PMID- 31969884
OWN - NLM
STAT- MEDLINE
DCOM- 20201116
LR  - 20201116
IS  - 1664-3224 (Electronic)
IS  - 1664-3224 (Linking)
VI  - 10
DP  - 2019
TI  - Illumination of PRRSV Cytotoxic T Lymphocyte Epitopes by the Three-Dimensional 
      Structure and Peptidome of Swine Lymphocyte Antigen Class I (SLA-I).
PG  - 2995
LID - 10.3389/fimmu.2019.02995 [doi]
LID - 2995
AB  - To investigate CTL epitope applications in swine, SLA-1(*)1502-restricted peptide 
      epitopes matching porcine reproductive and respiratory syndrome virus (PRRSV) 
      strains were explored by crystallography, biochemistry, and the specific 
      pathogen-free (SPF) swine experiments. First, nine predicted PRRSV peptides were 
      tested by assembly of the peptide-SLA-1(*)1502 (pSLA-1(*)1502) complexes, and the 
      crystal structure of the SLA-1(*)1502 complex with one peptide (NSP9-TMP9) was 
      determined. The NSP9-TMP9 peptide conformation presented by pSLA-1(*)1502 is 
      different from that of the peptides presented by the known pSLA-1(*)0401 and 
      pSLA-3(*)hs0202 complexes. Two consecutive Pro residues make the turn between P3 
      and P4 of NSP9-TMP9 much sharper. The D pocket of pSLA-1(*)1502 is unique and is 
      important for peptide binding. Next, the potential SLA-1(*)1502-restricted 
      peptide epitopes matching four typical genetic PRRSV strains were identified 
      based on the peptide-binding motif of SLA-1(*)1502 determined by structural 
      analysis and alanine scanning of the NSP9-TMP9 peptide. The tetrameric complex of 
      SLA-1(*)1502 and NSP9-TMP9 was constructed and examined. Finally, taking 
      NSP9-TMP9 as an example, the CTL immunogenicity of the identified PRRSV peptide 
      epitope was evaluated. The SPF swine expressing the SLA-1(*)1502 alleles were 
      divided into three groups: modified live vaccine (MLV), MLV+NSP9-TMP9, and the 
      blank control group. NSP9-TMP9 was determined as a PRRSV CTL epitope with strong 
      immunogenicity by flow cytometry and IFN-gamma expression. Our study developed an 
      integrated approach to identify SLA-I-restricted CTL epitopes from various 
      important viruses and is helpful in designing and applying effective 
      peptide-based vaccines for swine.
CI  - Copyright (c) 2020 Pan, Zhang, Wei, Jiang, Chen, Li, Liang, Zhang, Ma and Xia.
FAU - Pan, Xiaocheng
AU  - Pan X
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
AD  - Institute of Animal Husbandry and Veterinary Science, Anhui Academy of 
      Agricultural Science, Hefei, China.
FAU - Zhang, Nianzhi
AU  - Zhang N
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Wei, Xiaohui
AU  - Wei X
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Jiang, Yinan
AU  - Jiang Y
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Chen, Rong
AU  - Chen R
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Li, Qirun
AU  - Li Q
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Liang, Ruiying
AU  - Liang R
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Zhang, Lijie
AU  - Zhang L
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Ma, Lizhen
AU  - Ma L
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
FAU - Xia, Chun
AU  - Xia C
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing, China.
AD  - Key Laboratory of Animal Epidemiology of the Ministry of Agriculture, China 
      Agricultural University, Beijing, China.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20200108
PL  - Switzerland
TA  - Front Immunol
JT  - Frontiers in immunology
JID - 101560960
RN  - 0 (Epitopes, T-Lymphocyte)
RN  - 0 (Peptides)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Epitopes, T-Lymphocyte/*chemistry/*immunology
MH  - Hydrogen Bonding
MH  - Models, Molecular
MH  - Peptides/*chemistry/*immunology
MH  - Porcine Reproductive and Respiratory Syndrome/*immunology/virology
MH  - Porcine respiratory and reproductive syndrome virus/*immunology
MH  - Protein Conformation
MH  - Protein Folding
MH  - Protein Multimerization
MH  - Spectrum Analysis
MH  - Structure-Activity Relationship
MH  - Swine
MH  - T-Lymphocytes, Cytotoxic/*immunology/*metabolism
PMC - PMC6960135
OTO - NOTNLM
OT  - CTL
OT  - PRRSV
OT  - SLA
OT  - epitope
OT  - structure
OT  - vaccine
EDAT- 2020/01/24 06:00
MHDA- 2020/11/18 06:00
PMCR- 2019/01/01
CRDT- 2020/01/24 06:00
PHST- 2018/12/11 00:00 [received]
PHST- 2019/12/05 00:00 [accepted]
PHST- 2020/01/24 06:00 [entrez]
PHST- 2020/01/24 06:00 [pubmed]
PHST- 2020/11/18 06:00 [medline]
PHST- 2019/01/01 00:00 [pmc-release]
AID - 10.3389/fimmu.2019.02995 [doi]
PST - epublish
SO  - Front Immunol. 2020 Jan 8;10:2995. doi: 10.3389/fimmu.2019.02995. eCollection 
      2019.