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深海虾中的一种 Ib 型几丁质结合蛋白具有抗菌和免疫调节活性。

A Type Ib Crustin from Deep-Sea Shrimp Possesses Antimicrobial and Immunomodulatory Activity.

机构信息

CAS and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Center for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao 266071, China.

Laboratory for Marine Biology and Biotechnology, Pilot National Laboratory for Marine Science and Technology, Qingdao 266237, China.

出版信息

Int J Mol Sci. 2022 Jun 9;23(12):6444. doi: 10.3390/ijms23126444.

DOI:10.3390/ijms23126444
PMID:35742887
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9223358/
Abstract

Crustins are small antimicrobial proteins produced by crustaceans. Of the many reported crustins, very few are from deep sea environments. Crustins are categorized into several types. Recently, the Type I crustin has been further classified into three subtypes, one of which is Type Ib, whose function is unknown. Here, we studied the function of a Type Ib crustin (designated Crus2) identified from a deep-sea crustacean. Crus2 has a whey acidic protein (WAP) domain and a long C-terminal region (named P58). Recombinant Crus2 bound to peptidoglycan (PGN), lipoteichoic acid (LTA), and lipopolysaccharide (LPS), and killed Gram-positive and Gram-negative bacteria by permeabilizing the bacterial cytomembrane. Consistently, Crus2 dramatically attenuated the inflammatory response induced by LPS and LTA. Disruption of the disulfide bonds in the WAP domain abolished the bactericidal ability of Crus2, but had no effect on the bacterial binding ability of Crus2. Deletion of the C-terminal P58 region moderately affected the antimicrobial activity of Crus2 against some bacteria. P58 as a synthesized peptide could bind bacteria and inhibit the bactericidal activity of Crus2. Taken together, these results revealed different roles played by the WAP domain and the P58 region in Type Ib crustin, and provided new insights into the antimicrobial and immunomodulatory functions of crustins.

摘要

甲壳质是由甲壳类动物产生的小抗菌蛋白。在众多报道的甲壳质中，只有很少一部分来自深海环境。甲壳质分为几种类型。最近，I 型甲壳质进一步分为三个亚类，其中一个是 Ib 型，其功能未知。在这里，我们研究了从深海甲壳类动物中鉴定出的 Ib 型甲壳质（命名为 Crus2）的功能。 Crus2 具有乳清酸性蛋白 (WAP) 结构域和长 C 末端区域（命名为 P58）。重组 Crus2 与肽聚糖 (PGN)、脂磷壁酸 (LTA) 和脂多糖 (LPS) 结合，并通过破坏细菌细胞质膜来杀死革兰氏阳性菌和革兰氏阴性菌。一致地， Crus2 显着减轻了 LPS 和 LTA 诱导的炎症反应。破坏 WAP 结构域中的二硫键会使 Crus2 的杀菌能力丧失，但对 Crus2 的细菌结合能力没有影响。删除 C 末端 P58 区域会适度影响 Crus2 对某些细菌的抗菌活性。P58 作为合成肽可以结合细菌并抑制 Crus2 的杀菌活性。总之，这些结果揭示了 WAP 结构域和 P58 区域在 Ib 型甲壳质中发挥的不同作用，并为甲壳质的抗菌和免疫调节功能提供了新的见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/552e9088739f/ijms-23-06444-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/a865ead8a784/ijms-23-06444-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/fe846ec56325/ijms-23-06444-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/b31b744bc843/ijms-23-06444-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/be517104adef/ijms-23-06444-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/505c45ae512e/ijms-23-06444-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/552e9088739f/ijms-23-06444-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/a865ead8a784/ijms-23-06444-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/fe846ec56325/ijms-23-06444-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/b31b744bc843/ijms-23-06444-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/be517104adef/ijms-23-06444-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/505c45ae512e/ijms-23-06444-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5452/9223358/552e9088739f/ijms-23-06444-g006.jpg

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