Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Loss of FCoV-23 spike domain 0 enhances fusogenicity and entry kinetics.
Journal, issue, pages	Nature, Vol. 645, Issue 8079, Page 235-243, Year 2025
Publish date	Jul 9, 2025
Authors	M Alejandra Tortorici / Annette Choi / Cecily A Gibson / Jimin Lee / Jack T Brown / Cameron Stewart / Anshu Joshi / Sheri Harari / Isabelle Willoughby / Catherine Treichel / Elizabeth M Leaf / Jesse D Bloom / Neil P King / Christine Tait-Burkard / Gary R Whittaker / David Veesler /
PubMed Abstract	The ability of coronaviruses to recombine and cross species barriers affects human and animal health globally and is a pandemic threat. FCoV-23 is a recently emerged, highly pathogenic recombinant ...The ability of coronaviruses to recombine and cross species barriers affects human and animal health globally and is a pandemic threat. FCoV-23 is a recently emerged, highly pathogenic recombinant coronavirus responsible for a widespread outbreak of feline infectious peritonitis. Here we report cryogenic electron microscopy structures of two FCoV-23 spike isoforms that correspond to the in-host loss of domain 0 observed in clinical samples. The loss of domain 0 markedly enhances the fusogenicity and kinetics of entry into cells and possibly enables biotype switching and lethality. We show that FCoV-23 can use several aminopeptidase N orthologues as receptors and reveal the molecular determinants of receptor species tropism, including a glycan that modulates human receptor engagement. We define antigenic relationships among alphacoronaviruses that infect humans and other mammalian species and identify a cross-reactive alphacoronavirus monoclonal antibody that inhibits FCoV-23 entry. Our results pave the way for the development of vaccines and therapeutics that target this highly pathogenic virus.
External links	Nature / PubMed:40634609 / PubMed Central
Methods	EM (single particle)
Resolution	2.3 - 3.2 Å
Structure data	46708 9daz EMDB-46708, PDB-9daz: Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. Complex of fAPN with FCoV-23 RBD Method: EM (single particle) / Resolution: 2.5 Å 46709 9db0 EMDB-46709, PDB-9db0: Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. FCoV-23 S short Method: EM (single particle) / Resolution: 2.5 Å 46710 9db1 EMDB-46710, PDB-9db1: Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. FCoV-23 S Do in proximal conformation (local refinement) Method: EM (single particle) / Resolution: 3.2 Å 46714 9db3 EMDB-46714, PDB-9db3: Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. FCoV-23 S long with Do in swung-out conformation Method: EM (single particle) / Resolution: 2.3 Å 46716 9dbe EMDB-46716, PDB-9dbe: Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. FCoV-23 S long domain 0 in swung-out conformation (local refinement) Method: EM (single particle) / Resolution: 2.4 Å 46739 9dbz EMDB-46739, PDB-9dbz: Molecular basis of pathogenicity of the recently emerged FCoV-23 coronavirus. FCoV-23 S long with Do in mixed conformations (global refinement). Method: EM (single particle) / Resolution: 2.7 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-ZN: Unknown entry ChemComp-HOH: WATER ChemComp-PAM: PALMITOLEIC ACID
Source	feline coronavirus felis catus (domestic cat)
Keywords	VIRAL PROTEIN/HYDROLASE / Coronavirus / alphacoronavirus / feline coronavirus / cryo-EM / neutralization assays / binding assays / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / VIRAL PROTEIN-HYDROLASE complex / VIRAL PROTEIN