MHJ-0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae

Jarocki, VM; Santos, J; Tacchi, JL; Raymond, BBA; Deutscher, AT; Jenkins, C; Padula, MP; Djordjevic, SP

MHJ-0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae

Jarocki, VM

Santos, J

Tacchi, JL Raymond, BBA

Deutscher, AT Jenkins, C

Padula, MP

Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Open Biology, 2015, 5 (1)
Issue Date:: 2015-01-01

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Field	Value	Language
dc.contributor.author	Jarocki, VM https://orcid.org/0000-0003-1249-0994	en_US
dc.contributor.author	Santos, J https://orcid.org/0000-0003-4067-220X	en_US
dc.contributor.author	Tacchi, JL	en_US
dc.contributor.author	Raymond, BBA https://orcid.org/0000-0003-3610-9289	en_US
dc.contributor.author	Deutscher, AT	en_US
dc.contributor.author	Jenkins, C https://orcid.org/0000-0002-5966-072X	en_US
dc.contributor.author	Padula, MP https://orcid.org/0000-0002-8283-0643	en_US
dc.contributor.author	Djordjevic, SP https://orcid.org/0000-0001-9301-5372	en_US
dc.date.issued	2015-01-01	en_US
dc.identifier.citation	Open Biology, 2015, 5 (1)	en_US
dc.identifier.uri	http://hdl.handle.net/10453/32661
dc.description.abstract	© 2015 The Authors. Published. 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.	en_US
dc.relation.ispartof	Open Biology	en_US
dc.relation.isbasedon	10.1098/rsob.140175	en_US
dc.subject.mesh	Mycoplasma hyopneumoniae	en_US
dc.subject.mesh	Plasminogen	en_US
dc.subject.mesh	Leucyl Aminopeptidase	en_US
dc.subject.mesh	Heparin	en_US
dc.subject.mesh	Amino Acids	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Membrane Proteins	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Substrate Specificity	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.title	MHJ-0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	5	en_US
utslib.for	060114 Systems Biology	en_US
utslib.for	060109 Proteomics and Intermolecular Interactions (excl. Medical Proteomics)	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	1107 Immunology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	open_access
pubs.issue	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	5	en_US

Abstract:

© 2015 The Authors. Published. 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.

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http://hdl.handle.net/10453/32661