Structure of the capsid amino-terminal domain from the betaretrovirus, jaagsiekte sheep retrovirus

Mortuza, G.B., Goldstone, D.C., Pashley, C., Haire, L.F., Palmarini, M. , Taylor, W.R., Stoye, J.P. and Taylor, I.A. (2009) Structure of the capsid amino-terminal domain from the betaretrovirus, jaagsiekte sheep retrovirus. Journal of Molecular Biology, 386(4), pp. 1179-1192. (doi: 10.1016/j.jmb.2008.10.066)

Abstract

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.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Palmarini, Professor Massimo and Stoye, Dr Jonathan
• Authors: Mortuza, G.B., Goldstone, D.C., Pashley, C., Haire, L.F., Palmarini, M., Taylor, W.R., Stoye, J.P., and Taylor, I.A.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity; College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
• Journal Name: Journal of Molecular Biology
• ISSN: 0022-2836