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Titolo:
DEMONSTRATION OF PERIPHERAL FUCOSE UNITS IN N-LINKED GLYCANS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GP-120 - EFFECTS ON GLYCOPROTEIN CONFORMATION
Autore:
BOLMSTEDT A; BILLER M; HANSEN JES; MOORE JP; OLOFSSON S;
Indirizzi:
GOTHENBURG UNIV,DEPT CLIN VIROL,GULDHEDSGATAN 10B S-41346 GOTHENBURG SWEDEN GOTHENBURG UNIV,DEPT CLIN VIROL S-41346 GOTHENBURG SWEDEN UNIV COPENHAGEN,HVIDOVRE HOSP,DIV INFECT DIS DK-2650 HVIDOVRE DENMARK NYU,SCH MED,AARON DIAMOND AIDS RES CTR NEW YORK NY 00000
Titolo Testata:
Archives of virology
fascicolo: 12, volume: 142, anno: 1997,
pagine: 2465 - 2481
SICI:
0304-8608(1997)142:12<2465:DOPFUI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN MONOCLONAL-ANTIBODY; HAMSTER OVARY CELLS; ENVELOPE GLYCOPROTEIN; RECOMBINANT GP160; OLIGOSACCHARIDE STRUCTURES; OLIGOMERIC STRUCTURE; DEPENDENT EPITOPES; CD4 BINDING; SOLUBLE CD4; AIDS VIRUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
A. Bolmstedt et al., "DEMONSTRATION OF PERIPHERAL FUCOSE UNITS IN N-LINKED GLYCANS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GP-120 - EFFECTS ON GLYCOPROTEIN CONFORMATION", Archives of virology, 142(12), 1997, pp. 2465-2481

Abstract

Fucosylated N-linked glycans are important constituents of membrane glycoproteins, owing to their significance as biologically active ligands for several selectins and their role in modulating protein conformation of viral glycoproteins. The human immunodeficiency virus type 1 (HIV-1) glycoprotein contains more than 30 different glycan structures but so far fucose was found associated solely with the innermost GlcNAc of N-linked glycans. In the present report we determined whether fucose units also were linked to the distal GlcNAc via alpha(1-3) or alpha(1-4) linkages in N-linked glycans of gp 120. [H-3]-fucose labelled gp 120 was subjected to endoglycosidase F digestion, releasing diantennary complex type N-linked glycans, but leaving the inner polypeptide-bound carbohydrates, GlcNAc and possibly associated fucose units, intact. Gel filtration of the digested material revealed that [H-3]-fucose label was released from gp 120 by this treatment, indicating presence of peripheral fucose units. Furthermore, [H-3]-focuse label was also released by treatment of the labelled gp 120 with an alpha-1-fucosidasespecifically removing fucose in alpha(1-3) and alpha(1-4) linkages. Altogether the results indicated presence of fucose units linked to peripheral GlcNAc of gp 120 N-linked glycans. We have earlier shown that other peripheral carbohydrate determinants, i.e. beta(1-4)galactose onN-linked glycans, maintain a correct antigenic conformation of gp 120. Using a coupled ELISA system, where changes in antigenic behaviour of a viral glycoprotein were correlated to stepwise elimination of peripheral monosaccharides from N-linked glycans, we found that treatment of gp 120 with a pan-specific alpha-fucosidase as well as an enzyme specific for alpha(1-3)- or alpha(1-4)-linked fucose disclosed a hidden linear epitope situated in the gp 120 C2 region. The effects of the general fucosidase on epitope exposure was more prominent than those obtained with the enzyme with narrow specificity, suggesting that peripheral and inner fucose units co-operate in the maintenance of gp 120 conformation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 06:54:52