Studies on the structure and function of the nonstructural proteins (N
SP1-NSP5) of rotaviruses are important for dissection of the morphogen
esis and replication processes of rotavirus. Above all, NSP1, the prod
uct of gene 5, has several interesting features, such as extreme seque
nce diversity, a highly conserved cysteine-rich region, RNA-binding ac
tivity, accumulation on the cytoskeleton, and non-random segregation i
n reassortment. Recently, comparable NSP1 sequence analysis has been p
erformed on a number of rotavirus strains from various species. Furthe
rmore, characterization of mutants with rearranged NSP1. genes has hel
ped to elucidate the structure-function interaction of NSP1. We isolat
ed and characterized two interesting mutants which have a large deleti
on 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 rep
ort, we summarize the structure and function of NSP1.