Linked Life Data

12034479

Source:http://linkedlifedata.com/resource/pubmed/id/12034479

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-29
pubmed:databankReference
pubmed:abstractText
Previously, we have shown that an H3N2 influenza virus (clone 7a) induced more apoptosis in MDCK cells than an H1N1 (A/Fiji) influenza virus and that the virion neuraminidase (NA) played a role in the induction of apoptosis. In this study we have examined a further 6 N2 (H3/H2) and 3 N1 (Hsw/H1) viruses and confirmed that the N2 viruses induce more apoptosis in MDCK cells than the N1 viruses. Furthermore, the level of apoptosis, the level of cell infection and the NA activity of the virus preparations paralleled each other for all the viruses. The levels of infection depended upon the degree of interaction of the viral haemagglutinin (HA) with its receptors: while all the viruses utilised NeuAc alpha-2,6 Gal containing receptors, the H3/H2 viruses showed a greater interaction than the Hsw/H1 viruses. Removal of sialic acid from virions by treatment with bacterial NA enhanced infection and apoptosis but the effect was much greater for the A/Fiji virus than for the clone 7a virus. Thus, while the relative interaction of the HAs for their receptors is the major factor influencing infectivity and apoptosis, the viral NA possibly plays an indirect role by removing sialic acid from the HA, thereby increasing its receptor binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-31
pubmed:dateRevised
2005-11-22
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Correlation between levels of apoptosis, levels of infection and haemagglutinin receptor binding interaction of various subtypes of influenza virus: does the viral neuraminidase have a role in these associations.
pubmed:affiliation
School of BioSciences, The University of Birmingham, Edgbaston, Birminghm B15 2TT, UK.
pubmed:publicationType
Journal Article