Structural studies of orbivirus particles.
We are using crystallographic methods to investigate the structure of AHSV and BTV. Our initial approach was to investigate the structure of the major protein component of the viral core, VP7(T13). This trimeric protein has been studied in several crystal forms from both orbiviruses and reveals a structure made up of conserved domains, capable of conformational changes and possessing a cleavage site. Further crystallographic analyses of native particles have provided a picture of the VP7(T13) and VP3(T2) layers of the BTV core. The VP7(T13) layer consists of 260 trimers arranged rather symmetrically and possessing very similar structures, thereby following the rules of quasi equivalence. The VP3(T2) layer is thin and contains 120 copies of 100 kDa protein arranged as 60 approximate dimers. This type of icosahedral construction has not been observed before and appears to contain a genome which is highly ordered. We anticipate that all of these features will be common to AHSV.
Stuart
D I
DI
Oxford Center for Molecular Sciences, New Chemistry Laboratory, U.K.
Gouet
P
P
Grimes
J
J
Malby
R
R
Diprose
J
J
Zientara
S
S
Burroughs
J N
JN
Mertens
P P
PP
D000356:African Horse Sickness Virus / Q000737:chemistry*; D000818:Animals; D000956:Antigens, Viral / Q000737:chemistry; D001820:Bluetongue virus / Q000737:chemistry*; D003461:Crystallography; D011487:Protein Conformation; D014758:Viral Core Proteins / Q000737:chemistry; D015678:Viral Structural Proteins / Q000737:chemistry*; D014771:Virion / Q000737:chemistry*
D000956:Antigens, Viral; C113737:VP3 protein, African horse sickness virus; D014758:Viral Core Proteins; D015678:Viral Structural Proteins; C069264:VP7 major core antigen, African horsesickness virus