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Influenza A virus M1 blocks the classical complement pathway through interacting with C1qA

Institute of Microbiology, Chinese Academy of Sciences, Beijing, P. R. China

¹ E-mail: yex{at}im.ac.cn

The matrix (M1) protein of influenza A virus is a conserved multifunctional protein that plays essential roles in regulating viral life cycle. Here we demonstrate that M1 protein is able to interact with complement C1qA and plays an important inhibitory function in the classical complement pathway. The N terminal domain of M1 protein is required for its binding to the globular region of C1qA. As a consequence, M1 blocks the interaction between C1qA and heat aggregated IgG in vitro and inhibits hemolysis. We are able to show that M1 protein prevents the complement mediated neutralization of influenza virus in vitro. In addition, studies on mice indicate that the administration of M1 can promote a higher virus propagation rate in lung and shortened survival of mice infected with the virus. Taken together, these results strongly suggest that M1 protein plays a critical role in protecting the influenza virus from host innate immune system.

Received 11 June 2009; accepted 30 July 2009.