IDENTIFICATION, SYNTHESIS AND IMMUNOGENICITY OF CUTICULAR COLLAGENS FROM THE FILARIAL NEMATODES BRUGIA-MALAYI AND BRUGIA-PAHANGI
IDENTIFICATION, SYNTHESIS AND IMMUNOGENICITY OF CUTICULAR COLLAGENS FROM THE FILARIAL NEMATODES BRUGIA-MALAYI AND BRUGIA-PAHANGI
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DOI：
10.1016/0166-6851(89)90073-x
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发表时间：
1989-01-15
影响因子：
1.5
通讯作者：
MAIZELS, RM
中科院分区：
文献类型：
--
作者：
SELKIRK, ME;NIELSEN, L;MAIZELS, RM
用外源性碘标记和梭状芽胞杆菌胶原酶敏感性鉴定了丝虫寄生线虫马来丝虫和帕汉布氏丝虫角质层的主要结构蛋白。用双向电泳法从成虫中鉴定出至少16种酸性成分，分子量在35 000~160 000之间。这些蛋白质似乎是通过二硫键交联的，并定位于角质层的基底层和内皮质。外层皮质含有表皮层，不溶于1%十二烷基硫酸钠和5%2-巯基乙醇，不含细胞物质。尽管在完整的蠕虫中它们无法进入免疫系统，但角质胶原蛋白的抗体在感染了各种丝虫的人类中被激发。免疫交叉反应表明，35 kDa组分与人IV型(基底膜)胶原蛋白发生交叉反应。在一些淋巴丝虫病患者中检测到了IV型胶原的自身抗体，尽管与观察到的病理结果没有相关性。与秀丽隐杆线虫不同，角质层胶原蛋白的合成是不连续的，在成熟的成年雄虫中发生的水平可以忽略不计，而且似乎不涉及小分子前体的产生。与编码鸡1型胶原α2链的异源cDNA探针杂交表明，它们是由一个多基因家族编码的。
The major structural proteins of the cuticle of the filarial nematode parasites Brugia malayi and Brugia pahangi were identified by extrinsic iodination and sensitivity to clostridial collagenase. At least 16 acidic components were identified in adult worms by 2-dimensional electrophoresis, with molecular weights ranging from 35 000 to 160 000. These proteins appear to be cross-linked by disulphide bonds, and localised in the basal and inner cortical layer of the cuticle. The outer cortex, containing the epicuticle, is insoluble in 1% sodium dodecyl sulphate and 5% 2-mercaptoethanol, and can be isolated free of cellular material. Despite their inaccessibility to the immune system in intact worms, antibodies to the cuticular collagens are provoked in humans infected with a variety of filarial parasites. Immunological cross-reactivity was demonstrated between a 35 kDa component and human type IV (basement membrane) collagen. Autoantibodies to type IV collagen were detected in a number of individuals with lymphatic filariasis, although no correlation could be drawn with observed pathology. Synthesis of cuticular collagens is discontinuous, occurs at negligible levels in mature adult male worms and does not appear to involve the production of small molecular weight precursors, in contrast to Caenorhabditis elegans. Hybridization with a heterologous cDNA probe coding for the .alpha.2 chain of chicken type 1 collagen suggests that they are encoded by a multigene family.