Analysis of the affinity of influenza A virus protein epitopes for swine MHC I by a modified in vitro refolding method indicated cross-reactivity between swine and human MHC I specificities
Analysis of the affinity of influenza A virus protein epitopes for swine MHC I by a modified in vitro refolding method indicated cross-reactivity between swine and human MHC I specificities
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通过改良的体外重折叠方法分析甲型流感病毒蛋白表位对猪 MHC I 的亲和力,表明猪和人 MHC I 特异性之间存在交叉反应
DOI:
10.1007/s00251-018-1070-6
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发表时间:
2018-07
期刊:
影响因子:
3.2
通讯作者:
Wenshuai Zhu
中科院分区:
文献类型:
--
作者:
Shuhua Fan;Yongli Wang;Xian Wang;Li Huang;Yunxia Zhang;Xiaomeng Liu;Wenshuai Zhu
In vitro refolding assays can be used to investigate the affinity and stability of the binding of epitope peptides to major histocompatibility complex (MHC) class I molecules, which are key factors in the presentation of peptides to cytotoxic T lymphocytes (CTLs). The recognition of peptide epitopes by CTLs is crucial for protection against influenza A virus (IAV) infection. The peptide-binding motif of the swine SLA-3*hs0202 molecule has been previously reported and partly overlaps with the binding motif of the most abundant human MHC allele, HLA-A*0201. In this study, we screened all the protein sequences of the swine-origin epidemic IAV strain A/Beijing/01/2009 (H1N1), and a total of 73 9-mer epitope peptides were predicted to fit the consensus motif of the swine SLA-3*hs0202 or HLA-A*0201 molecule. Then, 14 peptides were selected, and their affinities to SLA-3*hs0202 were tested by a modified in vitro refolding assay. Our results show that ten epitopes could tolerate gel filtration, indicating that these epitopes formed stable or partly stable complexes with SLA-3*hs0202. Eight out of the ten epitopes have been previously reported as HLA-A2-restricted epitopes, which implied cross-reactivity between swine and human MHC I specificities. Furthermore, the modified mini-system refolding method could be applied for the screening of peptides because the refolding efficiency remained almost unchanged with the positive peptide (HA-KMN9) subjected to size-exclusion chromatography and Resource Q anion-exchange chromatography. The results presented here provide new insight into the development of epitope-based vaccines to control IAV and increase our understanding of swine molecular immunology.
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影响因子:
6.7
作者:
Macdonald IK;Harkiolaki M;Hunt L;Connelley T;Carroll AV;MacHugh ND;Graham SP;Jones EY;Morrison WI;Flower DR;Ellis SA
通讯作者:
Ellis SA
影响因子:
5.4
作者:
Nianzhi Zhang;J. Qi;Sijia Feng;F. Gao;Jun Liu;X. Pan;Rong Chen;Qirun Li;Zhaosan Chen;
通讯作者:
Nianzhi Zhang;J. Qi;Sijia Feng;F. Gao;Jun Liu;X. Pan;Rong Chen;Qirun Li;Zhaosan Chen;
影响因子:
3.6
作者:
Fan, Shuhua;Wang, Yongli;Xia, Chun
通讯作者:
Xia, Chun
DOI:
10.1073/pnas.1013387107
发表时间:
2010-11-02
影响因子:
11.1
作者:
Wang, Taia T.;Tan, Gene S.;Palese, Peter
通讯作者:
Palese, Peter
影响因子:
--
作者:
Harndahl, Mikkel;Justesen, Sune;Buus, Soren
通讯作者:
Buus, Soren