Evidence map›Paper›PMID 42535854›Full record

ArticlemBio2026

KREMEN1 residue W94 is essential for receptor binding and infection by a major group of enteroviruses.

Xiaohong Li, Pan Liu, Hongzheng Li, Youwei Zhu, Ruiyi Zhang, Xingchen Xie, Rui Yu, Feilong Zhou, Jingjing Yan, Min Wang and 9 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2026. 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

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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.

No citing paper in PubMed yet.

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

19 authors.

Xiaohong Li *Clinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.ORCID 0000-0001-5273-2404
Pan Liu *Shanghai Institute of Infectious Disease and Biosecurity, Fudan University, Shanghai, China.
Hongzheng Li *State Key Laboratory of Virology and Hubei Province Key Laboratory of Allergy and Immunology, and Department of Immunology, Wuhan University TaiKang Medical School (School of Basic Medical Sciences), Wuhan, China.
Youwei Zhu *Shanghai Institute of Infectious Disease and Biosecurity, Fudan University, Shanghai, China.
Ruiyi ZhangShanghai Institute of Infectious Disease and Biosecurity, Fudan University, Shanghai, China.
Xingchen XieInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.
Rui YuClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.
Feilong ZhouClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.
Jingjing YanShanghai Public Health Clinical Center, Fudan University, Shanghai, China.
Min WangShanghai Public Health Clinical Center, Fudan University, Shanghai, China.
Jiayi ShuClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.
Chenli QiuClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.
Shuo ZhangClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.
Zichen YangEngineering Research Center of Cell & Therapeutic Antibody, School of Pharmacy, Shanghai Jiao Tong University, Shanghai, China.
Zhijun LiuDepartment of Microbiology, Weifang Medical University, Weifang, China.
Xiaoyan ZhangClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.
Jianqing XuClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.ORCID 0000-0003-0896-9273
Chao ZhangShanghai Institute of Infectious Disease and Biosecurity, Fudan University, Shanghai, China.ORCID 0000-0002-8658-9009
Shuye ZhangClinical Center for Biotherapy, Zhongshan Hospital, Fudan University, Shanghai, China.ORCID 0000-0002-4749-6790

Funding

National Key Research and Development Program of China 2023YFC2306400National Natural Science Foundation of China 82472252
6 · The paper itself

Abstract

KREMEN1 (KRM1) serves as a cellular receptor for a major group of enteroviruses causing hand, foot, and mouth disease (HFMD), including CVA2-CVA6, CVA8, CVA10, and CVA12. The viral VP2 residue K140 has recently been identified as completely conserved among these viruses and critical for interaction with KRM1 and viral infection. However, the molecular determinants on the receptor side that govern broad enterovirus recognition remain incompletely understood. Here, we identify KRM1 tryptophan 94 (W94) as an essential residue for KRM1-mediated enterovirus infection. Alanine scanning of 29 KRM1 residues at the CVA10-KRM1 interface revealed that only W94A nearly abolished CVA10 infection. Structural analysis revealed that KRM1 W94 engages in a π-cation interaction with the viral VP2 residue K140, which is critical for receptor binding. Unlike wild-type mice, which succumbed to CVA10 infection, CRISPR-engineered mouse Krm1 W94A mutant mice were fully resistant. Moreover, the W94A mutation conferred universal resistance to all KRM1-dependent enteroviruses (CVA2-CVA6, CVA8, CVA10, and CVA12), both in cell culture and

Indexed as

EnterovirusEnterovirus InfectionsMembrane ProteinsReceptors, VirusVirus AttachmentAnimalsCapsid ProteinsHumansMiceProtein BindingCapsid ProteinsMembrane ProteinsReceptors, Virusenterovirushand, foot, and mouth diseaseinfectionKREMEN1 receptor

Identifiers

PMID42535854
PMCPMC13556202

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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.