Huang Hai, Du Juan, Li Shang-Wei, Gong Tao
Guizhou Provincial Key Laboratory for Agricultural Pest Management of Mountainous Regions, Institute of Entomology, Guizhou University, Guiyang 550025, China.
Biology (Basel). 2021 Apr 14;10(4):330. doi: 10.3390/biology10040330.
is a valuable medicinal insect resource in China. Previous studies have indicated that the antibacterial and anticancer effects of the extract mainly come from the active polypeptides. Lysozyme is an effective immune effector in insect innate immunity and usually has excellent bactericidal effects. There are two kinds of lysozymes in insects, c-type and i-type, which play an important role in innate immunity and intestinal digestion. Studying lysozyme in will be helpful to further explore the evolutionary relationship and functional differences among lysozymes of various species and to determine whether they have biological activity and medicinal value. In this study, a lysozyme CcLys2 was identified from . CcLys2 contains 223 amino acid residues, and possesses a typical domain of the c-type lysozyme and a putative catalytic site formed by two conserved residues Glu32 and Asp50. Phylogenetic analysis showed that CcLys2 belongs to the H-branch of the c-type lysozyme. The analysis of spatiotemporal expression patterns indicated that was mainly expressed in the fat body of adults and was highly expressed in the second- and fifth-instar nymphs. In addition, was significantly up-regulated after injecting and feeding bacteria. In the bacterial inhibition assay, it was found that CcLys2 had antibacterial activity against Gram-positive bacteria at a low pH. These results indicate that CcLys2 has muramidase activity, involves in the innate immunity of and is also closely related to the bacterial immune defense or digestive function of the intestine.
是中国一种有价值的药用昆虫资源。先前的研究表明,该提取物的抗菌和抗癌作用主要来自活性多肽。溶菌酶是昆虫先天免疫中的一种有效免疫效应物,通常具有出色的杀菌作用。昆虫中有两种溶菌酶,即c型和i型,它们在先天免疫和肠道消化中起重要作用。研究[昆虫名称]中的溶菌酶将有助于进一步探索各种物种溶菌酶之间的进化关系和功能差异,并确定它们是否具有生物活性和药用价值。在本研究中,从[昆虫名称]中鉴定出一种溶菌酶CcLys2。CcLys2包含223个氨基酸残基,具有c型溶菌酶的典型结构域以及由两个保守残基Glu32和Asp50形成的假定催化位点。系统发育分析表明CcLys2属于c型溶菌酶的H分支。时空表达模式分析表明,[基因名称]主要在[昆虫名称]成虫的脂肪体中表达,在二龄和五龄若虫中高表达。此外,在注射和喂食细菌后,[基因名称]显著上调。在细菌抑制试验中,发现CcLys2在低pH值下对革兰氏阳性菌具有抗菌活性。这些结果表明CcLys2具有溶菌酶活性,参与[昆虫名称]的先天免疫,并且也与肠道的细菌免疫防御或消化功能密切相关。