有哪些信誉好的足球投注网站a single base-pair change in 2009 h1n1 hemagglutinin increases human receptor affinity and leads to efficient airborne viral transmission in ferrets单个碱基对改变2009年甲型h1n1流感病毒血凝素增加人类受体亲和力并导致有效的雪貂的空气病毒传播.pdfVIP
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a single base-pair change in 2009 h1n1 hemagglutinin increases human receptor affinity and leads to efficient airborne viral transmission in ferrets单个碱基对改变2009年甲型h1n1流感病毒血凝素增加人类受体亲和力并导致有效的雪貂的空气病毒传播
A Single Base-Pair Change in 2009 H1N1 Hemagglutinin
Increases Human Receptor Affinity and Leads to Efficient
Airborne Viral Transmission in Ferrets
1 2 1 2 1
Akila Jayaraman , Claudia Pappas , Rahul Raman , Jessica A. Belser , Karthik Viswanathan , Zachary
1 2 1
Shriver , Terrence M. Tumpey , Ram Sasisekharan *
1 Harvard-MIT Division of Health Sciences and Technology, Singapore-MIT Alliance for Research and Technology, Department of Biological Engineering, Koch Institute for
Integrative Cancer Research, Massachusetts Institute of Technology (MIT), Cambridge, Massachusetts, United States of America, 2 Influenza Division, Centers for Disease
Control and Prevention (CDC), Atlanta, Georgia, United States of America
Abstract
The 2009 H1N1 influenza A virus continues to circulate among the human population as the predominant H1N1 subtype.
Epidemiological studies and airborne transmission studies using the ferret model have shown that the transmission
efficiency of 2009 H1N1 viruses is lower than that of previous seasonal strains and the 1918 pandemic H1N1 strain. We
recently correlated this reduced transmission efficiency to the lower binding affinity of the 2009 H1N1 hemagglutinin (HA)
to a2R6 sialylated glycan receptors (human receptors). Here we report that a single point mutation (Ile219RLys; a base
pair change) in the glycan receptor-binding site (RBS) of a representative 2009 H1N1 influenza A virus, A/California/04/09 or
CA04/09, quantitatively increases its human receptor-binding affinity. The increased human receptor-affinity is in the same
range as that of the HA from highly transmi
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