Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment.
Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment.
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DOI：
10.1186/1471-2180-10-141
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发表时间：
2010-05-12
期刊：
影响因子：
4.2
通讯作者：
Waterfield NR
中科院分区：
文献类型：
--
作者：
Jones RT;Sanchez-Contreras M;Vlisidou I;Amos MR;Yang G;Muñoz-Berbel X;Upadhyay A;Potter UJ;Joyce SA;Ciche TA;Jenkins AT;Bagby S;Ffrench-Constant RH;Waterfield NR
发光杆菌属是革兰氏阴性线虫共生菌和昆虫病原菌。Photorhabdus asybiotica能够感染人类和昆虫。我们研究了分泌蛋白质组的临床分离的P. asybiotica在不同的温度，以确定相关的蛋白质感染的两个不同的主机。在模拟昆虫温度（28°C）和人类温度（37°C）下，由P.asybiotica的临床分离株分泌的蛋白质的比较导致鉴定出小的且高度丰富的蛋白质，称为Pam，其仅在较低温度下分泌。pam基因存在于所有测试的光杆菌属菌株中，并且在整个属中显示出高水平的保守性，这表明它既是该属的祖先，也可能对细菌的生物学很重要。Pam蛋白与苏云金芽孢杆菌二元毒素的13.6 kDa组分显示有限的序列相似性。然而，注射或喂养异源生产的PAM没有表现出杀虫活性，无论是大蜡螟或烟草天蛾幼虫。在细菌菌落中，Pam与胞外多糖（EPS）样基质相关，并改变野生型细胞附着于人工表面的能力。有趣的是，表面等离子体共振（SPR）结合研究表明，Pam蛋白本身具有粘附特性。虽然Pam在整个昆虫感染过程中产生，但基因敲除不影响昆虫毒力或发光拟杆菌与其宿主线虫异小杆线虫形成共生关系的能力。我们研究了一个高度丰富的蛋白质，Pam，这是分泌的温度依赖性的方式在P. asybiotica。我们的研究结果表明，PAM在增强昆虫血液表面附着中起着重要作用。它与胞外多糖的结合表明它可能通过介导EPS性质发挥其作用。尽管Pam在该属中含量丰富且受到保护，但我们没有发现Pam在毒力或共生中发挥作用的证据。
Photorhabdus are Gram-negative nematode-symbiotic and insect-pathogenic bacteria. The species Photorhabdus asymbiotica is able to infect humans as well as insects. We investigated the secreted proteome of a clinical isolate of P. asymbiotica at different temperatures in order to identify proteins relevant to the infection of the two different hosts. A comparison of the proteins secreted by a clinical isolate of P. asymbiotica at simulated insect (28°C) and human (37°C) temperatures led to the identification of a small and highly abundant protein, designated Pam, that is only secreted at the lower temperature. The pam gene is present in all Photorhabdus strains tested and shows a high level of conservation across the whole genus, suggesting it is both ancestral to the genus and probably important to the biology of the bacterium. The Pam protein shows limited sequence similarity to the 13.6 kDa component of a binary toxin of Bacillus thuringiensis. Nevertheless, injection or feeding of heterologously produced Pam showed no insecticidal activity to either Galleria mellonella or Manduca sexta larvae. In bacterial colonies, Pam is associated with an extracellular polysaccharide (EPS)-like matrix, and modifies the ability of wild-type cells to attach to an artificial surface. Interestingly, Surface Plasmon Resonance (SPR) binding studies revealed that the Pam protein itself has adhesive properties. Although Pam is produced throughout insect infection, genetic knockout does not affect either insect virulence or the ability of P. luminescens to form a symbiotic association with its host nematode, Heterorhabditis bacteriophora. We studied a highly abundant protein, Pam, which is secreted in a temperature-dependent manner in P. asymbiotica. Our findings indicate that Pam plays an important role in enhancing surface attachment in insect blood. Its association with exopolysaccharide suggests it may exert its effect through mediation of EPS properties. Despite its abundance and conservation in the genus, we find no evidence for a role of Pam in either virulence or symbiosis.
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