Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1992-12-3
pubmed:abstractText
Receptor-binding properties of influenza viruses are usually characterized by the ability of viruses to interact with more or less defined sialic acid-containing carbohydrates, glycoproteins, or glycolipids assayed by haemagglutination (HA) or HA inhibition (HAI) tests. To overcome some drawbacks of these tests a solid-phase enzyme linked assay analogous to sandwich ELISA was developed. The virus is adsorbed specifically to the well of plastic microtitre plates coated with fetuin, and the binding of horseradish peroxidase (HRP)labelled sialylglycoproteins (SGPs) by the solid phase-attached virions is measured. The binding of unlabelled compounds is measured by competition with the attachment of a standard fetuin-HRP conjugate. The assay is easy to perform, quantitative (allows the determination of affinity constants), and sensitive (even the weak binding of free N-acetylneuraminic acid with Kd about 10(-1)-10(-2) M(-1) can be studied). Due to a higher stability of components of the present test system, as compared to red blood cells, the influence of pH, ionic strength, and other factors on virus-receptor interaction can also be investigated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0166-0934
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-23
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
A solid-phase enzyme-linked assay for influenza virus receptor-binding activity.
pubmed:affiliation
Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't