MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae

Veronica M. Jarocki, Jerran Santos, Jessica L. Tacchi, Benjamin B A Raymond, Ania T. Deutscher, Cheryl Jenkins, Matthew P. Padula, Steven P. Djordjevic*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)
1 Downloads (Pure)

Abstract

Aminopeptidases are part of the arsenal of virulence factors produced by bacterial pathogens that inactivate host immune peptides. Mycoplasma hyopneumoniae is a genome-reduced pathogen of swine that lacks the genetic repertoire to synthesize amino acids and relies on the host for availability of amino acids for growth. M. hyopneumoniae recruits plasmin(ogen) onto its cell surface via the P97 and P102 adhesins and the glutamyl aminopeptidase MHJ_0125. Plasmin plays an important role in regulating the inflammatory response in the lungs of pigs infected with M. hyopneumoniae. We show that recombinant MHJ_0461 (rMHJ_0461) functions as a leucine aminopeptidase (LAP) with broad substrate specificity for leucine, alanine, phenylalanine, methionine and arginine and that MHJ_0461 resides on the surface of M. hyopneumoniae. rMHJ_0461 also binds heparin, plasminogen and foreign DNA. Plasminogen bound to rMHJ-0461 was readily converted to plasmin in the presence of tPA. Computational modelling identified putative DNA and heparin-binding motifs on solvent-exposed sites around a large pore on the LAP hexamer. We conclude that MHJ-0461 is a LAP that moonlights as a multifunctional adhesin on the cell surface of M. hyopneumoniae.

Original languageEnglish
Article number140175
Pages (from-to)1-13
Number of pages13
JournalOpen Biology
Volume5
Issue number1
DOIs
Publication statusPublished - Jan 2015
Externally publishedYes

Bibliographical note

Copyright the Author(s) 2015. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

Keywords

  • Adhesin
  • DNA-binding protein
  • Heparin-binding protein
  • Leucine aminopeptidase
  • Moonlighting protein
  • Plasminogenbinding protein

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