Evidence map›Paper›PMID 30622256›Full record

ArticleNature communications2019

Molecular recognition of the native HIV-1 MPER revealed by STED microscopy of single virions.

Pablo Carravilla, Jakub Chojnacki, Edurne Rujas, Sara Insausti, Eneko Largo, Dominic Waithe, Beatriz Apellaniz, Taylor Sicard, Jean-Philippe Julien, Christian Eggeling and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

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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

11 authors.

Pablo CarravillaBiofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080, Bilbao, Spain.ORCID http://orcid.org/0000-0001-6592-7630
Jakub ChojnackiMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK.ORCID http://orcid.org/0000-0002-4457-8096
Edurne RujasBiofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080, Bilbao, Spain.
Sara InsaustiBiofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080, Bilbao, Spain.
Eneko LargoBiofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080, Bilbao, Spain.
Dominic WaitheMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK.ORCID http://orcid.org/0000-0003-2685-4226
Beatriz ApellanizBiofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080, Bilbao, Spain.
Taylor SicardProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, M5G 0A4, Canada.
Jean-Philippe JulienProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON, M5G 0A4, Canada.ORCID http://orcid.org/0000-0001-7602-3995
Christian EggelingMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, OX3 9DS, UK. christian.eggeling@rdm.ox.ac.uk.
José L NievaBiofisika Institute (CSIC, UPV/EHU) and Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080, Bilbao, Spain. joseluis.nieva@ehu.es.

Funding

Medical Research Council G0902418Medical Research Council MC_PC_15065Medical Research Council MC_UU_00008/9Medical Research Council MC_UU_12010/9Medical Research Council MR/K01577X/1Medical Research Council MR/S005382/1NIH HHS NIH-150414Wellcome Trust
6 · The paper itself

Abstract

Antibodies against the Membrane-Proximal External Region (MPER) of the Env gp41 subunit neutralize HIV-1 with exceptional breadth and potency. Due to the lack of knowledge on the MPER native structure and accessibility, different and exclusive models have been proposed for the molecular mechanism of MPER recognition by broadly neutralizing antibodies. Here, accessibility of antibodies to the native Env MPER on single virions has been addressed through STED microscopy. STED imaging of fluorescently labeled Fabs reveals a common pattern of native Env recognition for HIV-1 antibodies targeting MPER or the surface subunit gp120. In the case of anti-MPER antibodies, the process evolves with extra contribution of interactions with the viral lipid membrane to binding specificity. Our data provide biophysical insights into the recognition of the potent and broadly neutralizing MPER epitope on HIV virions, and as such is of importance for the design of therapeutic interventions.

Indexed as

Antibodies, NeutralizingEpitopesFluorescent DyesHEK293 CellsHIV-1HIV AntibodiesHIV Envelope Protein gp41HumansImage Processing, Computer-AssistedImmunoglobulin Fab FragmentsMicroscopy, FluorescenceProtein BindingVirionAntibodies, NeutralizingEpitopesFluorescent DyesHIV AntibodiesHIV Envelope Protein gp41Immunoglobulin Fab Fragments

Identifiers

PMID30622256
PMCPMC6325134

What OpenQuestion holds

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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.