Characterization and quantitation of peptide-MHC complexes produced from hen egg lysozyme using a monoclonal antibody
Characterization and quantitation of peptide-MHC complexes produced from hen egg lysozyme using a monoclonal antibody
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DOI：
10.1016/s1074-7613(00)80448-3
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发表时间：
1997-06-01
期刊：
影响因子：
32.4
通讯作者：
Unanue, ER
中科院分区：
文献类型：
--
作者：
Dadaglio, G;Nelson, CA;Unanue, ER
在这里，我们描述了Aw3.18的产生，这是一种识别与MHC II类分子I-A(k)结合的鸡蛋溶菌酶（HEL）肽基48-62的单克隆抗体。表位定位显示，Aw3.18检测到在P1位置的肽侧链被取代后，该肽- mhc复合物的溶剂暴露表面发生了变化。此外，Aw3.18阻断了部分（但不是全部）HEL 48-62反应性T细胞杂交瘤的识别，这表明T细胞对该复合物的反应存在异质性。最后，利用Aw3.18可以测定抗原提呈细胞在含HEL的培养基中培养后携带48-62肽的I-A(k)分子的比例。
Here we describe generation of Aw3.18, a monoclonal antibody that recognizes peptide residues 48-62 of hen egg lysozyme (HEL) bound to the MHC class II molecule I-A(k). Epitope mapping revealed that Aw3.18 detects a change in the solvent-exposed surface of this peptide-MHC complex upon substitution of the peptide side chain at position P1. Furthermore, Aw3.18 blocked recognition by some, but not all, of the HEL 48-62-reactive T cell hybridomas tested, suggesting a heterogeneity in the T cell response toward this complex. Finally, using Aw3.18, it was possible to determine the fraction of I-A(k) molecules loaded with 48-62 peptide after culture of an antigen-presenting cell in medium containing HEL.