Evidence map›Paper›PMID 31589168›Full record

ArticleThe Journal of clinical investigation2019

Glycan-dependent HIV-specific neutralizing antibodies bind to cells of uninfected individuals.

Jana Blazkova, Eric W Refsland, Katherine E Clarridge, Victoria Shi, J Shawn Justement, Erin D Huiting, Kathleen R Gittens, Xuejun Chen, Stephen D Schmidt, Cuiping Liu and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 13 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

15 authors at 3 institutions in 1 country.

Jana BlazkovaLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
Eric W RefslandLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
Katherine E ClarridgeLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
Victoria ShiLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
J Shawn JustementLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
Erin D HuitingLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
Kathleen R GittensCritical Care Medicine Department, Clinical Center, and.
Xuejun ChenVaccine Research Center, NIAID, NIH, Bethesda, Maryland, USA.
Stephen D SchmidtVaccine Research Center, NIAID, NIH, Bethesda, Maryland, USA.
Cuiping LiuVaccine Research Center, NIAID, NIH, Bethesda, Maryland, USA.
Nicole Doria-RoseVaccine Research Center, NIAID, NIH, Bethesda, Maryland, USA.
John R MascolaVaccine Research Center, NIAID, NIH, Bethesda, Maryland, USA.
Alonso HerediaInstitute of Human Virology, University of Maryland, Baltimore, Maryland, USA.
Susan MoirLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
Tae-Wook ChunLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases (NIAID).
National Institute of Allergy and Infectious Diseases · USCenter for Clinical Research (United States) · USUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of highly potent and broadly neutralizing antibodies (bNAbs) against the human immunodeficiency virus (HIV) have recently been shown to prevent transmission of the virus, suppress viral replication, and delay plasma viral rebound following discontinuation of antiretroviral therapy in animal models and infected humans. However, the degree and extent to which such bNAbs interact with primary lymphocytes have not been fully delineated. Here, we show that certain glycan-dependent bNAbs, such as PGT121 and PGT151, bind to B, activated T, and natural killer (NK) cells of HIV-infected and -uninfected individuals. Binding of these bNAbs, particularly PGT121 and PGT151, to activated CD4+ and CD8+ T cells was mediated by complex-type glycans and was abrogated by enzymatic inhibition of N-linked glycosylation. In addition, a short-term incubation of PGT151 and primary NK cells led to degranulation and cellular death. Our data suggest that the propensity of certain bNAbs to bind uninfected/bystander cells has the potential for unexpected outcomes in passive-transfer studies and underscore the importance of antibody screening against primary lymphocytes.

Indexed as

Antibody SpecificityAntibodies, NeutralizingCD4-Positive T-LymphocytesCD8-Positive T-LymphocytesFemaleGlucansGlycosylationHIV AntibodiesHumansKiller Cells, NaturalMaleAntibodies, NeutralizingGlucansHIV AntibodiesAIDS/HIVImmunoglobulinsImmunology

Identifiers

PMID31589168
PMCPMC6819136
OpenAlexW2978621704

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.