LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata
LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata
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DOI：
10.1128/iai.01643-07
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发表时间：
2008-05-01
影响因子：
3.1
通讯作者：
Adler, Ben
中科院分区：
文献类型：
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作者：
Hoke, David E.;Egan, Suhelen;Adler, Ben
LipL32是致病钩端螺旋体的主要外膜蛋白。它在致病物种中高度保守，在人类感染期间在体内表达。虽然这些数据表明在发病机制中发挥了作用，但LipL32的功能尚未定义。革兰氏阴性细菌的外膜蛋白是与宿主分子相互作用的第一线，许多蛋白已被证明与宿主细胞外基质(ECM)结合。对钩端螺旋体ECM相互作用蛋白的搜索确定了主要的外膜蛋白LipL32。为了验证这一发现，在大肠杆菌中表达了重组LipL32，并发现它能结合Matrigel ECM和ECM的单个成分，包括层粘连蛋白、1号胶原和V型胶原。此外，还表达了衣状假单胞菌D2株基因组中的一个同源蛋白，发现该蛋白在功能上相似，并具有免疫交叉反应。最后，结合活性被映射到C端的72个氨基酸。这些研究表明，LipL32和衣原体中的一个同源蛋白具有免疫交叉反应，并通过保守的C-末端区域发挥细胞外基质相互作用蛋白的功能。
LipL32 is the major outer membrane protein in pathogenic Leptospira. It is highly conserved throughout pathogenic species and is expressed in vivo during human infection. While these data suggest a role in pathogenesis, a function for LipL32 has not been defined. Outer membrane proteins of gram-negative bacteria are the first line of molecular interaction with the host, and many have been shown to bind host extracellular matrix (ECM). A search for leptospiral ECM-interacting proteins identified the major outer membrane protein, LipL32. To verify this finding, recombinant LipL32 was expressed in Escherichia coli and was found to bind Matrigel ECM and individual components of ECM, including laminin, collagen 1, and collagen V. Likewise, an orthologous protein found in the genome of Pseudoalteromonas tunicata strain D2 was expressed and found to be functionally similar and immunologically cross-reactive. Lastly, binding activity was mapped to the C-terminal 72 amino acids. These studies show that LipL32 and an orthologous protein in P. tunicata are immunologically cross-reactive and function as ECM-interacting proteins via a conserved C-terminal region.