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1994-10-24
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Document 2062
DOCN M94A2062
TI Synthetic peptides from the V3 loop modulate HIV-1 infection.
DT 9412
AU Zanotto C; De Rossi A; Calderazzo F; Cabrelle A; Dettin M; Di Bello C;
Chieco-Bianchi L; Inst. Oncology, University of Padova, Italy.
SO Int Conf AIDS. 1994 Aug 7-12;10(1):39 (abstract no. 131A). Unique
Identifier : AIDSLINE ICA10/94370513
AB OBJECTIVE: It has been demonstrated that a 23-mer peptide (DB3) derived
from the V3 loop of MN strain enhances HIV-1 infection (Virol. 1991;
184, 187, Biochem. Biophys. Res. Commun. 1993; 191, 364). We have
studied the mechanism and structural features required for this
biological effect. METHODS: DB3 analogues with a single amino acid
substitution and shortened derivatives were prepared. MOLT-3 cells were
infected with HIV-1 in the presence of scalar dilutions of these
peptides. HIV-1 p24 antigen levels in supernatants were determined by an
Elisa assay. Expression of CD4 molecules on the peptide-treated cells
was quantitated by cytofluorimetric analyses. Soluble CD4-gp120 Elisa
assays were performed in the presence of scalar dilutions of the
peptides. RESULTS: We found that the substitution of Lysine with
Asparagine near the C-terminus (peptide DB3-Asn19) increased the
enhancing effect of DB3 while the replacement of any other positively
charged amino acid decreased the peptide's activity on viral infection.
Peptides in which an aromatic amino acid was changed to Isoleucine,
peptides with D-amino acids, and shortened derivatives of DB3, did not
show any enhancing effect. DB3 and DB3-Asn19 enhanced CD4 expression and
gp120 binding to soluble CD4; all other tested peptides did not.
CONCLUSIONS: These results suggest that the effect of DB3 on the viral
infection process is influenced by the presence of positively charged
and aromatic amino acids and by the conformation of the primary
sequence. Moreover, this activity appears to be mediated by an increase
in CD4 expression and/or CD4-gp120 binding affinity.
DE Amino Acid Sequence Antigens, CD4/ANALYSIS DNA-Binding
Proteins/PHARMACOLOGY Enzyme-Linked Immunosorbent Assay Flow Cytometry
HIV Core Protein p24/IMMUNOLOGY HIV Envelope Protein
gp120/ANALYSIS/METABOLISM HIV-1/*GENETICS
Peptides/*GENETICS/PHARMACOLOGY MEETING ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).