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TitleThe 2.6 Å Structure of a Tulane Virus Variant with Minor Mutations Leading to Receptor Change.
Journal, issue, pagesBiomolecules, Vol. 14, Issue 1, Year 2024
Publish dateJan 16, 2024
AuthorsChen Sun / Pengwei Huang / Xueyong Xu / Frank S Vago / Kunpeng Li / Thomas Klose / Xi Jason Jiang / Wen Jiang /
PubMed AbstractHuman noroviruses (HuNoVs) are a major cause of acute gastroenteritis, contributing significantly to annual foodborne illness cases. However, studying these viruses has been challenging due to ...Human noroviruses (HuNoVs) are a major cause of acute gastroenteritis, contributing significantly to annual foodborne illness cases. However, studying these viruses has been challenging due to limitations in tissue culture techniques for over four decades. Tulane virus (TV) has emerged as a crucial surrogate for HuNoVs due to its close resemblance in amino acid composition and the availability of a robust cell culture system. Initially isolated from rhesus macaques in 2008, TV represents a novel belonging to the genus. Its significance lies in sharing the same host cell receptor, histo-blood group antigen (HBGA), as HuNoVs. In this study, we introduce, through cryo-electron microscopy (cryo-EM), the structure of a specific TV variant (the 9-6-17 TV) that has notably lost its ability to bind to its receptor, B-type HBGA-a finding confirmed using an enzyme-linked immunosorbent assay (ELISA). These results offer a profound insight into the genetic modifications occurring in TV that are necessary for adaptation to cell culture environments. This research significantly contributes to advancing our understanding of the genetic changes that are pivotal to successful adaptation, shedding light on fundamental aspects of evolution.
External linksBiomolecules / PubMed:38254719 / PubMed Central
MethodsEM (single particle)
Resolution2.08 - 3.2 Å
Structure data

43222

8vgr

EMDB-43222, PDB-8vgr:
Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 5-12-18
Method: EM (single particle) / Resolution: 3.2 Å

43292

8vjr

EMDB-43292, PDB-8vjr:
Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 9-14-18, DTT-treated
Method: EM (single particle) / Resolution: 2.63 Å

43293

8vjs

EMDB-43293, PDB-8vjs:
Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 9-14-18 without DTT treatment
Method: EM (single particle) / Resolution: 2.73 Å

45962

9cve

EMDB-45962, PDB-9cve:
Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 5-12-18
Method: EM (single particle) / Resolution: 3.18 Å

45963

9cvf

EMDB-45963, PDB-9cvf:
Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 9-14-18
Method: EM (single particle) / Resolution: 3.0 Å

45964

9cvg

EMDB-45964, PDB-9cvg:
Cryo-EM structure of Tulane virus 9-6-17 variant capsid protein VP1 9-14-18, DTT-treated
Method: EM (single particle) / Resolution: 2.08 Å

Source
  • tulane virus
KeywordsVIRUS / virion capsid / capsid protein / Tulane virus

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