Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization.
Primary and laboratory-adapted variants of human immunodeficiency virus type 1 (HIV-1) exhibit a wide range of sensitivities to neutralization by antibodies directed against the viral envelope glycoproteins. An antibody directed against an artificial FLAG epitope inserted into the envelope glycoproteins of three HIV-1 isolates with vastly different neutralization sensitivities inhibited all three viruses equivalently. Thus, naturally occurring HIV-1 isolates that are neutralization resistant are not necessarily more impervious to the inhibitory consequences of bound antibody. Moreover, the binding affinity of the anti-FLAG antibody correlated with neutralizing potency, underscoring the dominant impact on neutralization of antibody binding to the envelope glycoproteins.
Yang
Xinzhen
X
Beth Israel Deaconess Medical Center, 330 Brookline Avenue, R.E. 213A, Boston, MA 02215, USA. xyang1@bidmc.harvard.edu
Lipchina
Inna
I
Cocklin
Simon
S
Chaiken
Irwin
I
Sodroski
Joseph
J
D000915:Antibody Affinity; D002460:Cell Line; D000939:Epitopes / Q000276:immunology; D017930:Genes, Reporter; D015483:HIV Antibodies / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000276:immunology; D015497:HIV-1 / Q000276:immunology* / Q000502:physiology; D006801:Humans; D008156:Luciferases; D009500:Neutralization Tests; D014779:Virus Replication
D000939:Epitopes; D015483:HIV Antibodies; D015699:HIV Envelope Protein gp120; D008156:Luciferases