Evidence map›Paper›PMID 31028779›Full record

ReviewJournal of molecular biology2019

Protein and Glycan Mimicry in HIV Vaccine Design.

Gemma E Seabright, Katie J Doores, Dennis R Burton, Max Crispin

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 115 citations in OpenAlex.

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16 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

Gemma E SeabrightOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK; School of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK.
Katie J DooresDepartment of Infectious Diseases, King's College London, Guy's Hospital, London, SE1 9RT, UK.
Dennis R BurtonDepartment of Immunology and Microbiology, the Scripps Centre for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVI-ID), International AIDS Vaccine Initiative Neutralizing Antibody Centre, Scripps Research, La Jolla, CA 92037, USA.
Max CrispinSchool of Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK; Department of Immunology and Microbiology, the Scripps Centre for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVI-ID), International AIDS Vaccine Initiative Neutralizing Antibody Centre, Scripps Research, La Jolla, CA 92037, USA. Electronic address: max.crispin@soton.ac.uk.
University of Southampton · GBGuy's Hospital · GBInternational AIDS Vaccine Initiative · US

Funding

Support Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BAROUCH, DAN H. · 2012 to 2018
$131.5M
Medical Research Council MR/K024426/1NIAID NIH HHS UM1 AI100663
6 · The paper itself

Abstract

Antigenic mimicry is a fundamental tenet of structure-based vaccinology. Vaccine strategies for the human immunodeficiency virus type 1 (HIV-1) focus on the mimicry of its envelope spike (Env) due to its exposed location on the viral membrane and role in mediating infection. However, the virus has evolved to minimize the immunogenicity of conserved epitopes on the envelope spike. This principle is starkly illustrated by the presence of an extensive array of host-derived glycans, which act to shield the underlying protein from antibody recognition. Despite these hurdles, a subset of HIV-infected individuals eventually develop broadly neutralizing antibodies that recognize these virally presented glycans. Effective HIV-1 immunogens are therefore likely to involve some degree of mimicry of both the protein and glycan components of Env. As such, considerable efforts have been made to characterize the structure of the envelope spike and its glycan shield. This review summarizes the recent progress made in this field, with an emphasis on our growing understanding of the factors shaping the glycan shield of Env derived from both virus and soluble immunogens. We argue that recombinant mimics of the envelope spike are currently capable of capturing many features of the native viral glycan shield. Finally, we explore strategies through which the immunogenicity of Env glycans may be enhanced in the development of future immunogens.

Indexed as

AIDS VaccinesAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusEpitopesHIV-1HIV InfectionsHumansModels, MolecularMolecular MimicryPolysaccharidesAIDS VaccinesAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusEpitopesPolysaccharidesantibodiesglycosylationhuman immunodeficiency virusstructurevaccinology

Identifiers

PMID31028779
PMCPMC6556556
OpenAlexW2942255206

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.