IV mutation literature information.


  Comparative virulence of wild-type H1N1pdm09 influenza A isolates in swine.
 PMID: 25601799       2015       Veterinary microbiology
Abstract: A/Swine/IL/5265/2010 (IL/10), with substitutions I120M, S146G, S186P, V252M, had lower viral titers in the lungs and nasal secretions and fewer lung lesions.


  Evolution of the hemagglutinin protein of the new pandemic H1N1 influenza virus: maintaining optimal receptor binding by compensatory substitutions.
 PMID: 24109242       2013       Journal of virology
Abstract: Strikingly, two major variants harbor combinations of substitutions (S186P/A137T and S188T/A200T, respectively) with opposite individual effects on binding.
Abstract: Two changes (S186P and S188T) were shown to increase the receptor-binding avidity of HA, whereas two others (A137T and A200T) decreased binding avidity.


  Antibody pressure by a human monoclonal antibody targeting the 2009 pandemic H1N1 virus hemagglutinin drives the emergence of a virus with increased virulence in mice.
 PMID: 22647789       2012       mBio
Abstract: One mutation near the receptor binding site, S186P, increased the binding affinity of the HA to the receptor.


  A single base-pair change in 2009 H1N1 hemagglutinin increases human receptor affinity and leads to efficient airborne viral transmission in ferrets.
 PMID: 21407805       2011       PloS one
Result: However this would involve at least two amino acid substitutions, Ser186 Pro and Glu227 Ala, to make this interaction network similar to that observed in SC18 HA (Figure S1).



Browser Board

 Co-occurred Entities




   Filtrator