Literature detail

LRP4 is an entry receptor for multiple encephalitic alphaviruses.

Sicheng Tian1 Bingting Ma2 Hongyuan Guo1 Zhenlu Chong3 Theron C Gilliland4 Sean Hui3 Guojie Wang1 Yuyi Zhang1 Jiayue Zhou1 Alan Sariol3 Xinran Sun1 Yingxin Hu5 Zhuohao He5 Daved H Fremont3 William B Klimstra4 Michael S Diamond6 Ye Xiang7 Rong Zhang8
Affiliations 8 institutions
  1. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai, China.
  2. Beijing Frontier Research Center for Biological Structure, Center for Infection Biology, School of Basic Medical Sciences, Tsinghua University, Beijing, China.
  3. Departments of Medicine, Pathology & Immunology, and Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, USA.
  4. The Center for Vaccine Research and Department of Immunology, The University of Pittsburgh, Pittsburgh, PA, USA.
  5. Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, University of the Chinese Academy of Sciences, Shanghai, China.
  6. Departments of Medicine, Pathology & Immunology, and Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, USA. [email protected].
  7. Beijing Frontier Research Center for Biological Structure, Center for Infection Biology, School of Basic Medical Sciences, Tsinghua University, Beijing, China. [email protected].
  8. Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, School of Basic Medical Sciences, Fudan University, Shanghai, China. [email protected].
PMID 42265108 2026 Nat Commun eng aheadofprint
PubMed DOI Browse context

Article

Publication summary

Encephalitic alphaviruses, including Eastern equine encephalitis virus (EEEV), cause severe neurological disease with high mortality rates, and thus are a public health threat. Although members of the low-density lipoprotein receptor (LDLR) family, including VLDLR, LRP8 (ApoER2), and LDLR recently were identified as receptors for EEEV, residual infection in receptor-deficient cells suggests that additional entry factors exist. Using a CRISPR-based activation screen, we identified LDLR-related protein 4 (LRP4) as a candidate entry factor for EEEV and several related alphaviruses (Western equine encephalitis, Semliki Forest, and Sindbis viruses). LRP4 mediates viral attachment and internalization, and its ligand-binding domain binds directly to virions. Soluble LRP4 decoy proteins potently inhibit EEEV infection in primary mouse neuronal cells, male mice, and human brain organoids, suggesting possible therapeutic applications. Mammalian and avian LRP4 orthologs demonstrate conserved functions in promoting EEEV infection, supporting a possible role in its host range of infection and transmission. Our findings establish LRP4 as a shared entry receptor for multiple alphaviruses and expand our understanding of alphavirus tropism, pathogenesis, and countermeasure development.

Structured evidence records

Evidence records

2 total
1 records
Extraction confidence 0.90
Key finding

Mammalian and avian LRP4 orthologs both promote EEEV infection, indicating a conserved receptor mechanism that may influence host range.

Virus
Not specified
Host
Not specified
Location
Not specified
Supporting text

Mammalian and avian LRP4 orthologs demonstrate conserved functions in promoting EEEV infection, supporting a possible role in its host range of infection and transmission.

Method
functional assays with orthologs
Study design
comparative receptor assay
Transmission direction
molecular mechanism only
Event type
conserved receptor function across vertebrate hosts
Genes or proteins
LRP4
Receptors
LRP4
Mechanism types
host receptor conservation
1 records
Extraction confidence 0.95
Key finding

LRP4 functions as an entry receptor that mediates attachment and internalization for multiple encephalitic alphaviruses.

Virus
Location
Not specified
Supporting text

Using a CRISPR-based activation screen, we identified LDLR-related protein 4 (LRP4) as a candidate entry factor for EEEV and several related alphaviruses ... LRP4 mediates viral attachment and internalization, and its ligand-binding domain binds directly to virions.

Method
CRISPR-based activation screen | binding assays | infection assays in cells and organoids
Sample type
primary mouse neuronal cells | male mice | human brain organoids
Study design
receptor-binding assay
Transmission direction
molecular mechanism only
Event type
LRP4-mediated entry mechanism
Genes or proteins
LRP4
Receptors
LRP4
Mechanism types
viral attachment | internalization | receptor binding