2oto: Difference between revisions

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~~'''~~N-terminal fragment of Streptococcus pyogenes M1 protein~~'''~~

===N-terminal fragment of Streptococcus pyogenes M1 protein===

~~==Overview==~~

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~~Antigenically variable M proteins are major virulence factors and immunogens of the human pathogen group A Streptococcus (GAS). Here~~, ~~we report~~ the ~~approximately 3 angstrom resolution structure of a GAS M1 fragment containing~~ the ~~regions responsible for eliciting type-specific, protective immunity and for binding fibrinogen, which promotes M1 proinflammatory and antiphagocytic functions~~. ~~The structure revealed substantial irregularities and instabilities throughout the coiled coil of the M1 fragment~~. ~~Similar structural irregularities occur in myosin and tropomyosin~~, ~~explaining~~ the ~~patterns of cross~~-reactivity seen in autoimmune sequelae of GAS infection. Sequence idealization of a large segment of the M1 coiled coil enhanced stability but diminished fibrinogen binding, proinflammatory effects, and antibody cross-~~reactivity, whereas it left protective immunogenicity undiminished. Idealized M proteins appear to have promise as vaccine immunogens.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18323455}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18323455 is the PubMed ID number.

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==About this Structure==

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[[Category: Toxin]]

[[Category: Virulence factor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 11~~:38:03 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:45:22 2008''

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-[[Image:2oto.jpg|left|200px]]
+{{Seed}}
+[[Image:2oto.png|left|200px]]
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 {{STRUCTURE_2oto|  PDB=2oto  |  SCENE=  }}
-'''N-terminal fragment of Streptococcus pyogenes M1 protein'''
+===N-terminal fragment of Streptococcus pyogenes M1 protein===
-==Overview==
+<!--
-Antigenically variable M proteins are major virulence factors and immunogens of the human pathogen group A Streptococcus (GAS). Here, we report the approximately 3 angstrom resolution structure of a GAS M1 fragment containing the regions responsible for eliciting type-specific, protective immunity and for binding fibrinogen, which promotes M1 proinflammatory and antiphagocytic functions. The structure revealed substantial irregularities and instabilities throughout the coiled coil of the M1 fragment. Similar structural irregularities occur in myosin and tropomyosin, explaining the patterns of cross-reactivity seen in autoimmune sequelae of GAS infection. Sequence idealization of a large segment of the M1 coiled coil enhanced stability but diminished fibrinogen binding, proinflammatory effects, and antibody cross-reactivity, whereas it left protective immunogenicity undiminished. Idealized M proteins appear to have promise as vaccine immunogens.
+The line below this paragraph, {{ABSTRACT_PUBMED_18323455}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18323455 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18323455}}
 ==About this Structure==
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 [[Category: Toxin]]
 [[Category: Virulence factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:38:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:45:22 2008''