...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Fish & Shellfish Immunology >Identification and characterization of a cell surface scavenger receptor cysteine-rich protein of Sciaenops ocellatus: bacterial interaction and its dependence on the conserved structural features of the SRCR domain.
【24h】

Identification and characterization of a cell surface scavenger receptor cysteine-rich protein of Sciaenops ocellatus: bacterial interaction and its dependence on the conserved structural features of the SRCR domain.

机译：鉴定和表征Sciaenops ocellatus的细胞表面清除剂受体富含半胱氨酸的蛋白：细菌相互作用及其对SRCR结构域保守结构特征的依赖性。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The scavenger receptor cysteine-rich (SRCR) proteins are secreted or membrane-bound receptors with one or multiple SRCR domains. Members of the SRCR superfamily are known to have diverse functions that include pathogen recognition and immunoregulation. In teleost, although protein sequences with SRCR structure have been identified in some species, very little functional investigation has been carried out. In this study, we identified and characterized a teleost SRCR protein from red drum Sciaenops ocellatus. The protein was named S. ocellatus SRCR1 (SoSRCRP1). SoSRCRP1 is 410-residue in length and was predicted to be a transmembrane protein, with the extracellular region containing a collagen triple helix repeat and a SRCR domain. The SRCR domain has six conserved cysteines, of which, C338 and C399, C351 and C409, and C379 and C389 were predicted to form three disulfide bonds. SoSRCRP1 expression was detected mainly in immune-relevant tissues and upregulated by bacterial and viral infection. In head kidney leukocytes, bacterial infection stimulated the expression of SoSRCRP1, and the expressed SoSRCRP1 was localized on cell surface. Recombinant SoSRCRP1 (rSoSRCRP1) corresponding to the SRCR domain was purified from Escherichia coli and found to be able to bind Gram-negative and Gram-positive bacteria. To examine the structure-function relationship of SoSRCRP1, the mutant proteins SoSRCRP1M1, SoSRCRP1M2, SoSRCRP1M3, and SoSRCRP1M4 were created, which bear C351S and C409S, C338S, C379S, and R325A mutations respectively. Compared to rSoSRCRP1, all mutants were significantly reduced in the ability of bacterial interaction, with the highest reduction observed with SoSRCRP1M4. Taken together, these results indicate that SoSRCRP1 is a cell surface-localized SRCR protein that binds bacterial ligands in a manner that depends on the conserved structural features of the SRCR domain.
机译：清除剂受体富含半胱氨酸（SRCR）蛋白是具有一个或多个SRCR域的分泌型或膜结合型受体。已知SRCR超家族成员具有多种功能，包括病原体识别和免疫调节。在硬骨鱼中，尽管在某些物种中已鉴定出具有SRCR结构的蛋白质序列，但很少进行功能研究。在这项研究中，我们鉴定并鉴定了来自红鼓鲈鱼的硬骨鱼SRCR蛋白。该蛋白被命名为S. ocellatus SRCR1（SoSRCRP1）。 SoSRCRP1的长度为410个残基，预计是跨膜蛋白，其胞外区域包含胶原三螺旋重复序列和SRCR域。 SRCR域具有六个保守的半胱氨酸，其中C338和C399，C351和C409以及C379和C389被预测会形成三个二硫键。 SoSRCRP1表达主要在免疫相关组织中检测到，并被细菌和病毒感染上调。在头肾白细胞中，细菌感染刺激了SoSRCRP1的表达，并且表达的SoSRCRP1定位在细胞表面。从大肠杆菌中纯化了对应于SRCR域的重组SoSRCRP1（rSoSRCRP1），发现它能够结合革兰氏阴性和革兰氏阳性细菌。为了检查SoSRCRP1的结构-功能关系，创建了突变蛋白SoSRCRP1M1，SoSRCRP1M2，SoSRCRP1M3和SoSRCRP1M4，它们分别带有C351S和C409S，C338S，C379S和R325A突变。与rSoSRCRP1相比，所有突变体的细菌相互作用能力均显着降低，其中SoSRCRP1M4的降低幅度最大。综上所述，这些结果表明，SoSRCRP1是一种细胞表面定位的SRCR蛋白，其结合细菌配体的方式取决于SRCR域的保守结构特征。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号