Evidence map›Paper›PMID 40702326›Full record

ReviewNature reviews. Microbiology2025

The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodies.

P J Klasse, Rogier W Sanders, Andrew B Ward, Ian A Wilson, John P Moore

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

21 citing papers in PubMed, 1 synthesis or guideline pooled it.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

P J KlasseDepartment of Microbiology and Immunology, Weill Cornell Medicine, Cornell University, New York, NY, USA. pek2003@med.cornell.edu.ORCID http://orcid.org/0000-0001-8222-278X
Rogier W SandersDepartment of Microbiology and Immunology, Weill Cornell Medicine, Cornell University, New York, NY, USA.
Andrew B WardDepartment of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, CA, USA.ORCID http://orcid.org/0000-0001-7153-3769
Ian A WilsonDepartment of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, CA, USA.ORCID http://orcid.org/0000-0002-6469-2419
John P MooreDepartment of Microbiology and Immunology, Weill Cornell Medicine, Cornell University, New York, NY, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To end the AIDS pandemic, an effective vaccine is sought to prevent new infections by inducing broadly active HIV-1 neutralizing antibodies. Monoclonal neutralizing antibodies can be administered therapeutically to people living with HIV-1 and preventively to those who are uninfected and at risk. Neutralizing antibodies block viral entry into susceptible cells by targeting the HIV-1 envelope glycoprotein, which mediates entry by membrane fusion. The envelope glycoprotein evades neutralizing antibody responses by multiple means, including extreme sequence variation and a dense protective glycan shield. Despite these impediments, many broadly active neutralizing human antibodies have been isolated, typically after years of HIV-1 infection. In this Review, we describe how such antibodies target distinct epitope clusters that cumulatively now cover most of the external surface of the envelope glycoprotein. These antibodies vary in potency, in the degree to which they reduce infectivity, in mechanism of action, and in structural basis, affinity and kinetics of binding. Broadly neutralizing antibody responses have, however, so far not been elicited by immunization with envelope glycoproteins. That situation may change though with the rapid advancement of structure-guided immunogen design strategies that engage germline versions of human antibodies and guide their maturation towards greater neutralization potency and breadth.

Indexed as

Antibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV-1HIV AntibodiesHIV InfectionsAIDS VaccinesAntibodies, MonoclonalEpitopesHumansAIDS VaccinesAntibodies, MonoclonalAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusEpitopesHIV Antibodies

Identifiers

PMID40702326

What OpenQuestion holds

Textmetadata
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.