Effects of mutations on HIV‐1 infectivity and neutralization involving the conserved NNNT amino acid sequence in the gp120 V3 loop | Zendy

Polzer Svenja | Zendy; Müller Harm | Zendy; Schreiber Michael | Zendy

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Effects of mutations on HIV‐1 infectivity and neutralization involving the conserved NNNT amino acid sequence in the gp120 V3 loop

Author(s) -

Polzer Svenja,

Müller Harm,

Schreiber Michael

Publication year - 2009

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2009.03.010

Subject(s) - neutralization , virology , infectivity , v3 loop , antibody , heterologous , biology , mutation , glycan , neutralizing antibody , peptide sequence , glycosylation , sequence (biology) , virus , glycoprotein , microbiology and biotechnology , genetics , gene , epitope

The N‐glycan g15 within the HIV‐1 gp120 V3 loop efficiently blocks antibodies to facilitate viral escape from humoral immune responses. However, we have isolated primary viruses all lacking the N‐glycosylation site g15 due to mutations (NNNT > YRNA, HNTV, SIQK), which showed resistance to neutralizing antibodies present in autologous or heterologous HIV‐1 positive sera. When introduced into the NL4‐3 background, the sequences YRNA, HNTV and SIQK caused an increase of viral infectivity and resistance to neutralization. Thus, despite the lack of g15, primary isolates can escape from neutralization because of specific mutations of the NNNT sequence altering coreceptor usage.

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