Evidence map›Paper›PMID 31092568›Full record

ArticleJournal of virology2019

Surface Plasmon Resonance Reveals Direct Binding of Herpes Simplex Virus Glycoproteins gH/gL to gD and Locates a gH/gL Binding Site on gD.

Tina M Cairns, Noah T Ditto, Doina Atanasiu, Huan Lou, Benjamin D Brooks, Wan Ting Saw, Roselyn J Eisenberg, Gary H Cohen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

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  12. Anti-herpes simplex virus activities and mechanisms of marine derived compounds.Frontiers in cellular and infection microbiology · 2023
    Review
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  16. Moving beyond Titers.Vaccines · 2022
    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

8 authors at 2 institutions in 1 country.

Tina M CairnsDepartment of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA tmcairns@upenn.edu.
Noah T DittoCarterra, Inc., Salt Lake City, Utah, USA.
Doina AtanasiuDepartment of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Huan LouDepartment of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Benjamin D BrooksCarterra, Inc., Salt Lake City, Utah, USA.
Wan Ting SawDepartment of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Roselyn J EisenbergDepartment of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Gary H CohenDepartment of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
University of Pennsylvania · USCarterra (United States) · US

Funding

Studies of Herpes Simplex Virus GlycoproteinsR37AI018289 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI COHEN, GARY H · 2005 to 2014
$3.9M
STUDIES OF HERPES SIMPLEX VIRUS GLYCOPROTEINSR01AI018289 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI COHEN, GARY H · 1985 to 2019
$3.8M
NIAID NIH HHS R01 AI018289NIAID NIH HHS R37 AI018289
6 · The paper itself

Abstract

Herpes simplex virus (HSV) requires fusion between the viral envelope and host membrane. Four glycoproteins, gD, gH/gL, and gB, are essential for this process. To initiate fusion, gD binds its receptor and undergoes a conformational change that hypothetically leads to activation of gH/gL, which in turn triggers the fusion protein gB to undergo rearrangements leading to membrane fusion. Our model predicts that gD must interact with both its receptor and gH/gL to promote fusion. In support of this, we have shown that gD is structurally divided into two "faces": one for the binding receptor and the other for its presumed interaction with gH/gL. However, until now, we have been unable to demonstrate a direct interaction between gD and gH/gL. Here, we used surface plasmon resonance to show that the ectodomain of gH/gL binds directly to the ectodomain of gD when (i) gD is captured by certain anti-gD monoclonal antibodies (MAbs) that are bound to a biosensor chip, (ii) gD is bound to either one of its receptors on a chip, and (iii) gD is covalently bound to the chip surface. To localize the gH/gL binding site on gD, we used multiple anti-gD MAbs from six antigenic communities and determined which ones interfered with this interaction. MAbs from three separate communities block gD-gH/gL binding, and their epitopes encircle a geographical area on gD that we propose comprises the gH/gL binding domain. Together, our results show that gH/gL interacts directly with gD, supporting a role for this step in HSV entry.

Indexed as

Protein Interaction MapsVirus InternalizationBinding SitesHerpesvirus 1, HumanProtein BindingSurface Plasmon ResonanceViral Envelope Proteinsglycoprotein D, Human herpesvirus 1glycoprotein H, herpes simplex virus type 1glycoprotein L, Human herpesvirus 1Viral Envelope Proteinsglycoproteinsherpes simplex virussurface plasmon resonancevirus entry

Identifiers

PMID31092568
PMCPMC6639271
OpenAlexW2945154138

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.