Linked Life Data

9240690

Source:http://linkedlifedata.com/resource/pubmed/id/9240690

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-8-14
pubmed:abstractText
The influenza virus A hemagglutinin (HA) is a trimeric glycoprotein that contains 3-9 N-linked glycosylation sequons per subunit, depending on the strain. The location of these sites is determined by the nucleotide sequence of the HA gene, and, since the viral genome is replicated by an error-prone RNA polymerase, mutations, which add or remove glycosylation sites, occur at a high frequency. Mutations that are not lethal to the virus add to the structural diversity of the virus population. Factors that determine the glycosylation of the HA are reviewed herein, as are the effects of host-specific glycosylation on receptor binding, fusion activity, and antigenic properties of the virus. Effects of host-specific glycosylation and selection on virulence and on vaccine efficacy and surveillance are discussed. In addition, inadequacies in our understanding of HA glycosylation and its effects on host range are emphasized.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1899
pubmed:author
pubmed:issnType
Print
pubmed:volume
176 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
S24-8
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Effects of glycosylation on the properties and functions of influenza virus hemagglutinin.
pubmed:affiliation
Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, Missouri 63104, USA.
pubmed:publicationType
Journal Article, Review