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  • Title: Sensitive and direct detection of receptor binding specificity of highly pathogenic avian influenza A virus in clinical samples.
    Author: Takahashi T, Kawakami T, Mizuno T, Minami A, Uchida Y, Saito T, Matsui S, Ogata M, Usui T, Sriwilaijaroen N, Hiramatsu H, Suzuki Y, Suzuki T.
    Journal: PLoS One; 2013; 8(10):e78125. PubMed ID: 24205123.
    Abstract:
    Influenza A virus (IAV) recognizes two types of N-acetylneuraminic acid (Neu5Ac) by galactose (Gal) linkages, Neu5Acα2,3Gal and Neu5Acα2,6Gal. Avian IAV preferentially binds to Neu5Acα2,3Gal linkage, while human IAV preferentially binds to Neu5Acα2,6Gal linkage, as a virus receptor. Shift in receptor binding specificity of avian IAV from Neu5Acα2,3Gal linkage to Neu5Acα2,6Gal linkage is generally believed to be a critical factor for its transmission ability among humans. Surveillance of this shift of highly pathogenic H5N1 avian IAV (HPAI) is thought to be a very important for prediction and prevention of a catastrophic pandemic of HPAI among humans. In this study, we demonstrated that receptor binding specificity of IAV bound to sialo-glycoconjugates was sensitively detected by quantifying the HA gene with real-time reverse-transcription-PCR. The new assay enabled direct detection of receptor binding specificity of HPAIs in chicken clinical samples including trachea and cloaca swabs in only less than 4 h.
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