Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-8-27
pubmed:abstractText
A 22-amino-acid-long multibranched peptide construct (CLV) derived from the cleavage region (KIEPLGVAPTKAKRR*VVQREKR*) of the human immunodeficiency virus (HIV) type-1 envelope precursor inhibits HIV infection (Virology, 1996, 223, 406-408). We attempted to characterize its activity for Env expressed via a recombinant vaccinia virus (rVV): gp 160 cleavage was delayed, but not impaired, in the presence of CLV (10 microM), whereas neither Env production nor Env membrane expression was significantly altered. Through the synthesis of analogs, we concluded that the presence of a cleavage sequence was required for inhibition of syncytium formation by CLV in rVV-infected CD(4+) cell cultures: indeed, a single amino acid residue substitution (R* > S) in the cleavage sites presented by CLV abolished its activity. Other analogs allowed us to further determine the region of CLV which mediates its activity. The ability of a radiolabeled CLV analog to enter cells was also shown. Although, these data strongly suggest that CLV acts on Env fusogenicity at least partially through interference with gp160 processing.
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:day
1
pubmed:volume
247
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
137-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
An anti-HIV peptide construct derived from the cleavage region of the Env precursor acts on Env fusogenicity through the presence of a functional cleavage sequence.
pubmed:affiliation
CNRS, Faculté de Médecine Nord, Marseille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't