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Structure and function of the parvoviral NS1 protein: a review

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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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Authors and Affiliations

  1. State Key Laboratory of Agrobiotechnology, Department of Biochemistry and Molecular Biology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China

    Qianqian Xie, Jigui Wang, Chenchen Gu, Jing Wu & Weiquan Liu

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  1. Qianqian Xie
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  2. Jigui Wang
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Contributions

Conceptualization: WL, QX; Writing—original draft preparation: QX; Writing—review and editing: WL, QX, JW; Supervision: CG, WL.

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Correspondence to Weiquan Liu.

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Xie, Q., Wang, J., Gu, C. et al. Structure and function of the parvoviral NS1 protein: a review. Virus Genes 59, 195–203 (2023). https://doi.org/10.1007/s11262-022-01944-2

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