Structural highlights
Publication Abstract from PubMed
Rotavirus nonstructural protein 4, the first viral enterotoxin to be identified, is a multidomain, multifunctional glycoprotein. Earlier, we reported a Ca(2+)-bound coiled-coil tetrameric structure of the diarrhea-inducing region of NSP4 from the rotavirus strains SA11 and I321 and a Ca(2+)-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 Ca(2+) 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.
New tetrameric forms of the rotavirus NSP4 with antiparallel helices.,Kumar S, Ramappa R, Pamidimukkala K, Rao CD, Suguna K Arch Virol. 2018 Feb 17. pii: 10.1007/s00705-018-3753-6. doi:, 10.1007/s00705-018-3753-6. PMID:29455326[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumar S, Ramappa R, Pamidimukkala K, Rao CD, Suguna K. New tetrameric forms of the rotavirus NSP4 with antiparallel helices. Arch Virol. 2018 Feb 17. pii: 10.1007/s00705-018-3753-6. doi:, 10.1007/s00705-018-3753-6. PMID:29455326 doi:http://dx.doi.org/10.1007/s00705-018-3753-6
