| Literature DB >> 9015101 |
K Taniguchi1, K Kojima, N Kobayashi, T Urasawa, S Urasawa.
Abstract
Studies on the structure and function of the nonstructural proteins (NSP1-NSP5) of rotaviruses are important for dissection of the morphogenesis and replication processes of rotavirus. Above all, NSP1, the product of gene 5, has several interesting features, such as extreme sequence diversity, a highly conserved cysteine-rich region, RNA-binding activity, accumulation on the cytoskeleton, and non-random segregation in reassortment. Recently, comparable NSP1 sequence analysis has been performed on a number of rotavirus strains from various species. Furthermore, characterization of mutants with rearranged NSP1 genes has helped to elucidate the structure-function interaction of NSP1. We isolated and characterized two interesting mutants which have a large deletion including the cysteine-rich region or a nonsense codon at the early portion in the open reading frame (ORF) of the NSP1 gene. In this report, we summarize the structure and function of NSP1.Entities:
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Year: 1996 PMID: 9015101 DOI: 10.1007/978-3-7091-6553-9_6
Source DB: PubMed Journal: Arch Virol Suppl ISSN: 0939-1983