HIV-1 gp120 dimers decrease the overall affinity of gp120 preparations for CD4-induced ligands

Journal of Virological Methods

Volumn 215-216, Issue , 2015, Pages 37-44

  Coutu, Mathieu ^a,b   Finzi, Andrés ^a,b,c  

^a CENTRE HOSPITALIER DE L UNIVERSITÉ DE MONTRÉAL   (Canada)

^b UNIVERSITÉ DE MONTRÉAL   (Canada)

^c MCGILL UNIVERSITY   (Canada)

Author keywords

CD4 induced epitopes; FPLC; Gp120; Gp120 dimers; HIV; Surface plasmon resonance

Indexed keywords

CD4 ANTIBODY; DIMER; DISULFIDE; GLYCOPROTEIN GP 120; CD4 ANTIGEN; GP120 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTEIN BINDING; RECOMBINANT PROTEIN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; EMBRYO; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOPRECIPITATION; LIGAND BINDING; MAMMAL CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; PROTEIN PURIFICATION; SURFACE PLASMON RESONANCE; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; PROCEDURES; PROTEIN MULTIMERIZATION; SIZE EXCLUSION CHROMATOGRAPHY;

HUMAN IMMUNODEFICIENCY VIRUS 1; MAMMALIA;

ANTIGENS, CD4; CHROMATOGRAPHY, GEL; HIV ENVELOPE PROTEIN GP120; HUMANS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SURFACE PLASMON RESONANCE;

EID: 84924985686     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2015.02.017     Document Type: Article

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