ErpC, a member of the complement regulator-acquiring family of surface proteins from Borrelia burgdorferi, possesses an architecture previously unseen in this protein family.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 69(Pt 6): 624-8, 2013 Jun.
Article
em En
| MEDLINE
| ID: mdl-23722838
ABSTRACT
Borrelia burgdorferi is a spirochete responsible for Lyme disease, the most commonly occurring vector-borne disease in Europe and North America. The bacterium utilizes a set of proteins, termed complement regulator-acquiring surface proteins (CRASPs), to aid evasion of the human complement system by recruiting and presenting complement regulator factor H on its surface in a manner that mimics host cells. Presented here is the atomic resolution structure of a member of this protein family, ErpC. The structure provides new insights into the mechanism of recruitment of factor H and other factor H-related proteins by acting as a molecular mimic of host glycosaminoglycans. It also describes the architecture of other CRASP proteins belonging to the OspE/F-related paralogous protein family and suggests that they have evolved to bind specific complement proteins, aiding survival of the bacterium in different hosts.
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MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
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Receptores de Superfície Celular
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Borrelia burgdorferi
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Proteínas de Membrana
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article