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Review
. 2022 Jul 11:9:872205.
doi: 10.3389/fvets.2022.872205. eCollection 2022.

Research Progress on the NSP9 Protein of Porcine Reproductive and Respiratory Syndrome Virus

Affiliations
Review

Research Progress on the NSP9 Protein of Porcine Reproductive and Respiratory Syndrome Virus

Huiyang Sha et al. Front Vet Sci. .

Abstract

Porcine reproductive and respiratory syndrome (PRRS) is a contagious disease caused by the porcine reproductive and respiratory syndrome virus (PRRSV). PRRS is also called "blue ear disease" because of the characteristic blue ear in infected sows and piglets. Its main clinical features are reproductive disorders of sows, breathing difficulties in piglets, and fattening in pigs, which cause considerable losses to the swine industry. NSP9, a non-structural protein of PRRSV, plays a vital role in PRRSV replication and virulence because of its RNA-dependent RNA polymerase (RdRp) structure. The NSP9 sequence is highly conserved and contains T cell epitopes, which are beneficial for the development of future vaccines. NSP9 acts as the protein interaction hub between virus and host during PRRSV infection, especially in RNA replication and transcription. Herein, we comprehensively review the application of NSP9 in terms of genetic evolution analysis, interaction with host proteins that affect virus replication, interaction with other viral proteins, pathogenicity, regulation of cellular immune response, antiviral drugs, vaccines, and detection methods. This review can therefore provide innovative ideas and strategies for PRRSV prevention and control.

Keywords: NSP9; PRRSV; RdRp; pathogenicity; protein interaction.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Structure diagram of NSP9 of PRRSV. N-terminal is linked to NSP8 and contains a newly discovered nucleotide transferase domain (NiRAN) related to pancreatic virus RdRp, and C-terminal contains the RdRP domain.
Figure 2
Figure 2
A neighbor-joining phylogenetic tree was constructed based on the NSP9 sequences of 20 PRRSV strains, using MEGA software (ver. 7.0; Center for Evolutionary Medicine and Informatics, Tempe, AZ) with 1000 bootstrap replicates.
Figure 3
Figure 3
The NSP9 of PRRSV and non-structural proteins with host proteins mentioned in this paragraph. In addition to the host protein, it is also shown that the N protein related to the production of IFN-I also interacts with NSP9.

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