Linked Life Data

1962453

Source:http://linkedlifedata.com/resource/pubmed/id/1962453

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-1-7
pubmed:abstractText
To complete our analysis of the E2 glycoprotein of Venezuelan equine encephalomyelitis (VEE) virus, we prepared six synthetic peptides corresponding to the extramembranal carboxy-terminal one-third of the protein. NIH-Swiss mice were immunized with the peptides, and antipeptide and antiviral titers were determined by enzyme-linked immunosorbent assay (ELISA). Challenge studies revealed that peptide 13 (amino acids 241-265) protected 60-70% of virus-challenged mice. Although the other peptides generally elicited antipeptide ELISA titers but no or low antiviral titers and did not protect mice, significant E2 reactivity was found in immunoblots. These results provide the first direct evidence that much of the E2 carboxy-terminal domain is cryptic in the VEE virion, even when virus was bound to polystyrene ELISA plates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
185
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
840-2
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Synthetic peptides of Venezuelan equine encephalomyelitis virus E2 glycoprotein. III. Identification of a protective peptide derived from the carboxy-terminal extramembranal one-third of the protein.
pubmed:affiliation
Division of Vector-Borne Infectious Diseases, Centers for Disease Control, Fort Collins, Colorado 80522.
pubmed:publicationType
Journal Article