PMID- 35546407
OWN - NLM
STAT- MEDLINE
DCOM- 20220517
LR  - 20220531
IS  - 1746-6148 (Electronic)
IS  - 1746-6148 (Linking)
VI  - 18
IP  - 1
DP  - 2022 May 11
TI  - A novel amino acid site of N protein could affect the PRRSV-2 replication by 
      regulating the viral RNA transcription.
PG  - 171
LID - 10.1186/s12917-022-03274-9 [doi]
LID - 171
AB  - BACKGROUND: Finding the key amino acid sites that could affect viral 
      biological properties or protein functions has always been a topic of substantial 
      interest in virology. The nucleocapsid (N) protein is one of the principal 
      proteins of the porcine reproductive and respiratory syndrome virus (PRRSV) and 
      plays a vital role in the virus life cycle. The N protein has only 123 or 128 
      amino acids, some of key amino acid sites which could affect the protein 
      functions or impair the viral biological characteristics have been identified. In 
      this research, our objective was to find out whether there are other novel amino 
      acid sites of the N protein can affect N protein functions or PRRSV-2 
      replication. RESULTS: In this study, we found mutated the serine(78) and serine 
      (99)of the nucleocapsid (N) protein can reduce the N-induced expression of IL-10 
      mRNA; Then, by using reverse genetics system, we constructed and rescued the 
      mutant viruses, namely, A78 and A99.The IFA result proved that the mutations did 
      not affect the rescue of the PRRSV-2. However, the results of the multistep 
      growth kinetics and qPCR assays indicated that, compared with the viral 
      replication ability, the titres and gRNA levels of A78 were significantly 
      decreased compared with the wild-type. Further study showed that a single amino 
      acid change from serine to alanine at position 78 of the N protein could 
      abrogates the level of viral genomic and subgenomic RNAs. It means the mutation 
      could significant decrease the viral replication efficiency in vitro. 
      CONCLUSIONS: Our results suggest that the serine(78) of N protein is a key site 
      which could affect the N protein function and PRRSV replication ability.
CI  - (c) 2022. The Author(s).
FAU - Deng, Hua
AU  - Deng H
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China.
FAU - Xin, Ning
AU  - Xin N
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China.
FAU - Zeng, Fancong
AU  - Zeng F
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China.
FAU - Wen, Feng
AU  - Wen F
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China.
FAU - Yi, Heyou
AU  - Yi H
AD  - MOA Key Laboratory of Animal Vaccine Development, Ministry of Agriculture, 
      College of Veterinary Medicine, South China Agricultural University, Guangzhou, 
      510642, People's Republic of China.
FAU - Ma, Chunquan
AU  - Ma C
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China.
FAU - Huang, Shujian
AU  - Huang S
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China.
FAU - Zhang, Guihong
AU  - Zhang G
AD  - MOA Key Laboratory of Animal Vaccine Development, Ministry of Agriculture, 
      College of Veterinary Medicine, South China Agricultural University, Guangzhou, 
      510642, People's Republic of China. guihongzh@scau.edu.cn.
FAU - Chen, Yao
AU  - Chen Y
AD  - School of Life Science and Engineering, Foshan University, Foshan, 528000, 
      People's Republic of China. yaochenvet@fosu.edu.cn.
LA  - eng
GR  - No. 31872489/National Natural Science Foundation of China/
GR  - No.2019A1515110056/GuangDong Basic and Applied Basic Research Foundation/
PT  - Journal Article
DEP - 20220511
PL  - England
TA  - BMC Vet Res
JT  - BMC veterinary research
JID - 101249759
RN  - 0 (Amino Acids)
RN  - 0 (Nucleocapsid Proteins)
RN  - 0 (RNA, Viral)
RN  - 452VLY9402 (Serine)
SB  - IM
MH  - Amino Acids/chemistry/metabolism
MH  - Animals
MH  - Cell Line
MH  - Nucleocapsid Proteins/chemistry/genetics/metabolism
MH  - *Porcine Reproductive and Respiratory Syndrome/virology
MH  - *Porcine respiratory and reproductive syndrome virus/genetics
MH  - RNA, Viral/genetics
MH  - Serine/chemistry
MH  - Swine
MH  - *Swine Diseases
MH  - Virus Replication/physiology
PMC - PMC9092334
OTO - NOTNLM
OT  - IL-10
OT  - Nucleocapsid protein
OT  - Porcine reproductive and respiratory syndrome virus (PRRSV)
OT  - Replication ability
COIS- All authors state that they have no conflicts of interests.
EDAT- 2022/05/14 06:00
MHDA- 2022/05/18 06:00
PMCR- 2022/05/11
CRDT- 2022/05/13 01:45
PHST- 2022/02/12 00:00 [received]
PHST- 2022/04/22 00:00 [accepted]
PHST- 2022/05/13 01:45 [entrez]
PHST- 2022/05/14 06:00 [pubmed]
PHST- 2022/05/18 06:00 [medline]
PHST- 2022/05/11 00:00 [pmc-release]
AID - 10.1186/s12917-022-03274-9 [pii]
AID - 3274 [pii]
AID - 10.1186/s12917-022-03274-9 [doi]
PST - epublish
SO  - BMC Vet Res. 2022 May 11;18(1):171. doi: 10.1186/s12917-022-03274-9.