TY - JOUR

T1 - The shift from low to high non-structural protein 1 expression in rotavirus-infected MA-104 cells

AU - Martínez-Álvarez, Laura

AU - Piña-Vázquez, Carolina

AU - Zarco, Wilbert

AU - Padilla-Noriega, Luis

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Animals

KW - Capsid Proteins/metabolism

KW - Cell Line

KW - Gene Expression Regulation, Viral

KW - Guinea Pigs

KW - RNA, Viral/genetics

KW - Rotavirus/metabolism

KW - Viral Nonstructural Proteins/metabolism

KW - Virus Replication

U2 - 10.1590/S0074-0276108042013005

DO - 10.1590/S0074-0276108042013005

M3 - Journal article

C2 - 23827992

VL - 108

SP - 421

EP - 428

JO - Memórias do Instituto Oswaldo Cruz

JF - Memórias do Instituto Oswaldo Cruz

SN - 0074-0276

IS - 4

ER -