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编码细胞毒性抗链球菌/抗肌球蛋白单克隆抗体36.2.2的V基因序列的分子分析,该抗体可识别心脏细胞表面蛋白层粘连蛋白。

Molecular analysis of V gene sequences encoding cytotoxic anti-streptococcal/anti-myosin monoclonal antibody 36.2.2 that recognizes the heart cell surface protein laminin.

作者信息

Antone S M, Adderson E E, Mertens N M, Cunningham M W

机构信息

Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City 73162, USA.

出版信息

J Immunol. 1997 Dec 1;159(11):5422-30.

PMID:9548482
Abstract

Anti-streptococcal/anti-myosin mAb 36.2.2 is unique among the cross-reactive anti-streptococcal mAbs due to its cytotoxicity for rat heart cells and its ability to strongly label the surface of heart cells in indirect immunofluorescence assays. In this study, cytotoxic mAb 36.2.2 was found to react strongly with the extracellular matrix protein laminin in immunoblots and inhibition assays, while 11 other cross-reactive anti-streptococcal mAbs did not react with laminin and were not cytotoxic. Cytotoxicity appeared to correlate with the presence of laminin on the surface of cells. Heavy and light chain variable region genes encoding mAb 36.2.2 were highly homologous to other V genes encoding anti-carbohydrate and/or autoantibodies. VH, JH, and Jkappa segments of mAb 36.2.2 may be encoded by germline gene segments. The VH segment may be identical with an as yet unidentified VH7183 family germline sequence, and the 36.2.2 Vkappa region gene is encoded by a Vkappa8 family member.

摘要

抗链球菌/抗肌球蛋白单克隆抗体36.2.2在交叉反应性抗链球菌单克隆抗体中独具特色,这是因为它对大鼠心脏细胞具有细胞毒性,并且在间接免疫荧光试验中能够强烈标记心脏细胞表面。在本研究中,发现细胞毒性单克隆抗体36.2.2在免疫印迹和抑制试验中与细胞外基质蛋白层粘连蛋白发生强烈反应,而其他11种交叉反应性抗链球菌单克隆抗体则不与层粘连蛋白反应,也没有细胞毒性。细胞毒性似乎与细胞表面层粘连蛋白的存在相关。编码单克隆抗体36.2.2的重链和轻链可变区基因与其他编码抗碳水化合物和/或自身抗体的V基因高度同源。单克隆抗体36.2.2的VH、JH和Jκ片段可能由种系基因片段编码。VH片段可能与一个尚未确定的VH7183家族种系序列相同,并且36.2.2 Vκ区域基因由一个Vκ8家族成员编码。

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