_pdb" />. The barrel domain cavity could serve as the binding site for an exposed protein loop, small peptide, or linear saccharide hanging off the tick gut wall<ref name="1rjl_pdb" />. <scene name='G14secL04Tpc3/1-4_beta_strands_showing3/2'>Beta strands 1-4</scene> on free OspB's N-terminus are cleaved when OspB is bound to antibody fragment H6831, suggesting that they're removed by the proteolysis in the H6831-bound complex<ref name = "1rjl_pdb" />. The OspB protein is an integral membrane lipoprotein, with its lipidated N-terminus imbedded in the outer membrane of the spirochete and its C-terminus directed away from the membrane<ref>M E Brandt, B S Riley, J D Radolf and M V Norgard. Immunogenic integral membrane proteins of ''Borrelia burgdorferi'' are lipoproteins Infect. Immun. 1990, 58(4):983. http://iai.asm.org/content/58/4/983.short</ref>. Therefore, it is speculated that proteolytic action on these N-terminus beta strands somehow cause lysis of the spirochete. Studies have shown that when complement-independent antibodies such as H6831 act on OspB, the result is blebbing of the outer membrane of the bacteria <ref name="Blebbing">Timothy J. LaRocca, David J. Holthausen, Chyongere Hsieh, Christian Renken, Carmen A. Mannella, Jorge L. Benach and Arturo Casadevall | ||
Proceedings of the National Academy of Sciences of the United States of America , Vol. 106, No. 26 (Jun. 30, 2009), pp. 10752-10757 | Proceedings of the National Academy of Sciences of the United States of America , Vol. 106, No. 26 (Jun. 30, 2009), pp. 10752-10757 | ||
http://www.jstor.org/stable/40483625?&Search=yes&searchText=region&searchText=antibody&searchText=protein&searchText=directed&searchText=bactericidal&searchText=Borrelia&searchText=variable&searchText=burgdorferi&searchText=OspB&list=hide&searchUri=%2Faction%2FdoBasicSearch%3FQuery%3D%2BA%2Bbactericidal%2Bantibody%2Bto%2BBorrelia%2Bburgdorferi%2Bis%2Bdirected%2Bagainst%2Ba%2Bvariable%2Bregion%2Bof%2Bthe%2BOspB%2Bprotein%26acc%3Don%26wc%3Don&prevSearch=&item=3&ttl=7&returnArticleService=showFullText</ref>. This blebbing of the bacterial membrane has been shown to create small openings in the outer membrane of the bacteria, which leads for potential osmotic lysis depending on the solution the bacteria is in<ref name="Blebbing" />. | http://www.jstor.org/stable/40483625?&Search=yes&searchText=region&searchText=antibody&searchText=protein&searchText=directed&searchText=bactericidal&searchText=Borrelia&searchText=variable&searchText=burgdorferi&searchText=OspB&list=hide&searchUri=%2Faction%2FdoBasicSearch%3FQuery%3D%2BA%2Bbactericidal%2Bantibody%2Bto%2BBorrelia%2Bburgdorferi%2Bis%2Bdirected%2Bagainst%2Ba%2Bvariable%2Bregion%2Bof%2Bthe%2BOspB%2Bprotein%26acc%3Don%26wc%3Don&prevSearch=&item=3&ttl=7&returnArticleService=showFullText</ref>. This blebbing of the bacterial membrane has been shown to create small openings in the outer membrane of the bacteria, which leads for potential osmotic lysis depending on the solution the bacteria is in<ref name="Blebbing" />. | ||
==OspB complexed with H6831 Antibody Fab Fragment== | ==OspB complexed with H6831 Antibody Fab Fragment== | ||
