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An M29 Aminopeptidase from Listeria Monocytogenes 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 Listeria monocytogenes (LmAmpII). We show that LmAmpII contains a conserved cataly...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7023490/ https://www.ncbi.nlm.nih.gov/pubmed/31941013 http://dx.doi.org/10.3390/microorganisms8010110 |
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author | Zhang, Xian Guan, Chiyu Hang, Yi Liu, Fengdan Sun, Jing Yu, Huifei Gan, Li Zeng, Huan Zhu, Yiran Chen, Zhongwei Song, Houhui Cheng, Changyong |
author_facet | Zhang, Xian Guan, Chiyu Hang, Yi Liu, Fengdan Sun, Jing Yu, Huifei Gan, Li Zeng, Huan Zhu, Yiran Chen, Zhongwei Song, Houhui Cheng, Changyong |
author_sort | Zhang, Xian |
collection | PubMed |
description | 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 Listeria monocytogenes (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 L. monocytogenes 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 Listeria infection. |
format | Online Article Text |
id | pubmed-7023490 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70234902020-03-12 An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection Zhang, Xian Guan, Chiyu Hang, Yi Liu, Fengdan Sun, Jing Yu, Huifei Gan, Li Zeng, Huan Zhu, Yiran Chen, Zhongwei Song, Houhui Cheng, Changyong Microorganisms Article 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 Listeria monocytogenes (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 L. monocytogenes 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 Listeria infection. MDPI 2020-01-13 /pmc/articles/PMC7023490/ /pubmed/31941013 http://dx.doi.org/10.3390/microorganisms8010110 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zhang, Xian Guan, Chiyu Hang, Yi Liu, Fengdan Sun, Jing Yu, Huifei Gan, Li Zeng, Huan Zhu, Yiran Chen, Zhongwei Song, Houhui Cheng, Changyong An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection |
title | An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection |
title_full | An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection |
title_fullStr | An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection |
title_full_unstemmed | An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection |
title_short | An M29 Aminopeptidase from Listeria Monocytogenes Contributes to In Vitro Bacterial Growth but not to Intracellular Infection |
title_sort | m29 aminopeptidase from listeria monocytogenes contributes to in vitro bacterial growth but not to intracellular infection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7023490/ https://www.ncbi.nlm.nih.gov/pubmed/31941013 http://dx.doi.org/10.3390/microorganisms8010110 |
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