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Processing of SeMV polyproteins revisited

Nair, Smita and Savithri, HS (2010) Processing of SeMV polyproteins revisited. In: Virology, 396 (1). pp. 106-117.

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Processing of Sesbania mosaic virus (SeMV) polyprotein 2a and 2ab was reanalyzed in the view of the new genome organization of sobemoviruses. Polyprotein 2a when expressed in E coli, from the new cDNA clone, got cleaved at the earlier identified sites E325-T326, E402-T403 and E498-S499 to release protease, VPg, P10 and P8, respectively. Additionally, a novel cleavage was identified within the protease domain at position E132-S133, which was found to be essential for efficient polyprotein processing. Products, corresponding to cleavages identified in E. coli, were also detected in infected Sesbania leaves. Interestingly, though the sites are exactly the same in polyprotein 2ab, it got cleaved between Protease-VPg but not between VPg-RdRp. This indicates to a differential cleavage preference, governed probably by the conformation of 2ab. Also, the studies revealed that, in SeMV, processing is regulated by mode of cleavage and context of the cleavage site.

Item Type: Journal Article
Publication: Virology
Publisher: Elsevier Science
Additional Information: copyright of this article belongs to Elsevier Science.
Keywords: Sobemoviruses; Sesbania mosaic virus; Polyprotein processing; Glutamate specific protease; VPg; P10; P8; Cis/trans cleavages
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 09 Jan 2010 05:49
Last Modified: 19 Sep 2010 05:53
URI: http://eprints.iisc.ac.in/id/eprint/25297

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