Anderson D C, Barry M E, Buchanan T M
Department of Pathobiology, University of Washington, Seattle, WA 98195.
J Immunol. 1988 Jul 15;141(2):607-13.
With the use of solid phase synthesis of peptides corresponding to major and minor peaks in a Hopp-Woods hydrophilicity plot, the epitopes for 10 of 14 known different mAb to the Mycobacterium leprae 65-kDa protein, a prominent T and B cell Ag of this bacillus, have been located in the primary structure. Five epitopes have been precisely mapped by using the synthetic peptides in inhibition ELISA experiments, and five others have been located on peptides of 22 amino acids or less in length. The epitope of an important species-specific antibody, IIIE9, which may be useful for seriodiagnosis of leprosy, appears to be distinguished from the epitope of the antibody IVD2, widely cross-reactive among mycobacteria, not by its sequence, but only by its critical residues. All epitopes studied appear continuous insofar as can be determined by this approach.
通过使用固相合成法合成与霍普-伍兹亲水性图中主要和次要峰相对应的肽段，已在14种已知的针对麻风分枝杆菌65 kDa蛋白（该杆菌突出的T和B细胞抗原）的不同单克隆抗体中的10种的表位定位在了一级结构中。通过在抑制ELISA实验中使用合成肽段，精确绘制了5个表位的图谱，另外5个表位位于长度为22个氨基酸或更少的肽段上。一种重要的种特异性抗体IIIE9的表位，可能对麻风病的血清学诊断有用，它似乎与在分枝杆菌中广泛交叉反应的抗体IVD2的表位不同，不是通过其序列，而是仅通过其关键残基。就这种方法所能确定的而言，所有研究的表位似乎都是连续的。
