ArticleVirus research2011
Identification of non-essential regions in nucleocapsid protein of porcine reproductive and respiratory syndrome virus for replication in cell culture.
Article in Virus research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Reverse genetics construction and pathogenicity of a novel recombinant NADC30-like PRRSV isolated in China.Frontiers in veterinary science · 2024Article
- Research Progress on NSP11 of Porcine Reproductive and Respiratory Syndrome Virus.Veterinary sciences · 2023Review
- A novel amino acid site of N protein could affect the PRRSV-2 replication by regulating the viral RNA transcription.BMC veterinary research · 2022Article
- Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function.Veterinary microbiology · 2018Article
- Article
- Engineering the PRRS virus genome: updates and perspectives.Veterinary microbiology · 2014Review
- Use of reverse genetics to develop a novel marker porcine reproductive and respiratory syndrome virus.Virus genes · 2012Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleocapsid (N) protein of porcine reproductive and respiratory syndrome virus (PRRSV) plays a central role in virus replication. In this study, serial N- and C-terminal truncations of N protein were performed in the context of type 2 PRRSV infectious cDNA clone, and our results revealed that a stretch of inter-genotypic variable N terminal residues aa 5-13 ((5)NGKQQKKK(13)K) and the last four inter-genotypic variable aa residues ((120)SPS(123)A) at the C terminus of N protein were dispensable for type 2 PRRSV infectivity. All the recovered deletion mutant viruses had spontaneous mutations in the N coding region, including substitution, deletion and insertion. We re-engineered the additional internal deletion with or without the original C-terminal deletion back into wild-type APRRS and found that the internal domain spanning the inter-genotypic variable residues 39-42 ((39)KGP(42)G) and conserved residues 48-52 ((48)KNPE(52)K), respectively, were dispensable for type 2 PRRSV viability. These results demonstrated that N protein contains non-essential regions for virus viability in cell culture. Such dispensable regions could be utilized as insertion site for foreign tag expression and the rescued viruses could be the candidates for marker vaccine.
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Registered trials
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