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Titolo:
IDENTIFICATION OF AN N-LINKED GLYCAN IN THE V1-LOOP OF HIV-1 GP120 INFLUENCING NEUTRALIZATION BY ANTI-V3 ANTIBODIES AND SOLUBLE CD4
Autore:
GRAM GJ; HEMMING A; BOLMSTEDT A; JANSSON B; OLOFSSON S; AKERBLOM L; NIELSEN JO; HANSEN JES;
Indirizzi:
HVIDOVRE UNIV HOSP,INFECT DIS LAB 144,KETTEGARD ALLE 30 DK-2650 HVIDOVRE DENMARK GOTHENBURG UNIV,DEPT CLIN VIROL S-41346 GOTHENBURG SWEDEN NATL VET INST,CTR BIOMED,DEPT VIROL S-75007 UPPSALA SWEDEN
Titolo Testata:
Archives of virology
fascicolo: 3-4, volume: 139, anno: 1994,
pagine: 253 - 261
SICI:
0304-8608(1994)139:3-4<253:IOANGI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; ENVELOPE GLYCOPROTEINS; TYPE-1; REGION; HTLV; DETERMINANT; INFECTIVITY; VARIANTS; AFFINITY; ASSAY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
G.J. Gram et al., "IDENTIFICATION OF AN N-LINKED GLYCAN IN THE V1-LOOP OF HIV-1 GP120 INFLUENCING NEUTRALIZATION BY ANTI-V3 ANTIBODIES AND SOLUBLE CD4", Archives of virology, 139(3-4), 1994, pp. 253-261

Abstract

Glycosylation is necessary for HIV-1 gp120 to attain a functional conformation, and individual N-linked glycans of gp120 are important, butnot essential, for replication of HIV-I in cell culture. We have constructed a mutant HIV-I infectious clone lacking a signal for N-linked glycosylation in the V1-loop of HIV-1 gp120. Lack of an N-linked glycan was verified by a mobility enhancement of mutant gp120 in SDS-gel electrophoresis. The mutated virus showed no differences in either gp120content per infectious unit or infectivity, indicating that the N-linked glycan was neither essential nor affecting viral infectivity in cell culture. We found that the mutated virus lacking an N-linked glycanin the V1-loop of gp120 was more resistant to neutralization by monoclonal antibodies to the V3-loop and neutralization by soluble recombinant CD4 (sCD4). Both viruses were equally well neutralized by ConA anda conformation dependent human antibody IAM-2G12. This suggests that the N-linked glycan in the V1-loop modulates the three-dimensional conformation of gp120, without changing the overall functional integrity of the molecule.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 14:28:43