Structure and Function of the Parvoviral NS1 Protein: a Review

Overview

Journal Virus Genes

Specialties Microbiology
Molecular Biology

Date 2022 Oct 17

PMID 36253516

Authors

Qianqian Xie

Jigui Wang

Chenchen Gu

Jing Wu

Weiquan Liu

Affiliations

Soon will be listed here.

Abstract

Parvoviruses possess a single-stranded DNA genome of about 5 kb, which contains two open reading frames (ORFs), one encoding nonstructural (NS) proteins, the other capsid proteins. The NS1 protein contains an N-terminal origin-binding domain, a helicase domain, and a C-terminal transactive domain, and is essential for effective viral replication and production of infectious virus. We first summarize the developments in the structure of NS1 protein, including the original binding domain and the helicase domain. We discuss the role of different DNA substrates in the oligomerization of these two domains of NS1. During the parvovirus life cycle, the NS1 protein is closely related to the viral gene expression, viral replication, and infection. We provide the current understanding of the impact of parvovirus NS1 protein mutations on its biological properties. Overall, in this review, we focus on the structure and function of the parvoviral NS1 protein.

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