Structure of the capsid amino-terminal domain from the betaretrovirus, Jaagsiekte sheep retrovirus.
Jaagsiekte sheep retrovirus is a betaretrovirus and the causative agent of pulmonary adenocarcinoma, a transmissible lung tumour of sheep. Here we report the crystal structure of the capsid amino-terminal domain and examine the self-association properties of Jaagsiekte sheep retrovirus capsid. We find that the structure is remarkably similar to the amino-terminal domain of the alpharetrovirus, avian leukosis virus, revealing a previously undetected evolutionary similarity. Examination of capsid self-association suggests a mode of assembly not driven by the strong capsid carboxy-terminal domain interactions that characterise capsid assembly in the lentiviruses. Based on these data, we propose this structure provides a model for the capsid of betaretroviruses including the HML-2 family of endogenous human betaretroviruses.
Mortuza
Gulnahar B
GB
Division of Molecular Structure, National Institute for Medical Research, the Ridgeway, Mill Hill, London NW7 1AA, UK.
Goldstone
David C
DC
Pashley
Clare
C
Haire
Lesley F
LF
Palmarini
Massimo
M
Taylor
William R
WR
Stoye
Jonathan P
JP
Taylor
Ian A
IA
D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D022141:Jaagsiekte sheep retrovirus / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions
D036022:Capsid Proteins; D012996:Solutions