1OOP

The Crystal Structure of Swine Vesicular Disease Virus

Summary for 1OOP

• Entry DOI: 10.2210/pdb1oop/pdb
• Descriptor: Coat protein VP1, Coat protein VP2, Coat protein VP3, ... (6 entities in total)
• Functional Keywords: picornavirus structure, virus/viral protein, virus-receptor interactions, host adaptation, car, daf, coxsackievirus, icosahedral virus, virus
• Biological source: Swine vesicular disease virus (STRAIN UKG/27/72); More
• Cellular location: Capsid protein VP0: Virion . Capsid protein VP4: Virion . Capsid protein VP2: Virion . Capsid protein VP3: Virion . Capsid protein VP1: Virion . Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion . Protease 3C: Host cytoplasm . Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P13900 P13900 P13900 P13900
• Total number of polymer chains: 4
• Total formula weight: 94260.38

Authors

Fry, E.E.,Knowles, N.J.,Newman, J.W.I.,Wilsden, G.,Rao, Z.,King, A.M.Q.,Stuart, D.I. (deposition date: 2003-03-04, release date: 2003-04-22, Last modification date: 2024-04-03)

Primary citation

Fry, E.E.,Knowles, N.J.,Newman, J.W.I.,Wilsden, G.,Rao, Z.,King, A.M.Q.,Stuart, D.I.
Crystal Structure of Swine Vesicular Disease Virus and Implications for Host Adaptation
J.Virol., 77:5475-5486, 2003

PubMed Abstract: Swine vesicular disease virus (SVDV) is an Enterovirus of the family Picornaviridae that causes symptoms indistinguishable from those of foot-and-mouth disease virus. Phylogenetic studies suggest that it is a recently evolved genetic sublineage of the important human pathogen coxsackievirus B5 (CBV5), and in agreement with this, it has been shown to utilize the coxsackie and adenovirus receptor (CAR) for cell entry. The 3.0-A crystal structure of strain UK/27/72 SVDV (highly virulent) reveals the expected similarity in core structure to those of other picornaviruses, showing most similarity to the closest available structure to CBV5, that of coxsackievirus B3 (CBV3). Features that help to cement together and rigidify the protein subunits are extended in this virus, perhaps explaining its extreme tolerance of environmental factors. Using the large number of capsid sequences available for both SVDV and CBV5, we have mapped the amino acid substitutions that may have occurred during the supposed adaptation of SVDV to a new host onto the structure of SVDV and a model of the SVDV/CAR complex generated by reference to the cryo-electron microscopy-visualized complex of CBV3 and CAR. The changes fall into three clusters as follows: one lines the fivefold pore, a second maps to the CAR-binding site and partially overlaps the site for decay accelerating factor (DAF) to bind to echovirus 7 (ECHO7), and the third lies close to the fivefold axis, where the low-density lipoprotein receptor binds to the minor group of rhinoviruses. Later changes in SVDV (post-1971) map to the first two clusters and may, by optimizing recognition of a pig CAR and/or DAF homologue, have improved the adaptation of the virus to pigs.

PubMed: 12692248
DOI: 10.1128/JVI.77.9.5475-5486.2003

Experimental method

X-RAY DIFFRACTION (3 Å)