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)

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Publisher's URL: http://dx.doi.org/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:Stoye, Dr Jonathan and Palmarini, Professor Massimo
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 > Institute of Infection Immunity and Inflammation
Journal Name:Journal of Molecular Biology
ISSN:0022-2836

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