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New tetrameric forms of the rotavirus NSP4 with antiparallel helices

Kumar, Sushant and Ramappa, Raghavendra and Pamidimukkala, Kiranmayee and Rao, C D and Suguna, K (2018) New tetrameric forms of the rotavirus NSP4 with antiparallel helices. In: ARCHIVES OF VIROLOGY, 163 (6). pp. 1531-1547.

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Official URL: http://dx.doi.org/10.1007/s00705-018-3753-6


Rotavirus nonstructural protein 4, the first viral enterotoxin to be identified, is a multidomain, multifunctional glycoprotein. Earlier, we reported a Ca2+-bound coiled-coil tetrameric structure of the diarrhea-inducing region of NSP4 from the rotavirus strains SA11 and I321 and a Ca2+-free pentameric structure from the rotavirus strain ST3, all with a parallel arrangement of alpha-helices. pH was found to determine the oligomeric state: a basic pH favoured a tetramer, whereas an acidic pH favoured a pentamer. Here, we report two novel forms of the coiled-coil region of NSP4 from the bovine rotavirus strains MF66 and NCDV. These crystallized at acidic pH, forming antiparallel coiled-coil tetrameric structures without any bound Ca2+ ion. Structural and mutational studies of the coiled-coil regions of NSP4 revealed that the nature of the residue at position 131 (Tyr/His) plays an important role in the observed structural diversity.

Item Type: Journal Article
Additional Information: Copy right for this article belong to SPRINGER WIEN, SACHSENPLATZ 4-6, PO BOX 89, A-1201 WIEN, AUSTRIA
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Microbiology & Cell Biology
Depositing User: Id for Latest eprints
Date Deposited: 05 Jun 2018 14:07
Last Modified: 05 Jun 2018 14:07
URI: http://eprints.iisc.ac.in/id/eprint/59944

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