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PLoS One. 2013 Oct 18;8(10):e78125. doi: 10.1371/journal.pone.0078125.
Sensitive and direct detection of receptor binding specificity of highly pathogenic avian influenza a virus in clinical samples.
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.
Source
Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Shizuoka, Japan.
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.
PMID:
24205123
[PubMed - in process]
PMCID:
PMC3799784
Free PMC Article
Sensitive and direct detection of receptor binding specificity of highly pathogenic avian influenza a virus in clinical samples.
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.
Source
Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Shizuoka, Japan.
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.
PMID:
24205123
[PubMed - in process]
PMCID:
PMC3799784
Free PMC Article
