Evidence map›Paper›PMID 28133801›Full record

ReviewImmunological reviews2017

Anti-retroviral antibody FcγR-mediated effector functions.

Stylianos Bournazos, Jeffrey V Ravetch

Open access · greenAbstract readReview
In one paragraph

Review in Immunological reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 55 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

2 authors at 1 institution in 1 country.

Stylianos BournazosThe Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY, USA.
Jeffrey V RavetchThe Laboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY, USA.
Rockefeller University · US

Funding

Stuctural basis of bNab activityP01AI100148 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Pamela J Bjorkman · 2013 to 2026
$43.3M
MOLECULAR ASPECTS OF ANTITUMOR ANTIBODIESR01CA080757 · NCI · ROCKEFELLER UNIVERSITY · PI RAVETCH, JEFFREY VICTOR · 1999 to 2015
$5.2M
Study of FcR Genes: Macrophages and LymphocytesR56AI034662 · NIAID · ROCKEFELLER UNIVERSITY · PI RAVETCH, JEFFREY VICTOR · 2013 to 2013
$418k
NCI NIH HHS R01 CA080757NIAID NIH HHS P01 AI100148NIAID NIH HHS R56 AI034662
6 · The paper itself

Abstract

The antiviral activity of antibodies reflects the bifunctional properties of these molecules. While the Fab domains mediate highly specific antigenic recognition to block virus entry, the Fc domain interacts with diverse types of Fcγ receptors (FcγRs) expressed on the surface of effector leukocytes to induce the activation of distinct immunomodulatory pathways. Fc-FcγR interactions are tightly regulated to control IgG-mediated inflammation and immunity and are largely determined by the structural heterogeneity of the IgG Fc domain, stemming from differences in the primary amino acid sequence of the various subclasses, as well as the structure and composition of the Fc-associated N-linked glycan. Engagement of specific FcγR types on effector leukocytes has diverse consequences that affect several aspects of innate and adaptive immunity. In this review, we provide an overview of the complexity of FcγR-mediated pathways, discussing their role in the in vivo protective activity of anti-HIV-1 antibodies. We focus on recent studies on broadly neutralizing anti-HIV-1 antibodies that revealed that Fc-FcγR interactions are required to achieve full therapeutic activity through clearance of IgG-opsonized virions and elimination of HIV-infected cells. Manipulation of Fc-FcγR interactions to specifically activate distinct FcγR-mediated pathways has the potential to affect downstream effector responses, influencing thereby the in vivo protective activity of anti-HIV-1 antibodies; a strategy that has already been successfully applied to other IgG-based therapeutics, substantially improving their clinical efficacy.

Indexed as

AnimalsAntibodies, NeutralizingHIV-1HIV AntibodiesHIV InfectionsHumansImmunoglobulin Fab FragmentsImmunomodulationImmunotherapyPhagocytosisReceptors, IgGViral LoadAntibodies, NeutralizingHIV AntibodiesImmunoglobulin Fab FragmentsReceptors, IgGAIDSantibodiescytotoxicityFc receptorsimmunotherapiesinflammation

Identifiers

PMID28133801
PMCPMC7379163
OpenAlexW2580378056

What OpenQuestion holds

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LicenceTDM
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.