Linked Life Data

1376537

Source:http://linkedlifedata.com/resource/pubmed/id/1376537

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-7-16
pubmed:abstractText
An improved binding assay for detection of ganglioside receptors for influenza A, B, and C viruses was developed. In this system, the virions bound to gangliosides that were developed on a silica gel thin-layer plate were detected by mouse monoclonal antibody against viral hemagglutinin and peroxidase-conjugated anti-mouse immunoglobin. No hydrolysis of the gangliosides by viral receptor-destroying enzyme was detected in the present condition. The reactivity of the viruses to gangliosides depended on the amount of developed gangliosides (10 pmols-10 nmols), the molecular species of sialic acid, and their sugar sequences. Human influenza A (PR/8/34), B (Lee/40), and C (Ann Arbor/1/50) viruses bound different receptor epitopes of sialo-sugar chains of gangliosides. The A/PR/8 virus bound most effectively to Neu5Ac-containing lacto-series gangliosides carrying type I and type II sugar chains, followed by ganglio-series and hematoside-series gangliosides. The A/PR/8 virus weakly bound to Neu5Ac alpha 2,6lactotetraosylceramide [IV6(Neu5Ac)Lc4Cer] and Neu5Ac alpha 2,6paragloboside [IV6(Neu5Ac)nLc4Cer] carrying Neu5Ac alpha 2,6Gal sequence, although their Neu5Ac alpha 2,3Gal derivatives were the most potent gangliosides tested. B/Lee/40 bound restrictively to IV6(Neu5Ac)Lc4Cer and IV6(Neu5Ac)nLc4Cer, which carry Neu5Ac alpha 2,6Gal sequence, and type I and type II lacto-series sugar chain, respectively. C/Ann Arbor/1/50 reacted only with 9-O-Ac-Neu5Ac-carrying sugar chains in all the gangliosides tested. This method also allowed the microanalysis of receptor gangliosides of unknown samples. ESK cells, sensitive to the influenza A viruses infection, expressed several kinds of receptor active gangliosides, while those from ESK-R cells, resistant to the virus infection, were undetectable.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
189
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
121-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Structural determination of gangliosides that bind to influenza A, B, and C viruses by an improved binding assay: strain-specific receptor epitopes in sialo-sugar chains.
pubmed:affiliation
Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't