Evidence map›Paper›PMID 36536068›Full record

ReviewNature reviews. Immunology2023

Beyond neutralization: Fc-dependent antibody effector functions in SARS-CoV-2 infection.

Ali Zhang, Hannah D Stacey, Michael R D'Agostino, Yona Tugg, Art Marzok, Matthew S Miller

Open access · bronzeAbstract readReview
In one paragraph

Review in Nature reviews. Immunology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed, 1 pooled it
19.6field-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

145 citing papers in PubMed, 1 synthesis or guideline pooled it, 203 citations in OpenAlex.

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  11. Proceedings of the National Academy of Sciences of the United States of America · 2026
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85 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

6 authors at 1 institution in 1 country.

Ali ZhangMichael G. DeGroote Institute for Infectious Disease Research, McMaster Immunology Research Centre, Department of Biochemistry & Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Hannah D StaceyMichael G. DeGroote Institute for Infectious Disease Research, McMaster Immunology Research Centre, Department of Biochemistry & Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Michael R D'AgostinoMichael G. DeGroote Institute for Infectious Disease Research, McMaster Immunology Research Centre, Department of Biochemistry & Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Yona TuggMichael G. DeGroote Institute for Infectious Disease Research, McMaster Immunology Research Centre, Department of Biochemistry & Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Art MarzokMichael G. DeGroote Institute for Infectious Disease Research, McMaster Immunology Research Centre, Department of Biochemistry & Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Matthew S MillerMichael G. DeGroote Institute for Infectious Disease Research, McMaster Immunology Research Centre, Department of Biochemistry & Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada. mmiller@mcmaster.ca.ORCID 0000-0003-3426-5069
McMaster University Medical Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neutralizing antibodies are known to have a crucial role in protecting against SARS-CoV-2 infection and have been suggested to be a useful correlate of protection for vaccine clinical trials and for population-level surveys. In addition to neutralizing virus directly, antibodies can also engage immune effectors through their Fc domains, including Fc receptor-expressing immune cells and complement. The outcome of these interactions depends on a range of factors, including antibody isotype-Fc receptor combinations, Fc receptor-bearing cell types and antibody post-translational modifications. A growing body of evidence has shown roles for these Fc-dependent antibody effector functions in determining the outcome of SARS-CoV-2 infection. However, measuring these functions is more complicated than assays that measure antibody binding and virus neutralization. Here, we examine recent data illuminating the roles of Fc-dependent antibody effector functions in the context of SARS-CoV-2 infection, and we discuss the implications of these data for the development of next-generation SARS-CoV-2 vaccines and therapeutics.

Indexed as

COVID-19Antibodies, NeutralizingAntibodies, ViralCOVID-19 VaccinesHumansImmunoglobulin Fc FragmentsReceptors, FcSARS-CoV-2Antibodies, NeutralizingAntibodies, ViralCOVID-19 VaccinesImmunoglobulin Fc FragmentsReceptors, Fc

Identifiers

PMID36536068
PMCPMC9761659
OpenAlexW4312067520

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.