ArticleOpen biology2013
MHJ_0125 is an M42 glutamyl aminopeptidase that moonlights as a multifunctional adhesin on the surface of Mycoplasma hyopneumoniae.
Article in Open biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 56 citations in OpenAlex.
- Wide Diversity and Complex Evolution of M42 Aminopeptidases With Contrasted Functional Properties in Archaea.Molecular biology and evolution · 2025Article
- Elongation factor Tu promotes the onset of periodontitis through mediating bacteria adhesion.NPJ biofilms and microbiomes · 2025Article
- Updated Methods for Elucidating Bacterial Surfaceomes.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Non-Toxin-BasedPathogens (Basel, Switzerland) · 2023Article
- Toward the Complete Functional Characterization of a Minimal Bacterial Proteome.The journal of physical chemistry. B · 2022Article
- TheFrontiers in microbiology · 2022Review
- Proteomic and bioinformatic analyses of proteins in the outer membrane and extracellular compartments and outer membrane vesicles ofFrontiers in microbiology · 2022Article
- Review
- Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.Scientific reports · 2021Article
- Pathogenicity & virulence ofVirulence · 2020Review
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- Mycoplasma bovis Membrane Protein MilA Is a Multifunctional Lipase with Novel Lipid and Glycosaminoglycan Binding Activity.Infection and immunity · 2020Article
- Cell surface processing of the P1 adhesin of Mycoplasma pneumoniae identifies novel domains that bind host molecules.Scientific reports · 2020Article
- Combined Transcriptome Sequencing ofFrontiers in microbiology · 2020Article
- Genomic Variability and Post-translational Protein Processing Enhance the Immune Evasion ofFrontiers in immunology · 2020Review
- Mycoplasma hyopneumoniae surface-associated proteases cleave bradykinin, substance P, neurokinin A and neuropeptide Y.Scientific reports · 2019Article
- Mycoplasma hyopneumoniae evades phagocytic uptake by porcine alveolar macrophages in vitro.Veterinary research · 2019Article
- Terminomics Methodologies and the Completeness of Reductive Dimethylation: A Meta-Analysis of Publicly Available Datasets.Proteomes · 2019Article
- The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.Frontiers in microbiology · 2019Review
- Quantitative Proteomic Analyses of a Pathogenic Strain and Its Highly Passaged Attenuated Strain ofBioMed research international · 2019Article
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial aminopeptidases play important roles in pathogenesis by providing a source of amino acids from exogenous proteins, destroying host immunological effector peptides and executing posttranslational modification of bacterial and host proteins. We show that MHJ_0125 from the swine respiratory pathogen Mycoplasma hyopneumoniae represents a new member of the M42 class of bacterial aminopeptidases. Despite lacking a recognizable signal sequence, MHJ_0125 is detectable on the cell surface by fluorescence microscopy and LC-MS/MS of (i) biotinylated surface proteins captured by avidin chromatography and (ii) peptides released by mild trypsin shaving. Furthermore, surface-associated glutamyl aminopeptidase activity was detected by incubation of live M. hyopneumoniae cells with the diagnostic substrate H-Glu-AMC. MHJ_0125 moonlights as a multifunctional adhesin, binding to both heparin and plasminogen. Native proteomics and comparative modelling studies suggest MHJ_0125 forms a dodecameric, homopolymeric structure and provide insight into the positions of key residues that are predicted to interact with heparin and plasminogen. MHJ_0125 is the first aminopeptidase shown to both bind plasminogen and facilitate its activation by tissue plasminogen activator. Plasmin cleaves host extracellular matrix proteins and activates matrix metalloproteases, generating peptide substrates for MHJ_0125 and a source of amino acids for growth of M. hyopneumoniae. This unique interaction represents a new paradigm in microbial pathogenesis.
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