Evidence map›Paper›PMID 26251831›Full record

ArticleEmerging microbes & infections2015

Structural analysis of a novel rabbit monoclonal antibody R53 targeting an epitope in HIV-1 gp120 C4 region critical for receptor and co-receptor binding.

Ruimin Pan, Yuxin Chen, Michael Vaine, Guangnan Hu, Shixia Wang, Shan Lu, Xiang-Peng Kong

Open access · goldAbstract read
In one paragraph

Article in Emerging microbes & infections, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 32 citations in OpenAlex.

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  8. The wide utility of rabbits as models of human diseases.Experimental & molecular medicine · 2018
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Ruimin PanDepartments of Biochemistry and Molecular Pharmacology, New York University School of Medicine , New York, NY 10016, USA.
Yuxin ChenDepartment of Medicine, University of Massachusetts Medical School , Worcester, MA 01605, USA.
Michael VaineDepartment of Medicine, University of Massachusetts Medical School , Worcester, MA 01605, USA.
Guangnan HuDepartment of Medicine, University of Massachusetts Medical School , Worcester, MA 01605, USA.
Shixia WangDepartment of Medicine, University of Massachusetts Medical School , Worcester, MA 01605, USA.
Shan LuDepartment of Medicine, University of Massachusetts Medical School , Worcester, MA 01605, USA.
Xiang-Peng KongDepartments of Biochemistry and Molecular Pharmacology, New York University School of Medicine , New York, NY 10016, USA.
University of Massachusetts Chan Medical School · USNew York University · US

Funding

Optimizing the immunogenicity of next generation polyvalent HIV vaccine formulatiU19AI082676 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LU, SHAN · 2009 to 2016
$15.8M
Vaccines to Induce Functional Antibodies Targeting the V2 Loop P01AI100151 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI GORNY, MIROSLAW K · 2012 to 2017
$15.4M
Variation in HIV-1 R5 Envs: Consequences for tropism, neutralization & vaccinesP01AI082274 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LU, SHAN · 2009 to 2013
$9.7M
Polyvalent DNA Plus Protein HIV VaccinesR01AI065250 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LU, SHAN · 2006 to 2010
$1.9M
NCI NIH HHS Y1-CO-1020NIAID NIH HHS AI065250NIAID NIH HHS AI082274NIAID NIH HHS AI082676NIAID NIH HHS AI100151NIAID NIH HHS P01 AI082274NIAID NIH HHS P01 AI100151NIAID NIH HHS R01 AI065250NIAID NIH HHS U19 AI082676NIGMS NIH HHS N0GM-0080NIGMS NIH HHS Y01 GM000080NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The fourth conserved region (C4) in the HIV-1 envelope glycoprotein (Env) gp120 is a structural element that is important for its function, as it binds to both the receptor CD4 and the co-receptor CCR5/CXCR4. It has long been known that this region is highly immunogenic and that it harbors B-cell as well as T-cell epitopes. It is the target of a number of antibodies in animal studies, which are called CD4-blockers. However, the mechanism by which the virus shields itself from such antibody responses is not known. Here, we determined the crystal structure of R53 in complex with its epitope peptide using a novel anti-C4 rabbit monoclonal antibody R53. Our data show that although the epitope of R53 covers a highly conserved sequence (433)AMYAPPI(439), it is not available in the gp120 trimer and in the CD4-bound conformation. Our results suggest a masking mechanism to explain how HIV-1 protects this critical region from the human immune system.

Indexed as

AnimalsAntibodies, MonoclonalBinding, CompetitiveBinding Sites, AntibodyCD4 AntigensCrystallizationEpitopesHIV Envelope Protein gp120Immunoglobulin Fab FragmentsRabbitsReceptors, CCR5Receptors, CXCR4SheepAntibodies, MonoclonalCD4 AntigensEpitopesgp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120Immunoglobulin Fab FragmentsReceptors, CCR5Receptors, CXCR4C4CD4EnvHIV-1monoclonal antibody

Identifiers

PMID26251831
PMCPMC4522616
OpenAlexW1494602561

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.