Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico DF, Mexico.
Mem Inst Oswaldo Cruz. 2013 Jun;108(4):421-8. doi: 10.1590/S0074-0276108042013005.
A hallmark of group/species A rotavirus (RVA) replication in MA-104 cells is the logarithmic increase in viral mRNAs that occurs four-12 h post-infection. Viral protein synthesis typically lags closely behind mRNA synthesis but continues after mRNA levels plateau. However, RVA non-structural protein 1 (NSP1) is present at very low levels throughout viral replication despite showing robust protein synthesis. NSP1 has the contrasting properties of being susceptible to proteasomal degradation, but being stabilised against proteasomal degradation by viral proteins and/or viral mRNAs. We aimed to determine the kinetics of the accumulation and intracellular distribution of NSP1 in MA-104 cells infected with rhesus rotavirus (RRV). NSP1 preferentially localises to the perinuclear region of the cytoplasm of infected cells, forming abundant granules that are heterogeneous in size. Late in infection, large NSP1 granules predominate, coincident with a shift from low to high NSP1 expression levels. Our results indicate that rotavirus NSP1 is a late viral protein in MA-104 cells infected with RRV, presumably as a result of altered protein turnover.
群/种 A 轮状病毒(RVA)在 MA-104 细胞中的复制的一个标志是,在感染后 4-12 小时,病毒 mRNA 呈对数增加。病毒蛋白合成通常紧随 mRNA 合成之后,但在 mRNA 水平达到平台期后仍会继续。然而,尽管 RVA 非结构蛋白 1(NSP1)的蛋白合成非常活跃,但在整个病毒复制过程中,其水平一直很低。NSP1 具有相反的特性,即易受蛋白酶体降解,但可被病毒蛋白和/或病毒 mRNA 稳定对抗蛋白酶体降解。我们旨在确定感染恒河猴轮状病毒(RRV)的 MA-104 细胞中 NSP1 的积累和细胞内分布的动力学。NSP1 优先定位于感染细胞的细胞质的核周区,形成丰富的颗粒,大小不均。在感染后期,大的 NSP1 颗粒占主导地位,与 NSP1 表达水平从低到高的转变相一致。我们的结果表明,在感染 RRV 的 MA-104 细胞中,轮状病毒 NSP1 是一种晚期病毒蛋白,可能是由于蛋白质周转的改变所致。