Differential glycosylation of envelope gp120 affects reactivity with HIV-1 specific antibodies
نویسندگان
چکیده
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 the producing cell type and the differential glycosylation affects reactivities with serum antibodies of persons infected with HIV-1 subtype B. Here we studied reactivities of above proteins with panel of monoclonal gp120specific broadly neutralizing antibodies and sera from persons infected with HIV-1 subtype A/C.
منابع مشابه
Glycosylation Patterns of HIV-1 gp120 Depend on the Type of Expressing Cells and Affect Antibody Recognition*
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...
متن کاملDifferential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection
BACKGROUND HIV-1 entry into host cells is mediated by interactions between the virus envelope glycoprotein (gp120/gp41) and host-cell receptors. N-glycans represent approximately 50% of the molecular mass of gp120 and serve as potential antigenic determinants and/or as a shield against immune recognition. We previously reported that N-glycosylation of recombinant gp120 varied, depending on the ...
متن کاملMass Spectrometry Approach and ELISA Reveal the Effect of Codon Optimization on N-Linked Glycosylation of HIV-1 gp120
The genes encoding many viral proteins such as HIV-1 envelope glycoprotein gp120 have a tendency for codons that are poorly used by the human genome. Why these codons are frequently present in the HIV genome is not known. The presence of these codons limits expression of HIV-1 gp120 for biochemical studies. The poor codons are replaced by synonymous codons that are frequently present in the hig...
متن کاملNeutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120.
Amino acid sequences inducing neutralizing antibodies to HIV-1 were sought. Murine monoclonal antibodies (MAbs) were characterized by their reactivity with the envelope precursor gp160 or the Escherichia coli recombinant DNA products pB1 and pE3 representing the carboxy- and amino-terminal halves of mature envelope gp120. Fine mapping of the MAb determinants was performed using defined 15-mer s...
متن کاملMapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding
The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120(SU) plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. Gp120 has remarkably high levels of N-linked glycosylation and there is considerable evidence that this "glycan shield" can help protect the virus from antibody-mediated neutralization. In recent years, ho...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره 14 شماره
صفحات -
تاریخ انتشار 2014