Strug Iwona, Calvo-Calle J Mauricio, Green Karin M, Cruz John, Ennis Francis A, Evans James E, Stern Lawrence J
Department of Pathology, Proteomic and Mass Spectrometry Core Facility, Center for Infectious Disease and Vaccine Research, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
J Proteome Res. 2008 Jul;7(7):2703-11. doi: 10.1021/pr700780x. Epub 2008 May 29.
Class II MHC proteins bind peptides and present them to CD4 (+) T cells as part of the immune system's surveillance of bodily tissues for foreign and pathogenic material. Antigen processing and presentation pathways have been characterized in detail in normal cells, but there is little known about the actual viral peptides that are presented to CD4 (+) T cells that signal infection. In this study, two-dimensional LC-MS/MS was used to identify vaccinia virus-derived peptides among the hundreds to thousands of peptide antigens bound to the human class II MHC protein HLA-DR1 on the surface of vaccinia virus-infected cells. The peptides, derived from the I6L, D6R, and A10L viral proteins, were 15 residues in length, bound efficiently to HLA-DR1 as synthetic peptides, and were recognized by vaccinia-specific CD4 (+) T cells obtained from an immunized donor.
II类主要组织相容性复合体(MHC)蛋白结合肽段,并将其呈递给CD4(+) T细胞,作为免疫系统监测身体组织中异物和致病物质的一部分。抗原加工和呈递途径在正常细胞中已得到详细表征,但对于向发出感染信号的CD4(+) T细胞呈递的实际病毒肽段却知之甚少。在本研究中,二维液相色谱-串联质谱法(2D LC-MS/MS)被用于在痘苗病毒感染细胞表面与人类II类MHC蛋白HLA-DR1结合的成百上千种肽抗原中鉴定源自痘苗病毒的肽段。这些源自I6L、D6R和A10L病毒蛋白的肽段长度为15个氨基酸残基,作为合成肽能有效结合HLA-DR1,并被从免疫供体获得的痘苗病毒特异性CD4(+) T细胞识别。