Evidence map›Paper›PMID 31231397›Full record

ReviewFrontiers in immunology2019

Conceptual Approaches to Modulating Antibody Effector Functions and Circulation Half-Life.

Kevin O Saunders

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 214 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
214citing papers in PubMed, 1 pooled it
29.7field-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

214 citing papers in PubMed, 1 synthesis or guideline pooled it, 313 citations in OpenAlex.

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154 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

1 author at 1 institution in 1 country.

Kevin O SaundersLaboratory of Protein Expression, Departments of Surgery, Molecular Genetics and Microbiology, and Immunology, Duke University Medical Center, Duke Human Vaccine Institute, Durham, NC, United States.
Protein Express (United States) · US

Funding

Physical Resources CoreP01AI120756 · NIAID · DUKE UNIVERSITY · PI TOMARAS, GEORGIA DORIS · 2016 to 2020
$17.1M
HIV-1 vaccine-elicited antibodies target envelope glycansR01AI120801 · NIAID · DUKE UNIVERSITY · PI SAUNDERS, KEVIN O · 2015 to 2024
$7.5M
NIAID NIH HHS P01 AI120756NIAID NIH HHS R01 AI120801
6 · The paper itself

Abstract

Antibodies and Fc-fusion antibody-like proteins have become successful biologics developed for cancer treatment, passive immunity against infection, addiction, and autoimmune diseases. In general these biopharmaceuticals can be used for blocking protein:protein interactions, crosslinking host receptors to induce signaling, recruiting effector cells to targets, and fixing complement. With the vast capability of antibodies to affect infectious and genetic diseases much effort has been placed on improving and tailoring antibodies for specific functions. While antibody:antigen engagement is critical for an efficacious antibody biologic, equally as important are the hinge and constant domains of the heavy chain. It is the hinge and constant domains of the antibody that engage host receptors or complement protein to mediate a myriad of effector functions and regulate antibody circulation. Molecular and structural studies have provided insight into how the hinge and constant domains from antibodies across different species, isotypes, subclasses, and alleles are recognized by host cell receptors and complement protein C1q. The molecular details of these interactions have led to manipulation of the sequences and glycosylation of hinge and constant domains to enhance or reduce antibody effector functions and circulating half-life. This review will describe the concepts being applied to optimize the hinge and crystallizable fragment of antibodies, and it will detail how these interactions can be tuned up or down to mediate a biological function that confers a desired disease outcome.

Indexed as

AnimalsAntibodies, MonoclonalHalf-LifeHumansImmunoglobulin Heavy ChainsImmunotherapyProtein EngineeringProtein StabilityAntibodies, MonoclonalImmunoglobulin Heavy Chainsantibody engineeringbiologicsFc optimizationimmunotherapypassive immunitytherapeutic antibodies

Identifiers

PMID31231397
PMCPMC6568213
OpenAlexW2969038446

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.