Evidence map›Paper›PMID 39688401›Full record

ArticlemBio2025

From structure prediction to function: defining the domain on the African swine fever virus CD2v protein required for binding to erythrocytes.

Ana Luisa Reis, Anusyah Rathakrishnan, Vlad Petrovan, Muneeb Islam, Lynnette Goatley, Katy Moffat, Mai Tuyet Vuong, Yuan Lui, Simon J Davis, Shinji Ikemizu and 1 more

Abstract read
In one paragraph

Article in mBio, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
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.

Ana Luisa ReisThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.
Anusyah RathakrishnanThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.
Vlad PetrovanThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.
Muneeb IslamThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.
Lynnette GoatleyThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.
Katy MoffatThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.
Mai Tuyet VuongRadcliffe Department of Medicine, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, Oxford, United Kingdom.
Yuan LuiRadcliffe Department of Medicine, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, Oxford, United Kingdom.
Simon J DavisRadcliffe Department of Medicine, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, University of Oxford, Oxford, United Kingdom.
Shinji IkemizuGraduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan.
Linda K DixonThe Pirbright Institute, Woking, Pirbright, Surrey, United Kingdom.ORCID 0000-0003-3845-3016

Funding

GALVmed OPP1009497UKRI | Biotechnology and Biological Sciences Research Council (BBSRC) BBS/V0079447, BB/X011046/1, BB/X011038/1, BB/CCG2250/1, BBS/E/I/00007039, BBC/E/i/00007037UKRI | Medical Research Council (MRC) MC_UU_12010Wellcome TrustWellcome Trust (WT) 207547/Z/17/Z
6 · The paper itself

Abstract

African swine fever virus (ASFV) is a high-consequence pathogen posing a substantial threat to global food security. This large DNA virus encodes more than 150 open reading frames, many of which are uncharacterized. The IMPORTANCE: A better understanding of the interactions between viruses and their hosts is a crucial step in the development of strategies for controlling viral diseases, such as vaccines and antivirals. African swine fever, a pig disease with fatality rates approaching 100%, causes very substantial economic losses in affected countries, and new control measures are clearly needed. In this study, we characterized the interaction between the ASFV CD2v protein and host erythrocytes. The interaction plays a key role in viral persistence in blood since it can allow the virus to "hide" from the host immune system. We identified the amino acids in the viral protein that mediate the interaction with erythrocytes and used this information to construct a mutant virus that is no longer able to bind these cells. This virus induces strong immune responses that provide high levels of protection against infection with the deadly parental virus.

Indexed as

African Swine Fever VirusErythrocytesViral ProteinsVirus AttachmentAfrican Swine FeverAnimalsModels, MolecularProtein BindingProtein DomainsSwineViral ProteinsAfrican swine fever virusEP402Rerythrocyte adhesionimmune evasionpersistencevirulence factors

Identifiers

PMID39688401
PMCPMC11796414

What Socratic 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 Socratic graph.