Influenza A virus (H1N1) currently prevailing in Asia causes fatal pneumonia and multiple organ failure in humans. The two principle polypeptides, the Hemagglutinin (HA) and the Neuraminidase (NA), which are the target for the neutralizing antibodies immune response.Despite intensive research, understanding of the characteristics of influenza A virus that determine its virulence is incomplete. There are various immune cells inactivation is causing swine flu. Therefore, current, hot task of influenza virus research is to look for a way how to get us closer to a universal vaccine.In this study aims to identify the 3D structure of H1N1-M2 channels, HA2 gp and eM2 protein structures of patient samples from swine flu. With an explicit water-membrane environment, the molecular docking studies were performed for Oseltamivir and Zanamivir, these two commercial drugs generally used to treat influenza A virus infection. It was found that their binding affinity to the H1N1-M2 channel is significantly lower than that to the H5N1-HA2 gp, M2 and eM2 protein channel, fully consistent with the recent report that the H1N1 swine virus was resistant to the 2 drugs. The findings the relevant analysis reported here might provide useful structural insights for developing effective drugs against the new swine flu virus.

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