Glycosylation Site-Specific Analysis of Clade C HIV-1 Envelope Proteins
نویسندگان
چکیده
منابع مشابه
Global site-specific N-glycosylation analysis of HIV envelope glycoprotein
HIV-1 envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs) and the focus for design of an antibody-based HIV vaccine. The Env trimer is covered by ∼90N-linked glycans, which shield the underlying protein from immune surveillance. bNAbs to HIV develop during infection, with many showing dependence on glycans for binding to Env. The ability to routinely asses...
متن کاملComparative Immunogenicity of HIV-1 Clade C Envelope Proteins for Prime/Boost Studies
BACKGROUND Previous clinical efficacy trials failed to support the continued development of recombinant gp120 (rgp120) as a candidate HIV vaccine. However, the recent RV144 HIV vaccine trial in Thailand showed that a prime/boost immunization strategy involving priming with canarypox vCP1521 followed by boosting with rgp120 could provide significant, although modest, protection from HIV infectio...
متن کاملSite-specific O-Glycosylation Analysis of Human Blood Plasma Proteins*
Site-specific glycosylation analysis is key to investigate structure-function relationships of glycoproteins, e.g. in the context of antigenicity and disease progression. The analysis, though, is quite challenging and time consuming, in particular for O-glycosylated proteins. In consequence, despite their clinical and biopharmaceutical importance, many human blood plasma glycoproteins have not ...
متن کاملStructural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers.
A highly glycosylated, trimeric envelope glycoprotein (Env) mediates HIV-1 cell entry. The high density and heterogeneity of the glycans shield Env from recognition by the immune system, but paradoxically, many potent broadly neutralizing antibodies (bNAbs) recognize epitopes involving this glycan shield. To better understand Env glycosylation and its role in bNAb recognition, we characterized ...
متن کاملDifferential glycosylation of envelope gp120 affects reactivity with HIV-1 specific antibodies
Introduction Cellular entry of human immunodeficiency virus type 1 (HIV-1) depends on envelope glycoprotein (gp120/gp41) interactions with host-cell receptors. Approximately onehalf of molecular mass of gp120 consists of N-glycans which may act as antigenic determinants as well as a shield against immune recognition. We have shown that glycosylation of subtype B HIV-1 gp120 varies according to ...
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ژورنال
عنوان ژورنال: Journal of Proteome Research
سال: 2009
ISSN: 1535-3893,1535-3907
DOI: 10.1021/pr9002728