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TitleMolecular basis for shifted receptor recognition by an encephalitic arbovirus.
Journal, issue, pagesCell, Vol. 188, Issue 11, Page 2957-2973.e28, Year 2025
Publish dateMay 29, 2025
AuthorsXiaoyi Fan / Wanyu Li / Jessica Oros / Jessica A Plante / Brooke M Mitchell / Jesse S Plung / Himanish Basu / Sivapratha Nagappan-Chettiar / Joshua M Boeckers / Laurentia V Tjang / Colin J Mann / Vesna Brusic / Tierra K Buck / Haley Varnum / Pan Yang / Linzy M Malcolm / So Yoen Choi / William M de Souza / Isaac M Chiu / Hisashi Umemori / Scott C Weaver / Kenneth S Plante / Jonathan Abraham /
PubMed AbstractWestern equine encephalitis virus (WEEV) is an arbovirus that historically caused large outbreaks of encephalitis throughout the Americas. WEEV binds protocadherin 10 (PCDH10) as a receptor, and ...Western equine encephalitis virus (WEEV) is an arbovirus that historically caused large outbreaks of encephalitis throughout the Americas. WEEV binds protocadherin 10 (PCDH10) as a receptor, and highly virulent ancestral WEEV strains also bind low-density lipoprotein receptor (LDLR)-related proteins. As WEEV declined as a human pathogen in North America over the past century, isolates have lost the ability to bind mammalian receptors while still recognizing avian receptors. To explain shifts in receptor dependencies and assess the risk of WEEV re-emergence, we determined cryoelectron microscopy structures of WEEV bound to human PCDH10, avian PCDH10, and human very-low-density lipoprotein receptor (VLDLR). We show that one to three E2 glycoprotein substitutions are sufficient for a nonpathogenic strain to regain the ability to bind mammalian receptors. A soluble VLDLR fragment protects mice from lethal challenge by a virulent ancestral WEEV strain. Because WEEV recently re-emerged in South America after decades of inactivity, our findings have important implications for outbreak preparedness.
External linksCell / PubMed:40187345 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.4 Å
Structure data

47116

9dqv

EMDB-47116, PDB-9dqv:
Structure of western equine encephalitis virus CBA87 VLP in complex with human PCDH10 EC1
Method: EM (single particle) / Resolution: 3.3 Å

47117

9dqx

EMDB-47117, PDB-9dqx:
Structure of western equine encephalitis virus CBA87 VLP
Method: EM (single particle) / Resolution: 3.4 Å

47118

9dqy

EMDB-47118, PDB-9dqy:
Structure of western equine encephalitis virus Imperial 181 VLP in complex with house sparrow PCDH10 EC1
Method: EM (single particle) / Resolution: 2.8 Å

47119

9dqz

EMDB-47119, PDB-9dqz:
Structure of western equine encephalitis virus McMillan VLP in complex with human VLDLR
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CA:
Unknown entry

Source
  • western equine encephalitis virus
  • homo sapiens (human)
  • passer domesticus (house sparrow)
KeywordsVIRUS LIKE PARTICLE / western equine encephalitis virus / WEEV / receptor binding / PCDH10 / virus like particles / VLDLR

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