Linked Life Data

2374008

Source:http://linkedlifedata.com/resource/pubmed/id/2374008

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-8-24
pubmed:abstractText
The nucleotide and amino acid sequences of the mRNA and predicted polypeptide of the integral membrane small hydrophobic (SH) protein of human respiratory syncytial virus strain 18537 (a prototype strain of antigenic subgroup B) were determined from cloned cDNA. At the nucleotide and amino acid levels there was 78% and 76% identity, respectively, with the previously described SH mRNA and protein of strain A2 (a prototype strain of subgroup A). Most of the amino acid substitutions occurred in the predicted ectodomain (50% identity). The pattern of posttranslational processing of the strain 18537 SH protein was very similar to that of strain A2, yielding a nonglycosylated form and two glycosylated forms. Analysis of released virions of strain A2 by immunoprecipitation with SH-specific antibodies suggested that the major non-glycosylated species and one of the glycosylated species are virion structural components.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
71 ( Pt 7)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1571-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The small hydrophobic protein of human respiratory syncytial virus: comparison between antigenic subgroups A and B.
pubmed:affiliation
Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article, Comparative Study