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01-06-2018 | Original Article

New tetrameric forms of the rotavirus NSP4 with antiparallel helices

Authors: Sushant Kumar, Raghavendra Ramappa, Kiranmayee Pamidimukkala, C. D. Rao, K. Suguna

Published in: Archives of Virology | Issue 6/2018

Abstract

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 α-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.

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Title: New tetrameric forms of the rotavirus NSP4 with antiparallel helices
Authors: Sushant Kumar
Raghavendra Ramappa
Kiranmayee Pamidimukkala
C. D. Rao
K. Suguna
Publication date: 01-06-2018
Publisher: Springer Vienna
Published in: Archives of Virology / Issue 6/2018
Print ISSN: 0304-8608
Electronic ISSN: 1432-8798
DOI: https://doi.org/10.1007/s00705-018-3753-6

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