A 29.5 KDA heat-modifiable major outer membrane protein of Rickettsia prowazekii, putative virulence factor, is a peptidyl-prolyl cis/trans isomerase
A 29.5 KDA heat-modifiable major outer membrane protein of Rickettsia prowazekii, putative virulence factor, is a peptidyl-prolyl cis/trans isomerase
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DOI：
10.1080/15216540410001699321
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发表时间：
2004-04-01
期刊：
影响因子：
4.6
通讯作者：
Loukianov, EV
中科院分区：
文献类型：
--
作者：
Emelyanov, VV;Loukianov, EV
来自编码小小病毒样蛋白 (Plp)（一种可热修饰的 29.5 kDa 主要外膜蛋白）的三种普氏立克次体菌株的等位基因先前被克隆到表达载体 pQE 30 中。在这项工作中，重组蛋白在大肠杆菌中过量产生并纯化，并发现表现出预期的肽基-脯氨酰顺/反异构酶活性 具有寡肽底物的体外小病毒型。已知原型强毒 Breinl 菌株的天然多肽在 SDS-PAGE 迁移率方面与疫苗马德里 E 和强毒 EVir 分离株的天然多肽不同。由于电泳行为不同，三种菌株的未热修饰形式显示出与脂多糖分开的迁移。对 EVir Plp 基因进行了测序，发现推导的蛋白质序列与先前发表的 Breinl 和马德里 E 相同。目前的数据表明未知的翻译后模式。立克次体中的阳离子造成 Plp 的株间差异和热改性性。
Allelic genes from three Rickettsia prowazekii strains encoding parvulin-like protein (Plp), a heat-modifiable 29.5 kDa major outer membrane protein, were earlier cloned into expression vector pQE 30. In this work, recombinant proteins were overproduced in E. coli, purified, and found to exhibit an expected peptidyl-prolyl cis/trans isomerase activity of a parvulin type in vitro with oligopeptide substrates. Native polypeptide of prototype virulent Breinl strain is known to differ by SDS-PAGE mobility from those of both vaccine Madrid E and virulent EVir isolates. Being different in electrophoretic behavior, heat-unmodified forms of the three strains were shown to migrate apart from lipopolysaccharides. A EVir Plp gene was sequenced, and deduced protein sequence was found to be identical to previously published Breinl and Madrid E. Present data indicate that unknown post-translational modi. cation(s) in rickettsiae are responsible for both interstrain difference and heat-modifiability of Plp.