Evidence map›Paper›PMID 38045373›Full record

ArticlebioRxiv : the preprint server for biology2023

Structure guided mutagenesis of Henipavirus Receptor Binding Proteins reveals molecular determinants of receptor usage and antibody binding epitopes.

K Y Oguntuyo, G D Haas, K D Azarm, C S Stevens, L Brambilla, S Kowdle, V A Avanzato, R Pryce, A N Freiberg, T A Bowden and 1 more

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

K Y OguntuyoDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0001-7824-2892
G D HaasDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0002-2517-1071
K D AzarmDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0002-4859-5117
C S StevensDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0003-2472-6984
L BrambillaDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0002-5296-2426
S KowdleDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0002-7786-3547
V A AvanzatoDivision of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom.ORCID 0000-0001-5758-8624
R PryceDivision of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom.ORCID 0000-0001-8824-9721
A N FreibergDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA.ORCID 0000-0001-8413-8960
T A BowdenDivision of Structural Biology, Wellcome Center for Human Genetics, University of Oxford, OX3 7BN Oxford, United Kingdom.ORCID 0000-0002-8066-8785
B LeeDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID 0000-0003-0760-1709
Icahn School of Medicine at Mount Sinai · USCentre for Human Genetics · GBThe University of Texas Medical Branch at Galveston · US

Funding

TRAINING PROGRAM: MECHANISMS OF VIRUS-HOST INTERACTIONST32AI007647 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI Domenico Tortorella · 2000 to 2026
$11.5M
Tropism, pathogenicity, and potential for zoonotic spillover of emergent henipa- and henipa-like virusesR01AI123449 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI LEE, BENHUR · 2016 to 2020
$2.7M
Elucidating the molecular determinants of Henipavirus envelope-antibody and envelope-receptor interactions on viral entryF31AI154739 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI OGUNTUYO, KASOPEFOLUWA Y. · 2020 to 2022
$135k
Generation and characterization of broadly neutralizing antibodies against diverse HenipavirusesF31AI133943 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI AZARM, KRISTOPHER · 2018 to 2019
$90k
NIAID NIH HHS F31 AI133943NIAID NIH HHS F31 AI154739NIAID NIH HHS R01 AI123449NIAID NIH HHS T32 AI007647Wellcome Trust
6 · The paper itself

Abstract

Nipah virus (NiV) is a highly lethal, zoonotic henipavirus (HNV) that causes respiratory and neurological signs and symptoms in humans. Similar to other paramyxoviruses, HNVs mediate entry into host cells through the concerted actions of two surface glycoproteins: a receptor binding protein (RBP) that mediates attachment and a fusion glycoprotein (F) that triggers fusion in an RBP-dependent manner. NiV uses ephrin-B2 (EFNB2) and ephrin-B3 (EFNB3) as entry receptors. Ghana virus (GhV), a novel HNV identified in a Ghanaian bat, use EFNB2 but not EFNB3. In this study, we employ a structure-informed approach to identify receptor interfacing residues and systematically introduce GhV-RBP residues into a NiV-RBP backbone to uncover the molecular determinants of EFNB3 usage. We reveal two regions that severely impair EFNB3 binding by NiV-RBP and EFNB3-mediated entry by NiV pseudotyped viral particles. Further analyses uncovered two point mutations (

Identifiers

PMID38045373
PMCPMC10690272
OpenAlexW4388923484

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.