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J Mol Biol. 2009 Mar 6;386(4):1179-92. doi: 10.1016/j.jmb.2008.10.066. Epub 2008 Nov 5.

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

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  • 1Division of Molecular Structure, National Institute for Medical Research, the Ridgeway, Mill Hill, London NW7 1AA, UK.


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.

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