Tanaka Y, Zeng L, Shiraki H, Shida H, Tozawa H
Department of Immunology, School of Hygienic Sciences, Kitasato University, Kanagawa, Japan.
J Immunol. 1991 Jul 1;147(1):354-60.
We have generated a number of mAb against various epitopes on the external envelope glycoprotein, gp46, of human T cell leukemia virus type I (HTLV-I) from a WKA rat immunized with a recombinant vaccinia virus containing the HTLV-I env gene. Among these mAb, one group of mAb, represented by a mAb designated LAT-27, could neutralize the infectivity of HTLV-I, as determined by a HTLV-I-mediated cell fusion inhibition assay. LAT-27 also interfered with transformation of normal T lymphocytes by HTLV-I in vitro. An antibody-binding assay using overlapping synthetic oligopeptides showed that LAT-27 bound specifically to 10-mer peptides that contained the gp46 amino acid sequence 191-196 (Leu-Pro-His-Ser-Asn-Leu). Antibodies from HTLV-I+ humans interfered with the binding of LAT-27 to gp46 Ag. Sera from rabbits immunized with a LAT-27-reactive peptide, 190-199, conjugated with OVA, but not sera from OVA-immunized rabbits, reacted with gp46 Ag and neutralized infectivity of HTLV-I. These results show that the HTLV-I neutralization epitope recognized by LAT-27 locates to the gp46 amino acids 191-196, and that immunization with a peptide containing the LAT-27 epitope can elicit an HTLV-I neutralizing antibody response.
我们用含有人类I型T细胞白血病病毒（HTLV-I）env基因的重组痘苗病毒免疫一只WKA大鼠，产生了许多针对HTLV-I外膜糖蛋白gp46上各种表位的单克隆抗体（mAb）。在这些mAb中，一组以名为LAT-27的mAb为代表，通过HTLV-I介导的细胞融合抑制试验测定，它能够中和HTLV-I的感染性。LAT-27在体外也能干扰HTLV-I对正常T淋巴细胞的转化。使用重叠合成寡肽的抗体结合试验表明，LAT-27特异性结合包含gp46氨基酸序列191 - 196（亮氨酸-脯氨酸-组氨酸-丝氨酸-天冬酰胺-亮氨酸）的10肽。来自HTLV-I阳性人类的抗体干扰LAT-27与gp46抗原的结合。用与卵清蛋白（OVA）偶联的LAT-27反应性肽190 - 199免疫的兔血清，而不是OVA免疫兔的血清，与gp46抗原反应并中和HTLV-I的感染性。这些结果表明，LAT-27识别的HTLV-I中和表位位于gp46的191 - 196氨基酸处，并且用含有LAT-27表位的肽进行免疫可引发HTLV-I中和抗体反应。
