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10.1016/j.virol.2011.01.036 http://scihub22266oqcxt.onion/10.1016/j.virol.2011.01.036 21353279!ä!21353279 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=21353279&cmd=llinks): Failed to open stream: HTTP request failed! 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Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice |pdf=|usr=}}{{21353279}} gab.com Text Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice JO: Virology http://www.kidney.de/pget.php?&tw=1&pmid=21353279 #FOAvip Collectins in airway fluids and membrane-associated lectins such as the macrophage mannose receptor (MMR) recognize mannose-rich glycans on the envelope glycoproteins of influenza A viruses. In this study, we used a reverse genetic approach to examine the role of particular N-linked glycosylation sites on the hemagglutinin (HA) of A/Beijing/353/89 (Beij/89, H3N2) in determining sensitivity to lectin-mediated immune defenses and virulence in mice. We generated 7:1 reassortant viruses on an A/PR/8/34 'backbone' with Beij/89 HA or HA lacking one or more glycosylation sites. Asn(165) was an important determinant of sensitivity to mouse collectins and virulence but did not alter susceptibility of airway macrophages to infection. Removal of both Asn(165) and Asn(246) led to a further increase in virulence, characterized by enhanced virus replication, pulmonary inflammation and vascular leak. These studies define the importance of particular glycans on H3 HA in determining sensitivity to airway collectins and virulence in mice. Twit Text FOAVip Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice ????Virology http://www.kidney.de/pget.php?&tw=1&pmid=21353279 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21353279 #FOAvip English Wikipedia <ref>{{Cite pmid|21353279}}</ref> Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice #MMPMID21353279 Tate MD; Job ER; Brooks AG; Reading PC Virology 2011[Apr]; 413 (1): 84-92 PMID21353279show ga Collectins in airway fluids and membrane-associated lectins such as the macrophage mannose receptor (MMR) recognize mannose-rich glycans on the envelope glycoproteins of influenza A viruses. In this study, we used a reverse genetic approach to examine the role of particular N-linked glycosylation sites on the hemagglutinin (HA) of A/Beijing/353/89 (Beij/89, H3N2) in determining sensitivity to lectin-mediated immune defenses and virulence in mice. We generated 7:1 reassortant viruses on an A/PR/8/34 'backbone' with Beij/89 HA or HA lacking one or more glycosylation sites. Asn(165) was an important determinant of sensitivity to mouse collectins and virulence but did not alter susceptibility of airway macrophages to infection. Removal of both Asn(165) and Asn(246) led to a further increase in virulence, characterized by enhanced virus replication, pulmonary inflammation and vascular leak. These studies define the importance of particular glycans on H3 HA in determining sensitivity to airway collectins and virulence in mice. |Animals[MESH] |Collectins/genetics/immunology[MESH] |Glycosylation[MESH] |Hemagglutinins, Viral/genetics/*metabolism[MESH] |Humans[MESH] |Immunity, Innate[MESH] |Influenza A Virus, H3N2 Subtype/genetics/*metabolism/*pathogenicity[MESH] |Influenza, Human/*immunology/virology[MESH] |Male[MESH] |Mice[MESH] |Mice, Inbred C57BL[MESH] |Respiratory System/*immunology/virology[MESH]Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 i(epmc).pdf DeepDyve Pubget Overpricing