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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-8-21
pubmed:abstractText
Eighteen synthetic peptides have now been prepared from dengue (DEN) 2 virus, representing 80% of the extra-membranal domain of the DEN envelope (E)-glycoprotein. These peptides were selected based upon our previous results with Murray Valley encephalitis (MVE) virus, computer analysis of the DEN virus sequence, and the predicted E-glycoprotein secondary structure. Six of these peptides were "structural" peptides derived from either nonlinear amino acid sequences or predicted disulfide bridge-stabilized loop structures. As with MVE virus, some peptides could be recognized by antivirus hyperimmune ascitic fluids, but monoclonal antiflavivirus antibodies failed to react with any peptide. Immunogenicity of these peptides was tested in BALB/c or NIH-Swiss mice. Fourteen of these peptides elicited antipeptide antibody in one or both mouse strains. Eleven of these antipeptides reacted with virus. Peptides 35 (amino acids 35-55) and 17 (amino acids 352-368) elicited virus-neutralizing antibody. Four antipeptides were more efficient at binding to pH 5.0-treated virus. These antipeptides precisely defined a flavivirus group common sequence (amino acids 98-110) that has biochemical characteristics similar to previously defined viral fusion sequences.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
177
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
668-75
pubmed:dateRevised
2005-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Antibodies to dengue 2 virus E-glycoprotein synthetic peptides identify antigenic conformation.
pubmed:affiliation
Division of Vector-Borne Infectious Diseases, Centers for Disease Control, Fort Collins, Colorado 80522.
pubmed:publicationType
Journal Article