Evidence map›Paper›PMID 24604090›Full record

ArticlePLoS pathogens2014

The herpes virus Fc receptor gE-gI mediates antibody bipolar bridging to clear viral antigens from the cell surface.

Blaise Ndjamen, Alexander H Farley, Terri Lee, Scott E Fraser, Pamela J Bjorkman

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 42 citations in OpenAlex.

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  15. Alphaherpesvirus Vaccines.Current issues in molecular biology · 2021
    Review
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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

5 authors at 2 institutions in 1 country.

Blaise NdjamenDivision of Biology and Biochemical Engineering, California Institute of Technology, Pasadena, California, United States of America.
Alexander H FarleyDivision of Biology and Biochemical Engineering, California Institute of Technology, Pasadena, California, United States of America.
Terri LeeDivision of Biology and Biochemical Engineering, California Institute of Technology, Pasadena, California, United States of America.
Scott E FraserDivision of Biology and Biochemical Engineering, California Institute of Technology, Pasadena, California, United States of America.
Pamela J BjorkmanDivision of Biology and Biochemical Engineering, California Institute of Technology, Pasadena, California, United States of America; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California, United States of America.
California Institute of Technology · USHoward Hughes Medical Institute · US

Funding

Analysis of the Neonatal Fc Receptor/IgG InteractionR37AI041239 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 2004 to 2013
$3.7M
NEONATAL FC RECEPTOR/IGG INTERACTIONR01AI041239 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI BJORKMAN, PAMELA J · 1997 to 2018
$2.3M
Howard Hughes Medical InstituteNIAID NIH HHS 5R37 AI041239-15NIAID NIH HHS R01 AI041239NIAID NIH HHS R37 AI041239
6 · The paper itself

Abstract

The Herpes Simplex Virus 1 (HSV-1) glycoprotein gE-gI is a transmembrane Fc receptor found on the surface of infected cells and virions that binds human immunoglobulin G (hIgG). gE-gI can also participate in antibody bipolar bridging (ABB), a process by which the antigen-binding fragments (Fabs) of the IgG bind a viral antigen while the Fc binds to gE-gI. IgG Fc binds gE-gI at basic, but not acidic, pH, suggesting that IgG bound at extracellular pH by cell surface gE-gI would dissociate and be degraded in acidic endosomes/lysosomes if endocytosed. The fate of viral antigens associated with gE-gI-bound IgG had been unknown: they could remain at the cell surface or be endocytosed with IgG. Here, we developed an in vitro model system for ABB and investigated the trafficking of ABB complexes using 4-D confocal fluorescence imaging of ABB complexes with transferrin or epidermal growth factor, well-characterized intracellular trafficking markers. Our data showed that cells expressing gE-gI and the viral antigen HSV-1 gD endocytosed anti-gD IgG and gD in a gE-gI-dependent process, resulting in lysosomal localization. These results suggest that gE-gI can mediate clearance of infected cell surfaces of anti-viral host IgG and viral antigens to evade IgG-mediated responses, representing a general mechanism for viral Fc receptors in immune evasion and viral pathogenesis.

Indexed as

Antigens, ViralCell MembraneFluorescent Antibody TechniqueHeLa CellsHerpes SimplexHerpesvirus 1, HumanHumansImmune EvasionMicroscopy, ConfocalReceptors, FcTransfectionViral ProteinsAntigens, ViralReceptors, FcViral Proteins

Identifiers

PMID24604090
PMCPMC3946383
OpenAlexW2095003599

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.