Griffithsin Retains Anti-HIV-1 Potency with Changes in gp120 Glycosylation and Complements Broadly Neutralizing Antibodies PGT121 and PGT126 | Zendy

Kathryn Fischer | Zendy; Kimberly Nguyen | Zendy; Patricia J. LiWang | Zendy

Open Access

Griffithsin Retains Anti-HIV-1 Potency with Changes in gp120 Glycosylation and Complements Broadly Neutralizing Antibodies PGT121 and PGT126

Author(s) -

Kathryn Fischer,

Kimberly Nguyen,

Patricia J. LiWang

Publication year - 2019

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01084-19

Subject(s) - glycosylation , glycan , potency , antibody , neutralization , neutralizing antibody , glycoprotein , virology , mannose , biology , entry inhibitor , lectin , chemistry , immunology , microbiology and biotechnology , biochemistry , viral entry , virus , in vitro , viral replication

Griffithsin (Grft) is an antiviral lectin that has been shown to potently inhibit HIV-1 by binding high-mannose N-linked glycosylation sites on HIV-1 gp120. A key factor for Grft potency is glycosylation at N295 of gp120, which is directly adjacent to N332, a target glycan for an entire class of broadly neutralizing antibodies (bNAbs).

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