Evidence map›Paper›PMID 26686638›Full record

ArticleCell reports2015

Neutralizing Monoclonal Antibodies Block Chikungunya Virus Entry and Release by Targeting an Epitope Critical to Viral Pathogenesis.

Jing Jin, Nathan M Liss, Dong-Hua Chen, Maofu Liao, Julie M Fox, Raeann M Shimak, Rachel H Fong, Daniel Chafets, Sonia Bakkour, Sheila Keating and 6 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

80 citing papers in PubMed, 112 citations in OpenAlex.

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  14. Antiviral Protein-Protein Interaction Inhibitors.Journal of medicinal chemistry · 2024
    Review
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20 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

16 authors at 7 institutions in 1 country.

Jing JinBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Nathan M LissBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Dong-Hua ChenDepartment of Structural Biology, Stanford University, Stanford, CA 94305, USA.
Maofu LiaoDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Julie M FoxDepartments of Medicine, Molecular Microbiology, Pathology & Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Raeann M ShimakDepartments of Medicine, Molecular Microbiology, Pathology & Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Rachel H FongIntegral Molecular Inc., Philadelphia, PA 19104, USA.
Daniel ChafetsBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Sonia BakkourBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Sheila KeatingBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Marina E FominBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Marcus O MuenchBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Michael B ShermanDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Benjamin J DoranzIntegral Molecular Inc., Philadelphia, PA 19104, USA.
Michael S DiamondDepartments of Medicine, Molecular Microbiology, Pathology & Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Graham SimmonsBlood Systems Research Institute, San Francisco, CA 94118, USA; Department of Laboratory Medicine, University of California, San Francisco, San Francisco, CA 94143, USA. Electronic address: gsimmons@bloodsystems.org.
University of California, San Francisco · USBlood Systems Research Institute · USWashington University in St. Louis · USIntegral Molecular (United States) · USHarvard University · USStanford University · USThe University of Texas Medical Branch at Galveston · US

Funding

Antibody Based Therapeuticcs for Chikungunya VirusR01AI089591 · NIAID · WASHINGTON UNIVERSITY · PI DIAMOND, MICHAEL S · 2010 to 2014
$4.7M
Structural and functional basis of ultra potent CHKV neutralization by human mAbsR01AI114816 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI CROWE, JAMES E, DIAMOND, MICHAEL S · 2015 to 2019
$3.7M
Protective B-cell responses in chikungunya virus infectionR01AI119056 · NIAID · VITALANT · PI SIMMONS, GRAHAM · 2016 to 2019
$1.9M
Protective B-cell responses in chikungunya virus infectionR56AI119056 · NIAID · VITALANT · PI SIMMONS, GRAHAM · 2015 to 2015
$436k
NIAID NIH HHS HHSN272200700055CNIAID NIH HHS R01 AI089591NIAID NIH HHS R01 AI114816NIAID NIH HHS R01 AI119056NIAID NIH HHS R56 AI119056
6 · The paper itself

Abstract

We evaluated the mechanism by which neutralizing human monoclonal antibodies inhibit chikungunya virus (CHIKV) infection. Potently neutralizing antibodies (NAbs) blocked infection at multiple steps of the virus life cycle, including entry and release. Cryo-electron microscopy structures of Fab fragments of two human NAbs and chikungunya virus-like particles showed a binding footprint that spanned independent domains on neighboring E2 subunits within one viral spike, suggesting a mechanism for inhibiting low-pH-dependent membrane fusion. Detailed epitope mapping identified amino acid E2-W64 as a critical interaction residue. An escape mutation (E2-W64G) at this residue rendered CHIKV attenuated in mice. Consistent with these data, CHIKV-E2-W64G failed to emerge in vivo under the selection pressure of one of the NAbs, IM-CKV063. As our study suggests that antibodies engaging the residue E2-W64 can potently inhibit CHIKV at multiple stages of infection, antibody-based therapies or immunogens that target this region might have protective value.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingArthritisChemokinesChikungunya virusChlorocebus aethiopsCytokinesDisease Models, AnimalEpitope MappingEpitopesGenotypeHumansMembrane FusionMiceMice, Inbred C57BLAntibodies, MonoclonalAntibodies, NeutralizingChemokinesCytokinesEpitopesViral Envelope Proteins

Identifiers

PMID26686638
PMCPMC4720387
OpenAlexW2193670806

What OpenQuestion holds

Textmetadata
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.