A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella
A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella
复制标题
DOI：
10.1016/j.ibmb.2009.09.004
复制
发表时间：
2009-11-01
影响因子：
3.8
通讯作者：
East, Peter D.
中科院分区：
文献类型：
--
作者：
Brown, Susan E.;Howard, Antoinette;East, Peter D.
首次采用LC/MS法对大蜡螟的抗菌肽进行了研究。大蜡螟抗菌肽或蛋白质，即溶菌酶、moricin-like peptides（5）、cecropins（2）、gloverin、Gm脯氨酸富集肽1、Gm脯氨酸富集肽2、Gm阴离子肽1（P1-like）、Gm阴离子肽2。加利霉素、加利霉素、诱导型丝氨酸蛋白酶抑制剂2，6-tox和向日葵素样肽。其中6个以前只知道是核苷酸序列，因此这项研究为这些基因的表达提供了第一个证据。LC/MS数据还提供了对抗微生物Gm富含脯氨酸的肽1的表达和加工的深入了解。这种肽的基因被分离出来，并被证明是独特的蛾，并有一个异常长的前体区域（495 bp）。前体区域含有其他富含脯氨酸的肽，LC/MS数据表明这些肽被特异性加工，并以非常高的水平存在于血淋巴中。研究表明，G.大蜡螟可以同时释放一系列来自10个家族的至少18种已知或推定的抗微生物肽，以保护自己免受入侵微生物的侵害。(C)2009年由Elsevier Ltd.出版
The complete antimicrobial peptide repertoire of Galleria mellonella was investigated for the first time by LC/MS. Combining data from separate trypsin, Glu-C and Asp-N digests of immune hemolymph allowed detection of 18 known or putative G. mellonella antimicrobial peptides or proteins, namely lysozyme, moricin-like peptides (5), cecropins (2), gloverin, Gm proline-rich peptide 1, Gm proline-rich peptide 2, Gm anionic peptide 1 (P1-like), Gm anionic peptide 2. galiomicin, gallerimycin, inducible serine protease inhibitor 2, 6tox and heliocin-like peptide. Six of these were previously known only as nucleotide sequences, so this study provides the first evidence for expression of these genes. LC/MS data also provided insight into the expression and processing of the antimicrobial Gm proline-rich peptide 1. The gene for this peptide was isolated and shown to be unique to moths and to have an unusually long precursor region (495 bp). The precursor region contained other proline-rich peptides and LC/MS data suggested that these were being specifically processed and were present in hemolymph at very high levels. This study shows that G. mellonella can concurrently release an impressive array of at least 18 known or putative antimicrobial peptides from 10 families to defend itself against invading microbes. (C) 2009 Published by Elsevier Ltd.