An M29 Aminopeptidase from <i>Listeria Monocytogenes</i> Contributes to In Vitro Bacterial Growth but not to Intracellular Infection

Aminopeptidases that catalyze the removal of N-terminal residues from polypeptides or proteins are crucial for physiological processes. Here, we explore the biological functions of an M29 family aminopeptidase II from <i>Listeria monocytogenes</i> (LmAmpII). We show that LmAmpII contains...

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Bibliographic Details
Main Authors: Xian Zhang, Chiyu Guan, Yi Hang, Fengdan Liu, Jing Sun, Huifei Yu, Li Gan, Huan Zeng, Yiran Zhu, Zhongwei Chen, Houhui Song, Changyong Cheng
Format: Article
Language:English
Published: MDPI AG 2020-01-01
Series:Microorganisms
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Online Access:https://www.mdpi.com/2076-2607/8/1/110
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Summary:Aminopeptidases that catalyze the removal of N-terminal residues from polypeptides or proteins are crucial for physiological processes. Here, we explore the biological functions of an M29 family aminopeptidase II from <i>Listeria monocytogenes</i> (LmAmpII). We show that LmAmpII contains a conserved catalytic motif (EEHYHD) that is essential for its enzymatic activity and LmAmpII has a substrate preference for arginine and leucine. Studies on biological roles indicate that LmAmpII is required for in vitro growth in a chemically defined medium for optimal growth of <i>L. monocytogenes</i> but is not required for bacterial intracellular infection in epithelial cells and macrophages, as well as cell-to-cell spreading in fibroblasts. Moreover, LmAmpII is found as dispensable for bacterial pathogenicity in mice. Taken together, we conclude that LmAmpII, an M29 family aminopeptidase, can efficiently hydrolyze a wide range of substrates and is required for in vitro bacterial growth, which lays a foundation for in-depth investigations of aminopeptidases as potential targets to defend <i>Listeria</i> infection.
ISSN:2076-2607