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Hyper-phosphorylation of nsp2-related proteins of porcine reproductive and respiratory syndrome virus.

Abstract：

:Viruses exploit phosphorylation of both viral and host proteins to support viral replication. In this study, we demonstrate that porcine reproductive and respiratory syndrome virus replicase nsp2, and two nsp2-related -2/-1 frameshifting products, nsp2TF and nsp2N, are hyper-phosphorylated. By mapping phosphorylation sites, we subdivide an extended, previously uncharacterized region, located between the papain-like protease-2 (PLP2) domain and frameshifting site, into three distinct domains. These domains include two large hypervariable regions (HVR) with putative intrinsically disordered structures, separated by a conserved and partly structured interval domain that we defined as the inter-HVR conserved domain (IHCD). Abolishing phosphorylation of the inter-species conserved residue serine918, which is located within the IHCD region, abrogates accumulation of viral genomic and subgenomic RNAs and recombinant virus production. Our study reveals the biological significance of phosphorylation events in nsp2-related proteins, emphasizes pleiotropic functions of nsp2-related proteins in the viral life cycle, and presents potential links to pathogenesis.

journal_name

Virology

journal_title

Virology

authors

Shang P,Yuan F,Misra S,Li Y,Fang Y

doi

10.1016/j.virol.2020.01.018

subject

Has Abstract

pub_date

2020-04-01 00:00:00

pages

63-75

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(20)30024-6

journal_volume

543

pub_type

杂志文章

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