Verreck F A, van de Poel A, Termijtelen A, Amons R, Drijfhout J W, Koning F
Department of Immunohematology and Bloodbank, University Hospital, Leiden, The Netherlands.
Eur J Immunol. 1994 Feb;24(2):375-9. doi: 10.1002/eji.1830240216.
Molecules of the major histocompatibility complex (MHC) present antigenic peptides to T cells. Sequencing peptide pools eluted from MHC class I molecules has established allele-specific peptide binding motifs. We applied pool sequencing to analyze human MHC class II-bound peptides and found that HLA-DQ2-eluted peptides predominantly contained lysine, isoleucine, and phenylalanine at relative position i, i + 3 and i + 8, respectively. These residues putatively represent anchor residues for MHC binding. Analysis of a heterogeneous HLA-DPw3/DPw4-eluted peptide pool yielded a sequence matching an epitope from the endogenous enzyme glyceraldehyde-3-phosphate dehydrogenase. This self-peptide and a partially identical, known allo-epitope bound specifically to DPw3 and DR13 molecules, suggesting the sharing of a binding motif. In particular, the presence of an arginine at relative position 4 appeared important for binding to these HLA class II specificities. Thus, pool sequencing is applicable for the analysis of MHC class II-eluted peptides.
主要组织相容性复合体（MHC）分子将抗原肽呈递给T细胞。对从MHC I类分子洗脱的肽池进行测序已确定了等位基因特异性肽结合基序。我们应用池测序法分析人类MHC II类结合肽，发现从HLA-DQ2洗脱的肽在相对位置i、i + 3和i + 8处分别主要含有赖氨酸、异亮氨酸和苯丙氨酸。这些残基推测代表MHC结合的锚定残基。对异质性HLA-DPw3/DPw4洗脱肽池的分析产生了一个与内源性酶甘油醛-3-磷酸脱氢酶的一个表位匹配的序列。这个自身肽和一个部分相同的已知同种异体表位特异性结合DPw3和DR13分子，表明存在一个共享的结合基序。特别是，在相对位置4处存在精氨酸对于与这些HLA II类特异性结合似乎很重要。因此，池测序适用于MHC II类洗脱肽的分析。
