ArticleScientific reports2015
Aminopeptidase T of M29 Family Acts as A Novel Intracellular Virulence Factor for Listeria monocytogenes Infection.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Listeria monocytogenes: from a saprophytic to a cytosolic virulent pathogen.World journal of microbiology & biotechnology · 2025Review
- An anti-biofilm cyclic peptide targets a secreted aminopeptidase from P. aeruginosa.Nature chemical biology · 2023Article
- The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023Article
- Antimicrobial and immunomodulatory effects of tannic acid supplementation in broilers infected with Salmonella Typhimurium.Poultry science · 2022Article
- Characterization and heterologous expression of a novel CoApplied microbiology and biotechnology · 2022Article
- Transcriptomic Analysis ofFrontiers in microbiology · 2021Article
- An M29 Aminopeptidase fromMicroorganisms · 2020Article
- Metabolism of the Gram-Positive Bacterial PathogenMicrobiology spectrum · 2019Review
- TLR2 Promotes Monocyte/Macrophage Recruitment Into the Liver and Microabscess Formation to Limit the Spread ofFrontiers in immunology · 2019Article
- The Redox-Sensing Regulator Rex Contributes to the Virulence and Oxidative Stress Response ofFrontiers in cellular and infection microbiology · 2018Article
- Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression inFrontiers in microbiology · 2018Article
- Listeria monocytogenes cytosolic metabolism promotes replication, survival, and evasion of innate immunity.Cellular microbiology · 2017Review
- Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis.Scientific reports · 2017Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The foodborne pathogen Listeria monocytogenes employs a number of virulence determinants including metalloproteases to infect hosts. Here for the first time, we identified an M29 family aminopeptidase T (encoded by lmo1603) from L. monocytogenes that possesses a typical feature to catalyze the cleavage of amino acids from peptide substrates, with a preference for arginine. The purified recombinant Lmo1603 was activated by Fe(3+), Zn(2+) and Mn(2+), but strongly stimulated by Co(2+), indicating that Lmo1603 is a cobalt-dependent aminopeptidase. Single mutation at any of the Glu216, Glu281, His308, Tyr315, His327, and Asp329 completely abolished the enzymatic activity of Lmo1603. More importantly, we showed that Lmo1603 was mainly involved in Listeria infection, but not required for growth in rich laboratory medium and minimal defined medium. Disruption of Lmo1603 resulted in almost complete attenuation of Listeria virulence in a mouse infection model. In addition, we demonstrated that Lmo1603 was mainly localized in the bacterial cytosol and required for invasion and survival inside human epithelial cells and murine macrophages. We conclude that Lmo1603 encodes a functional aminopeptidase T of M29 family, which acts as a novel intracellular virulence factor essential in the successful establishment of L. monocytogenes infections in a mouse model.
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