Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition

. 2010 Jul 02 ; 285 (27) : 20860-9. [epub] 20100503

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid20439465

Grantová podpora
U01 AI067854 NIAID NIH HHS - United States
U01 AI028147 NIAID NIH HHS - United States
DK054495 NIDDK NIH HHS - United States
R24 DK064400 NIDDK NIH HHS - United States
RR-20136 NCRR NIH HHS - United States
P01 AI071739 NIAID NIH HHS - United States
U19 AI028147 NIAID NIH HHS - United States
R01 DK047322 NIDDK NIH HHS - United States
T35 HL007473 NHLBI NIH HHS - United States
P01 AI083027 NIAID NIH HHS - United States
AI071739 NIAID NIH HHS - United States
R01 GM098539 NIGMS NIH HHS - United States
AI083027 NIAID NIH HHS - United States
R21 AI078477 NIAID NIH HHS - United States
AI078477 NIAID NIH HHS - United States
C06 RR020136 NCRR NIH HHS - United States
AI067854 NIAID NIH HHS - United States
R01 DK054495 NIDDK NIH HHS - United States
DK047322 NIDDK NIH HHS - United States
P01 AI028147 NIAID NIH HHS - United States
U19 AI067854 NIAID NIH HHS - United States

Odkazy

PubMed 20439465
PubMed Central PMC2898351
DOI 10.1074/jbc.m109.085472
PII: S0021-9258(20)57373-0
Knihovny.cz E-zdroje

Human immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design.

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