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6V0R

BG505 SOSIP.664 Trimer

Summary for 6V0R
Entry DOI10.2210/pdb6v0r/pdb
EMDB information20396
DescriptorBG505 SOSIPv5.2 gp120, BG505 SOSIPv5.2 gp41, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsantibody, hiv, glycoprotein, viral protein, polyclonal, non-human primate, rhesus macaque
Biological sourceHuman immunodeficiency virus 1 (HIV-1)
More
Total number of polymer chains6
Total formula weight233285.05
Authors
Nogal, B.,Cottrell, C.A.,Ward, A.B. (deposition date: 2019-11-19, release date: 2020-04-01, Last modification date: 2020-07-29)
Primary citationNogal, B.,Bianchi, M.,Cottrell, C.A.,Kirchdoerfer, R.N.,Sewall, L.M.,Turner, H.L.,Zhao, F.,Sok, D.,Burton, D.R.,Hangartner, L.,Ward, A.B.
Mapping Polyclonal Antibody Responses in Non-human Primates Vaccinated with HIV Env Trimer Subunit Vaccines.
Cell Rep, 30:3755-3765.e7, 2020
Cited by
PubMed Abstract: 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.
PubMed: 32187547
DOI: 10.1016/j.celrep.2020.02.061
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.87 Å)
Structure validation

227344

數據於2024-11-13公開中

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