Giuseppe
Emeritus
[Source: US National Library of Medicine, full page: (LINK). Abstract, edited.]
J Virol. 2013 Sep 11. [Epub ahead of print]
Structural analysis of the hemagglutinin from the recent 2013 H7N9 influenza virus.
Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J.
Source: Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, GA.
Abstract
In March 2013, the Chinese Centers for Disease Control and Prevention reported human infections with an H7N9 influenza virus, and by July 20<SUP>th</SUP> 2013, the numbers of laboratory-confirmed cases had climbed to 134, including 43 fatalities and 127 hospitalizations. The newly emerging H7N9 viruses constitute an obvious public health concern because of the apparent severity of this outbreak. Here we focus on the hemagglutinin (HA) of these viruses and assess its receptor binding phenotype in relation to previous HAs studied. Glycan microarray and kinetic analysis of recombinant A(H7N9) HAs was performed to compare the receptor binding profile of wild-type receptor binding site variants, at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs suggesting that these viruses require further adaptation in order to adapt fully to humans.
PMID: 24027325 [PubMed - as supplied by publisher]
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J Virol. 2013 Sep 11. [Epub ahead of print]
Structural analysis of the hemagglutinin from the recent 2013 H7N9 influenza virus.
Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J.
Source: Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, GA.
Abstract
In March 2013, the Chinese Centers for Disease Control and Prevention reported human infections with an H7N9 influenza virus, and by July 20<SUP>th</SUP> 2013, the numbers of laboratory-confirmed cases had climbed to 134, including 43 fatalities and 127 hospitalizations. The newly emerging H7N9 viruses constitute an obvious public health concern because of the apparent severity of this outbreak. Here we focus on the hemagglutinin (HA) of these viruses and assess its receptor binding phenotype in relation to previous HAs studied. Glycan microarray and kinetic analysis of recombinant A(H7N9) HAs was performed to compare the receptor binding profile of wild-type receptor binding site variants, at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs suggesting that these viruses require further adaptation in order to adapt fully to humans.
PMID: 24027325 [PubMed - as supplied by publisher]
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