Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120.
AIDS
; 4(10): 953-60, 1990 Oct.
Article
em En
| MEDLINE
| ID: mdl-1702001
ABSTRACT
Amino acid sequences inducing neutralizing antibodies to HIV-1 were sought. Murine monoclonal antibodies (MAbs) were characterized by their reactivity with the envelope precursor gp160 or the Escherichia coli recombinant DNA products pB1 and pE3 representing the carboxy- and amino-terminal halves of mature envelope gp120. Fine mapping of the MAb determinants was performed using defined 15-mer synthetic peptides spanning the entire envelope gp120 region of HIV-1. One group of MAbs recognizes epitopes (amino acids 304-323) occurring in a small region with variable and conserved amino acid sequences of gp120. These MAbs mediate neutralization of the HIV-1 strain HTLV-IIIB (HIV-1IIIB) which was used for immunization. Nine out of 11 primary HIV-1 isolates were neutralized well or moderately well. In addition, prominent serological reactivity was noted with peptide sequences of strains of various European or American origins, but not with two HIV-1 strains of African origin. The cross-reactivity contrasts with previously described type-specific reactions to other sequences of this region. The reactivity to the short conserved site GPGR with its flanking amino acids may explain the broad sequence cross-reactivity seen with our neutralizing MAbs. Two other MAbs recognize conserved epitopes (amino acids 79-103) situated in the amino-terminal region of gp120. These MAbs did not neutralize HIV-1IIIB.
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Base de dados:
MEDLINE
Assunto principal:
Anticorpos Anti-HIV
/
Proteína gp120 do Envelope de HIV
/
HIV-1
/
Anticorpos Monoclonais
Limite:
Animals
Idioma:
En
Ano de publicação:
1990
Tipo de documento:
Article