PDBsum entry 6v0r

Viral protein

PDB id: 6v0r

Contents

Protein chains

439 a.a.

129 a.a.

Ligands

NAG-NAG ×12

NAG-NAG-BMA-MAN-MAN-MAN ×3

NAG-NAG-BMA ×6

NAG-NAG-FUC ×3

NAG-FUC ×3

NAG ×33

PDB id:

6v0r

Name:

Viral protein

Title:

Bg505 sosip.664 trimer

Structure:

Bg505 sosipv5.2 gp120. Chain: a, c, d. Fragment: unp residues 30-504. Synonym: env polyprotein. Engineered: yes. Bg505 sosipv5.2 gp41. Chain: b, e, f. Fragment: unp residues 509-661. Synonym: env polyprotein.

Source:

Human immunodeficiency virus 1. HIV-1. Organism_taxid: 11676. Gene: env. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293f. Expression_system_cell_line: hek293f

Authors:

B.Nogal,C.A.Cottrell,A.B.Ward

Key ref:

B.Nogal et al. (2020). Mapping Polyclonal Antibody Responses in Non-human Primates Vaccinated with HIV Env Trimer Subunit Vaccines. Cell Rep, 30, 3755. PubMed id: 32187547 DOI: 10.1016/j.celrep.2020.02.061

Date:

19-Nov-19 Release date: 01-Apr-20

Protein chains

Q2N0S6  (Q2N0S6_HV1) -  Envelope glycoprotein gp160 from Human immunodeficiency virus type 1

Seq: 860 a.a.

Struc: 439 a.a.*

Protein chains

Q2N0S6  (Q2N0S6_HV1) -  Envelope glycoprotein gp160 from Human immunodeficiency virus type 1

Seq: 860 a.a.

Struc: 129 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1016/j.celrep.2020.02.061

Cell Rep 30:3755 (2020)

PubMed id: 32187547

Mapping Polyclonal Antibody Responses in Non-human Primates Vaccinated with HIV Env Trimer Subunit Vaccines.

B.Nogal, M.Bianchi, C.A.Cottrell, R.N.Kirchdoerfer, L.M.Sewall, H.L.Turner, F.Zhao, D.Sok, D.R.Burton, L.Hangartner, A.B.Ward.

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.