期刊
JOURNAL OF VIROLOGY
卷 80, 期 22, 页码 11404-11408出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01102-06
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资金
- NIAID NIH HHS [AI24755, R01 AI039420, P30 AI042848, R21 AI064009, U19 AI067854, AI42848, AI40895, AI39420, R01 AI040895, U01 AI067854, R37 AI024755, AI064009, AI67854] Funding Source: Medline
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.
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