Characterization of the antibody response elicited by HIV-1 Env glycomutants in rabbits.
HIV-1 N-glycans are known to shield underlying epitopes towards the protective antibody repertoire. We previously described HIV-1 acute infection Env glycomutants designed from 3D-model in which the removal of clustered N-glycans did not disturb the envelope antigenicity, but increased the neutralization sensitivity. The potential of such immunogens to elicit neutralizing responses was estimated after rabbit immunizations with a DNA/protein protocol. Maturation of the Env-specific antibody response was confirmed by a change in avidity and conformational dependence. For one immunogen, the neutralizing response was increased with a higher breadth compared to the Wild-Type. Our data suggest that Env selective deglycosylation based on 3D data may represent a valuable strategy to improve elicitation of neutralizing antibodies.
Reynard
F
F
FRE 2736, CNRS-bioMerieux, IFR128, CERVI, 21 Avenue Tony Garnier, 69007 Lyon, France.
Willkomm
N
N
Fatmi
A
A
Vallon-Eberhard
A
A
Verrier
B
B
Bedin
F
F
D000818:Animals; D000915:Antibody Affinity / Q000276:immunology; D018791:CD4 Lymphocyte Count; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D006023:Glycoproteins / Q000235:genetics / Q000276:immunology; D015483:HIV Antibodies / Q000032:analysis / Q000096:biosynthesis*; D019302:HIV Envelope Protein gp160 / Q000235:genetics* / Q000276:immunology*; D015497:HIV-1 / Q000235:genetics* / Q000276:immunology*; D007117:Immunization, Secondary; D007074:Immunoglobulin G / Q000096:biosynthesis / Q000235:genetics; D008968:Molecular Conformation; D009500:Neutralization Tests; D010449:Peptide Mapping; D011817:Rabbits; D019444:Vaccines, DNA / Q000276:immunology; D022223:Vaccines, Subunit / Q000276:immunology
D000939:Epitopes; D006023:Glycoproteins; D015483:HIV Antibodies; D019302:HIV Envelope Protein gp160; D007074:Immunoglobulin G; D019444:Vaccines, DNA; D022223:Vaccines, Subunit