tetano
Editor, Senior Moderator
J Virol. 2013 Oct 23. [Epub ahead of print]
Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyper-glycosylation of the globular head domain.
Eggink D, Goff PH, Palese P.
Source
Department of Microbiology.
Abstract
Influenza virus hemagglutinin consists of a highly variable and immunodominant head domain and a more conserved, but immunosubdominant stalk domain. We introduced seven N-linked glycosylation sites in the hemagglutinin head domain to shield the immunodominant antigenic sites. The hyper-glycosylated hemagglutinin enhanced stalk-directed seroreactivity while dampening the head response in immunized mice. Upon influenza virus challenge, mice vaccinated with the hyper-glycosylated hemagglutinin were better protected against morbidity and mortality compared to mice receiving the wild-type hemagglutinin.
PMID:
24155380
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24155380
Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyper-glycosylation of the globular head domain.
Eggink D, Goff PH, Palese P.
Source
Department of Microbiology.
Abstract
Influenza virus hemagglutinin consists of a highly variable and immunodominant head domain and a more conserved, but immunosubdominant stalk domain. We introduced seven N-linked glycosylation sites in the hemagglutinin head domain to shield the immunodominant antigenic sites. The hyper-glycosylated hemagglutinin enhanced stalk-directed seroreactivity while dampening the head response in immunized mice. Upon influenza virus challenge, mice vaccinated with the hyper-glycosylated hemagglutinin were better protected against morbidity and mortality compared to mice receiving the wild-type hemagglutinin.
PMID:
24155380
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24155380