The role of a novel secretory peptidoglycan recognition protein with antibacterial ability from the Chinese Oak Silkworm Antheraea pernyi in humoral immunity

被引:1
|
作者
Duan, Xutong [1 ]
Fu, Ting [1 ]
Liu, Chang [2 ]
Wang, Fuhui [1 ]
Liu, Chengbao [1 ]
Zhao, Lin [1 ]
Yu, Jinzhu [1 ]
Wang, Xialu [2 ]
Zhang, Rong [1 ]
机构
[1] Shenyang Pharmaceut Univ, Sch Life Sci & Biopharmaceut, Shenyang 110016, Liaoning, Peoples R China
[2] Shenyang Pharmaceut Univ, Sch Med Devices, Shenyang 110016, Liaoning, Peoples R China
基金
中国国家自然科学基金;
关键词
Peptidoglycan recognition protein; Pattern recognition receptor; Humoral immunity; Amidase activity; Antibacterial activity; L-ALANINE AMIDASE; INNATE IMMUNITY; FUNCTIONAL-ANALYSIS; MOLECULAR-CLONING; COTTON BOLLWORM; GENE FAMILIES; BACTERIAL; INVOLVEMENT; ACTIVATION; PGRP;
D O I
10.1016/j.ibmb.2024.104151
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Peptidoglycan recognition proteins (PGRPs) are a family of pattern recognition receptors that play a critical role in the immune response of invertebrates and vertebrates. Herein, the short Ap PGRP-D gene was cloned from the model lepidopteran Antheraea pernyi. Quantitative PCR (qPCR) confirmed that Ap PGRP-D is an immune-related protein and that the expression of Ap PGRP-D can be induced by microorganisms. Ap PGRP-D is a broad-spectrum pattern recognition protein that activates the prophenoloxidase cascade activation system and promotes the agglutination of microbial cells. Likely due to its amidase activity, Ap PGRP-D can inhibit the growth of E. coli and S. aureus . In addition, we demonstrated for the first time that zinc ions, as important metal coenzymes, could promote multiple functions of Ap PGRP-D but not its amidase activity.
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页数:15
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