O'Callaghan D, Martineau P, Fayolle C, Leclerc C, Guillet J G, Charbit A, Hofnung M
Programmation Moléculaire et Toxicologie Génétique (CNRS URA 1444), Paris, France.
Vaccine. 1993;11(2):140-2. doi: 10.1016/0264-410x(93)90009-m.
The Escherichia coli maltose-binding protein is a highly versatile carrier protein allowing the construction of genetically engineered hybrid proteins. It accepts large fusions to both C- and N-termini as well as the insertion of shorter peptides at 'permissive sites' within the continuity of the protein. We have genetically inserted immunogenic peptides corresponding to defined viral B- and T-cell epitopes into two permissive sites: one at amino acid site 133, the other at site 303. The hybrid proteins are easily purifiable and immunogenic, inducing peptide-specific B- and T-cell responses. When delivered by live bacteria (E. coli K12 and aroA Salmonella typhimurium) antibody responses can be induced against both the MalE carrier and the inserted B-cell epitope. We discuss the induction of T-cell responses by bacterial delivery systems.
大肠杆菌麦芽糖结合蛋白是一种高度通用的载体蛋白，可用于构建基因工程杂交蛋白。它能接受在C端和N端的大型融合，以及在蛋白质序列内的“允许位点”插入较短的肽段。我们已将对应于特定病毒B细胞和T细胞表位的免疫原性肽段基因插入到两个允许位点：一个在氨基酸位点133，另一个在位点303。这些杂交蛋白易于纯化且具有免疫原性，可诱导肽段特异性的B细胞和T细胞反应。当通过活细菌（大肠杆菌K12和aroA鼠伤寒沙门氏菌）递送时，可诱导针对MalE载体和插入的B细胞表位的抗体反应。我们讨论了细菌递送系统诱导T细胞反应的情况。
