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TitleThe cryo-electron microscopy structure of feline calicivirus bound to junctional adhesion molecule A at 9-angstrom resolution reveals receptor-induced flexibility and two distinct conformational changes in the capsid protein VP1.
Journal, issue, pagesJ Virol, Vol. 85, Issue 21, Page 11381-11390, Year 2011
Publish dateAug 24, 2011
AuthorsDavid Bhella / Ian G Goodfellow /
PubMed AbstractCaliciviridae are small icosahedral positive-sense RNA-containing viruses and include the human noroviruses, a leading cause of infectious acute gastroenteritis and feline calicivirus (FCV), which ...Caliciviridae are small icosahedral positive-sense RNA-containing viruses and include the human noroviruses, a leading cause of infectious acute gastroenteritis and feline calicivirus (FCV), which causes respiratory illness and stomatitis in cats. FCV attachment and entry is mediated by feline junctional adhesion molecule A (fJAM-A), which binds to the outer face of the capsomere, inducing a conformational change in the capsid that may be important for viral uncoating. Here we present the results of our structural investigation of the virus-receptor interaction and ensuing conformational changes. Cryo-electron microscopy and three-dimensional image reconstruction were used to solve the structure of the virus decorated with a soluble fragment of the receptor at subnanometer resolution. In initial reconstructions, the P domains of the capsid protein VP1 and fJAM-A were poorly resolved. Sorting experiments led to improved reconstructions of the FCV-fJAM-A complex both before and after the induced conformational change, as well as in three transition states. These data showed that the P domain becomes flexible following fJAM-A binding, leading to a loss of icosahedral symmetry. Furthermore, two distinct conformational changes were seen; an anticlockwise rotation of up to 15° of the P domain was observed in the AB dimers, while tilting of the P domain away from the icosahedral 2-fold axis was seen in the CC dimers. A list of putative contact residues was calculated by fitting high-resolution coordinates for fJAM-A and VP1 to the reconstructed density maps, highlighting regions in both virus and receptor important for virus attachment and entry.
External linksJ Virol / PubMed:21865392 / PubMed Central
MethodsEM (single particle)
Resolution8.9 - 12.3 Å
Structure data

EMDB-1942:
Feline Calicivirus strain F9
Method: EM (single particle) / Resolution: 8.9 Å

EMDB-1943:
Feline Calicivirus strain F9 decorated with Junctional Adhesion Molecule A
Method: EM (single particle) / Resolution: 11.8 Å

EMDB-1944:
Feline Calicivirus strain F9 decorated with Junctional Adhesion Molecule A
Method: EM (single particle) / Resolution: 10.3 Å

EMDB-1945:
Feline Calicivirus strain F9 decorated with Junctional Adhesion Molecule A
Method: EM (single particle) / Resolution: 10.2 Å

EMDB-1946:
Feline Calicivirus strain F9 decorated with Junctional Adhesion Molecule A
Method: EM (single particle) / Resolution: 10.8 Å

EMDB-1947:
Feline Calicivirus strain F9 decorated with Junctional Adhesion Molecule A
Method: EM (single particle) / Resolution: 12.3 Å

EMDB-1948:
Feline Calicivirus strain F9 decorated with Junctional Adhesion Molecule A
Method: EM (single particle) / Resolution: 9.2 Å

Source
  • Felis catus (domestic cat)

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