PMID- 21900158
OWN - NLM
STAT- MEDLINE
DCOM- 20111216
LR  - 20220330
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 85
IP  - 22
DP  - 2011 Nov
TI  - Crystal structure of swine major histocompatibility complex class I SLA-1 0401 
      and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic 
      T lymphocyte epitope peptides.
PG  - 11709-24
LID - 10.1128/JVI.05040-11 [doi]
AB  - The presentation of viral epitopes to cytotoxic T lymphocytes (CTLs) by swine 
      leukocyte antigen class I (SLA I) is crucial for swine immunity. To illustrate 
      the structural basis of swine CTL epitope presentation, the first SLA crystal 
      structures, SLA-1 0401, complexed with peptides derived from either 2009 pandemic 
      H1N1 (pH1N1) swine-origin influenza A virus (S-OIV(NW9); NSDTVGWSW) or Ebola 
      virus (Ebola(AY9); ATAAATEAY) were determined in this study. The overall 
      peptide-SLA-1 0401 structures resemble, as expected, the general conformations of 
      other structure-solved peptide major histocompatibility complexes (pMHC). The 
      major distinction of SLA-1 0401 is that Arg(156) has a "one-ballot veto" function 
      in peptide binding, due to its flexible side chain. S-OIV(NW9) and Ebola(AY9) 
      bind SLA-1 0401 with similar conformations but employ different water molecules 
      to stabilize their binding. The side chain of P7 residues in both peptides is 
      exposed, indicating that the epitopes are "featured" peptides presented by this 
      SLA. Further analyses showed that SLA-1 0401 and human leukocyte antigen (HLA) 
      class I HLA-A 0101 can present the same peptides, but in different conformations, 
      demonstrating cross-species epitope presentation. CTL epitope peptides derived 
      from 2009 pandemic S-OIV were screened and evaluated by the in vitro refolding 
      method. Three peptides were identified as potential cross-species influenza virus 
      (IV) CTL epitopes. The binding motif of SLA-1 0401 was proposed, and 
      thermostabilities of key peptide-SLA-1 0401 complexes were analyzed by circular 
      dichroism spectra. Our results not only provide the structural basis of peptide 
      presentation by SLA I but also identify some IV CTL epitope peptides. These 
      results will benefit both vaccine development and swine organ-based 
      xenotransplantation.
FAU - Zhang, Nianzhi
AU  - Zhang N
AD  - Department of Microbiology and Immunology, College of Veterinary Medicine, China 
      Agricultural University, Beijing 100094, China.
FAU - Qi, Jianxun
AU  - Qi J
FAU - Feng, Sijia
AU  - Feng S
FAU - Gao, Feng
AU  - Gao F
FAU - Liu, Jun
AU  - Liu J
FAU - Pan, Xiaocheng
AU  - Pan X
FAU - Chen, Rong
AU  - Chen R
FAU - Li, Qirun
AU  - Li Q
FAU - Chen, Zhaosan
AU  - Chen Z
FAU - Li, Xiaoying
AU  - Li X
FAU - Xia, Chun
AU  - Xia C
FAU - Gao, George F
AU  - Gao GF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110907
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Epitopes, T-Lymphocyte)
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Histocompatibility Antigens Class II)
RN  - 0 (swine leukocyte antigen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Antigen Presentation
MH  - Circular Dichroism
MH  - Crystallography, X-Ray
MH  - Ebolavirus/immunology
MH  - Epitopes, T-Lymphocyte/immunology
MH  - Histocompatibility Antigens Class I/*chemistry
MH  - Histocompatibility Antigens Class II/*chemistry
MH  - Influenza A Virus, H1N1 Subtype/immunology
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Folding
MH  - Protein Stability
MH  - Sequence Homology
MH  - Swine
MH  - T-Lymphocytes, Cytotoxic/*immunology
PMC - PMC3209268
EDAT- 2011/09/09 06:00
MHDA- 2011/12/17 06:00
PMCR- 2012/05/01
CRDT- 2011/09/09 06:00
PHST- 2011/09/09 06:00 [entrez]
PHST- 2011/09/09 06:00 [pubmed]
PHST- 2011/12/17 06:00 [medline]
PHST- 2012/05/01 00:00 [pmc-release]
AID - JVI.05040-11 [pii]
AID - 5040-11 [pii]
AID - 10.1128/JVI.05040-11 [doi]
PST - ppublish
SO  - J Virol. 2011 Nov;85(22):11709-24. doi: 10.1128/JVI.05040-11. Epub 2011 Sep 7.