Klatser P R, De Wit M Y, Kolk A H, Hartskeerl R A
N.H. Swellengrebel Laboratory of Tropical Hygiene, Royal Tropical Institute, Amsterdam, The Netherlands.
Infect Immun. 1991 Jan;59(1):433-6. doi: 10.1128/iai.59.1.433-436.1991.
Using synthetic peptides representing overlapping sequences of the 100-amino-acid-long N-terminal region of the proline-rich antigen of Mycobacterium leprae (PRA), we have mapped the epitopes in the primary structure of PRA recognized by four monoclonal antibodies. The M. leprae-specific monoclonal antibody F47-9 recognized the amino acid sequence LGSAYP (residues 34 to 39). Both monoclonal antibodies F67-1 and F67-5 recognized the sequence YPPP within the repeated sequence of PRA at four sites (residues 38 to 41, 50 to 53, 60 to 63, and 70 to 73). Monoclonal antibody F126-5 recognized the sequence SYPPP, also within the repeat, at three sites (residues 49 to 53, 59 to 63, and 69 to 73). All three epitopes appeared to be linear as far as can be determined by this approach.
利用代表麻风分枝杆菌富含脯氨酸抗原(PRA)100个氨基酸长的N端区域重叠序列的合成肽,我们已在PRA一级结构中定位了四种单克隆抗体识别的表位。麻风分枝杆菌特异性单克隆抗体F47 - 9识别氨基酸序列LGSAYP(第34至39位残基)。单克隆抗体F67 - 1和F67 - 5均在PRA重复序列内的四个位点(第38至41位、50至53位、60至63位和70至73位残基)识别序列YPPP。单克隆抗体F126 - 5在重复序列内的三个位点(第49至53位、59至63位和69至73位残基)识别序列SYPPP。就通过该方法所能确定的而言,所有这三个表位似乎都是线性的。