期刊
CELL REPORTS
卷 30, 期 11, 页码 3755-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2020.02.061
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资金
- NIH [R01 AI136621, UM1 AI100663]
- Swiss National Science Foundation [P300PB_160969, P3P3PB_160970]
- NIH F31 Ruth L. Kirschstein Predoctoral Award [Al131873]
- Achievement Rewards for College Scientists Foundation
- Swiss National Science Foundation (SNF) [P300PB_160969, P3P3PB_160970] Funding Source: Swiss National Science Foundation (SNF)
Rational immunogen design aims to focus antibody responses to vulnerable sites on primary antigens. Given the size of these antigens, there is, however, potential for eliciting unwanted, off-target responses. Here, we use our electron microscopy polyclonal epitope mapping approach to describe the antibody specificities elicited by immunization of non-human primates with soluble HIV envelope trimers and subsequent repeated viral challenge. An increased diversity of epitopes recognized and the approach angle by which these antibodies bind constitute a hallmark of the humoral response in most protected animals. We also show that fusion peptide-specific antibodies are likely responsible for some neutralization breadth. Moreover, cryoelectron microscopy (cryo-EM) analysis of a fully protected animal reveals a high degree of clonality within a subset of putatively neutralizing antibodies, enabling a detailed molecular description of the antibody paratope. Our results provide important insights into the immune response against a vaccine candidate that entered into clinical trials in 2019.
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