Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-2-18
pubmed:abstractText
Phage peptide libraries constitute powerful tools for the mapping of epitopes recognized by monoclonal antibodies. We report here the characterization of an antibody directed against a 20-residue peptide derived from the surface glycoprotein of the feline immunodeficiency virus. The isolation of the WRPDF consensus sequence from a phage display library defined the exact epitope recognized by the mAb. Compared with known immunogenic peptides of the FIV envelope, it corresponds to the most immunodominant peptide found in the whole molecule. Kinetic data describing the antibody-peptide interactions were obtained by surface plasmon resonance. The antibody binds the peptide with a KD in the nanomolar range.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0165-2478
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
A FIV epitope defined by a phage peptide library screened with a monoclonal anti-FIV antibody.
pubmed:affiliation
Institut Cochin de Génétique Moléculaire, Unité d'Immunopharmacologie moléculaire et génétique des virus, CNRS UPR 415, Paris, France. sibille@icgm.inserm.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't