Evidence map›Paper›PMID 33283275›Full record

ArticleImmunology2021

IgA binds to the AD-2 epitope of glycoprotein B and neutralizes human cytomegalovirus.

Saima Siddiqui, Sarah Hackl, Hamid Ghoddusi, Megan R McIntosh, Ariane C Gomes, Joshua Ho, Matthew B Reeves, Gary R McLean

Open access · hybridAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Saima SiddiquiCellular and Molecular Immunology Research Centre, London Metropolitan University, London, UK.
Sarah HacklCellular and Molecular Immunology Research Centre, London Metropolitan University, London, UK.
Hamid GhoddusiMicrobiology Research Unit, London Metropolitan University, London, UK.
Megan R McIntoshInstitute for Immunity and Transplantation, University College London, London, UK.
Ariane C GomesInstitute for Immunity and Transplantation, University College London, London, UK.
Joshua HoInstitute for Immunity and Transplantation, University College London, London, UK.
Matthew B ReevesInstitute for Immunity and Transplantation, University College London, London, UK.
Gary R McLeanCellular and Molecular Immunology Research Centre, London Metropolitan University, London, UK.ORCID 0000-0002-1278-1743
London Metropolitan University · GBUniversity College London · GB

Funding

Wellcome Trust 204870/Z/16/Z
6 · The paper itself

Abstract

Human cytomegalovirus (HCMV) is a ubiquitous pathogen that is potentially pathogenic in immunosuppressed individuals and pregnant females during primary infection. The HCMV envelope glycoprotein B (gB) facilitates viral entry into all cell types and induces a potent immune response. AD-2 epitope is a highly conserved linear neutralizing epitope of gB and a critical target for antibodies; however, only 50% of sero-positive individuals make IgG antibodies to this site and IgA responses have not been fully investigated. This study aimed to compare IgG and IgA responses against gB and the AD-2 epitope in naturally exposed individuals and those receiving a recombinant gB/MF59 adjuvant vaccine. Thus, vaccination of sero-positive individuals improved pre-existing gB-specific IgA and IgG levels and induced de novo gB-specific IgA and IgG responses in sero-negative recipients. Pre-existing AD-2 IgG and IgA responses were boosted with vaccination, but de novo AD-2 responses were not detected. Naturally exposed individuals had dominant IgG responses towards gB and AD-2 compared with weaker and variable IgA responses, although a significant IgA binding response to AD-2 was observed within human breastmilk samples. All antibodies binding AD-2 contained kappa light chains, whereas balanced kappa/lambda light chain usage was found for those binding to gB. V region-matched AD-2-specific recombinant IgG and IgA bound both to gB and to AD-2 and neutralized HCMV infection in vitro. Overall, these results indicate that although human IgG responses dominate, IgA class antibodies against AD-2 are a significant component of human milk, which may function to protect neonates from HCMV.

Indexed as

EpitopesImmunogenicity, VaccineAdjuvants, ImmunologicAnimalsAntibodies, NeutralizingAntibodies, ViralAntibody SpecificityBinding Sites, AntibodyCell Line, TumorCytomegalovirusCytomegalovirus InfectionsHEK293 CellsHumansImmunoglobulin AImmunoglobulin GMiceAdjuvants, ImmunologicAntibodies, NeutralizingAntibodies, ViralEpitopesglycoprotein B, SimplexvirusImmunoglobulin AImmunoglobulin GMF59 oil emulsionPolysorbatesSqualeneViral Envelope ProteinsViral VaccinesAD-2 epitopeglycoprotein Bhuman cytomegalovirusimmunoglobulin A

Identifiers

PMID33283275
PMCPMC7884650
OpenAlexW3109455234

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.