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Immunization by avian H5 influenza hemagglutinin mutants with altered receptor binding specificity.


ABSTRACT: Influenza virus entry is mediated by the receptor binding domain (RBD) of its spike, the hemagglutinin (HA). Adaptation of avian viruses to humans is associated with HA specificity for alpha2,6- rather than alpha2,3-linked sialic acid (SA) receptors. Here, we define mutations in influenza A subtype H5N1 (avian) HA that alter its specificity for SA either by decreasing alpha2,3- or increasing alpha2,6-SA recognition. RBD mutants were used to develop vaccines and monoclonal antibodies that neutralized new variants. Structure-based modification of HA specificity can guide the development of preemptive vaccines and therapeutic monoclonal antibodies that can be evaluated before the emergence of human-adapted H5N1 strains.

SUBMITTER: Yang ZY 

PROVIDER: S-EPMC2367145 | biostudies-other | 2007 Aug

REPOSITORIES: biostudies-other

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Immunization by avian H5 influenza hemagglutinin mutants with altered receptor binding specificity.

Yang Zhi-Yong ZY   Wei Chih-Jen CJ   Kong Wing-Pui WP   Wu Lan L   Xu Ling L   Smith David F DF   Nabel Gary J GJ  

Science (New York, N.Y.) 20070801 5839


Influenza virus entry is mediated by the receptor binding domain (RBD) of its spike, the hemagglutinin (HA). Adaptation of avian viruses to humans is associated with HA specificity for alpha2,6- rather than alpha2,3-linked sialic acid (SA) receptors. Here, we define mutations in influenza A subtype H5N1 (avian) HA that alter its specificity for SA either by decreasing alpha2,3- or increasing alpha2,6-SA recognition. RBD mutants were used to develop vaccines and monoclonal antibodies that neutral  ...[more]

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