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West Nile virus nonstructural protein NS1 inhibits complement activation by binding the regulatory protein factor H.


ABSTRACT: The complement system, by virtue of its dual effector and priming functions, is a major host defense against pathogens. Flavivirus nonstructural protein (NS)-1 has been speculated to have immune evasion activity, because it is a secreted glycoprotein, binds back to cell surfaces, and accumulates to high levels in the serum of infected patients. Herein, we demonstrate an immunomodulatory function of West Nile virus NS1. Soluble and cell-surface-associated NS1 binds to and recruits the complement regulatory protein factor H, resulting in decreased complement activation in solution and attenuated deposition of C3 fragments and C5b-9 membrane attack complexes on cell surfaces. Accordingly, extracellular NS1 may function to minimize immune system targeting of West Nile virus by decreasing complement recognition of infected cells.

SUBMITTER: Chung KM 

PROVIDER: S-EPMC1664712 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

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West Nile virus nonstructural protein NS1 inhibits complement activation by binding the regulatory protein factor H.

Chung Kyung Min KM   Liszewski M Kathryn MK   Nybakken Grant G   Davis Alan E AE   Townsend R Reid RR   Fremont Daved H DH   Atkinson John P JP   Diamond Michael S MS  

Proceedings of the National Academy of Sciences of the United States of America 20061128 50


The complement system, by virtue of its dual effector and priming functions, is a major host defense against pathogens. Flavivirus nonstructural protein (NS)-1 has been speculated to have immune evasion activity, because it is a secreted glycoprotein, binds back to cell surfaces, and accumulates to high levels in the serum of infected patients. Herein, we demonstrate an immunomodulatory function of West Nile virus NS1. Soluble and cell-surface-associated NS1 binds to and recruits the complement  ...[more]

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