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Titolo:
ADAPTATION OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 TO CELLS EXPRESSINGA BINDING-DEFICIENT CD4 MUTANT (LYSINE-46 TO ASPARTIC-ACID)
Autore:
CHOE HR; SODROSKI J;
Indirizzi:
HARVARD UNIV,SCH MED,DANA FARBER CANC INST,DIV HUMAN RETROVIROL,JFB 824,44 BINNEY ST BOSTON MA 02115 HARVARD UNIV,SCH MED,DANA FARBER CANC INST,DIV HUMAN RETROVIROL BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT PATHOL BOSTON MA 02115 HARVARD UNIV,SCH PUBL HLTH,DEPT CANC BIOL BOSTON MA 02115
Titolo Testata:
Journal of virology
fascicolo: 5, volume: 69, anno: 1995,
pagine: 2801 - 2810
SICI:
0022-538X(1995)69:5<2801:AOHTTC>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN MONOCLONAL-ANTIBODY; ENVELOPE GLYCOPROTEIN FUNCTION; RECOMBINANT SOLUBLE CD4; SYNCYTIUM FORMATION; T-CELL; RECEPTOR-BINDING; HTLV-III; TRANSMEMBRANE GLYCOPROTEIN; NEUTRALIZING ANTIBODIES; MEMBRANE-FUSION;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
115
Recensione:
Indirizzi per estratti:
Citazione:
H.R. Choe e J. Sodroski, "ADAPTATION OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 TO CELLS EXPRESSINGA BINDING-DEFICIENT CD4 MUTANT (LYSINE-46 TO ASPARTIC-ACID)", Journal of virology, 69(5), 1995, pp. 2801-2810

Abstract

Human immunodeficiency virus (HIV-1) was adapted to replicate efficiently in cells expressing an altered form of the CD4 viral receptor. The mutant CD4 (46 K/D) contained a single amino acid change (lysine 46 to aspartic acid) in the CDR2 loop of domain 1, which results in a 15-fold reduction in affinity for the viral gp120 glycoprotein. The ability of the adapted virus to replicate in CD4 46 K/D-expressing cells was independently enhanced by single amino acid changes in the V2 variable loop, the V3 variable loop, and the fourth conserved (C4) region ofthe gp120 glycoprotein. Combinations of these amino acids in the sameenvelope glycoprotein resulted in additive enhancement of virus replication in cells expressing the CD4 46 K/D molecule. In cells expressing the wild-type CD4 glycoproteins, the same V2 and V3 residue changes also increased the efficiency of replication of a virus exhibiting decreased receptor-binding ability due to an amino acid change (aspartic acid 368 to glutamic acid) in the gp120 glycoprotein. In neither instance did the adaptive changes restore the binding ability of the monomeric gp120 glycoprotein or the oligomeric envelope glycoprotein complexfor the mutant or wild-type CD4 glycoproteins, respectively. Thus, particular conformations of the gp120 V2 and V3 variable loops and of the C4 region allow postreceptor binding events in the membrane fusion process to occur in the context of less than optimal receptor binding. These results suggest that the fusion-related functions of the V2, V3,and C4 regions of gp120 are modulated by CD4 binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 20:15:13