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- W2034773500 abstract "The publisher regrets that the authors of this paper were inadvertently printed in the incorrect order. The complete article is reproduced on the following pages. Understanding the antibody response in HIV-1 infection is important to vaccine design. We have studied the antibody response to HIV-1 envelope at the molecular level and determined the characteristics of neutralizing and non-neutralizing antibodies. These antibodies were isolated from phage display libraries prepared from long-term seropositive asymptomatic individuals. The HIV-1 envelope is presented to the immune system in several antigenically distinct configurations: unprocessed gp160, gp120 and gp41 subunits and native envelope, each of which may be important in eliciting an antibody response in HIV-1 infection. The antibodies tested characteristically had poor affinities for native envelope as expressed on the surface of virions or infected cells, but had high affinities against non-native forms of HIV-1 envelope (viral debris). An exceptionally potent neutralizing antibody in contrast, bound native envelope with equivalent or somewhat higher affinity than this. This indicates that the antibody response in HIV-1 infection is principally elicited by viral debris rather than virions, and that these antibodies bind and neutralize viruses sub-optimally. Potential vaccines should be designed to elicit responses against native envelope." @default.
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- W2034773500 date "1997-07-01" @default.
- W2034773500 modified "2023-09-28" @default.
- W2034773500 title "Erratum to “Relevance of the antibody response against human immunodeficiency virus type 1 envelope to vaccine design” [Immunol. Lett. 57 (1997) 105–112]" @default.
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- W2034773500 doi "https://doi.org/10.1016/s0165-2478(97)00109-0" @default.
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