Kong Xue, Liu Helu, Li Yanan, Zhang Haibin
Institute of Deep-Sea Science and Engineering, Chinese Academy of Sciences, Sanya, China.
College of Earth and Planetary Sciences, University of Chinese Academy of Sciences, Beijing, China.
Front Physiol. 2018 Oct 23;9:1476. doi: 10.3389/fphys.2018.01476. eCollection 2018.
Vesicomyidae clams are common species living in cold seeps, which incorporates symbiotic bacteria into their body maintaining endosymbiosis relationship. As members of pattern recognition receptor (PRR) family, peptidoglycan recognition proteins (PGRPs) recognize pathogen associated molecular patterns and play an important role in innate immunity. In present study, two short PGRPs (ApPGRP-1 and -2) were first identified from Vesicomyidae clam . Sequences analysis showed that they have both conserved Zn binding sites (H-H-C) and amidase catalytic sites (H-Y-H-T-C), and phylogenetic tree indicated that they clustered with short PGRPs of other molluscs. PGN assay showed that ApPGRPs could bind Lys-type PGN from and Dap-type PGN from , and revealed amidase activity with selective zinc ion dependence. rApPGRP-1 and -2 (recombinant ApPGRP-1 and -2) could bind six bacteria with a broad spectrum and had both zinc-dependent and -independent bactericidal activity. ApPGRPs had the complete functions of effectors and partial functions of receptors from PGRPs. Further analyses showed that ApPGRPs from might be involved in the endosymbiosis relationship between the host clam and endosymbiotic bacteria as a regulator. The results of these experiments suggested that ApPGRPs were involved in cold seep clams' immune response. This study provides basic information for further research on the immune mechanisms of deep sea organisms.
泡蛤科蛤类是生活在冷泉中的常见物种,它们将共生细菌纳入体内,维持内共生关系。作为模式识别受体(PRR)家族的成员,肽聚糖识别蛋白(PGRP)识别病原体相关分子模式,并在先天免疫中发挥重要作用。在本研究中,首次从泡蛤科蛤类中鉴定出两种短型PGRP(ApPGRP-1和-2)。序列分析表明,它们都具有保守的锌结合位点(H-H-C)和酰胺酶催化位点(H-Y-H-T-C),系统发育树表明它们与其他软体动物的短型PGRP聚类。PGN检测表明,ApPGRPs可以结合来自[具体来源1]的赖氨酸型PGN和来自[具体来源2]的Dap型PGN,并显示出具有选择性锌离子依赖性的酰胺酶活性。重组ApPGRP-1和-2(rApPGRP-1和-2)可以广谱结合六种细菌,并且具有锌依赖性和非依赖性杀菌活性。ApPGRPs具有效应器的完整功能和PGRPs受体的部分功能。进一步分析表明,来自[具体来源]的ApPGRPs可能作为调节因子参与宿主蛤类与内共生细菌之间的内共生关系。这些实验结果表明,ApPGRPs参与了冷泉蛤类的免疫反应。本研究为进一步研究深海生物的免疫机制提供了基础信息。