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MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae.
Jarocki, Veronica M; Santos, Jerran; Tacchi, Jessica L; Raymond, Benjamin B A; Deutscher, Ania T; Jenkins, Cheryl; Padula, Matthew P; Djordjevic, Steven P.
Afiliação
  • Jarocki VM; The ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Santos J; The ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Tacchi JL; The ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Raymond BB; The ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Deutscher AT; NSW Department of Primary Industries, Private Bag 4008, Narellan, New South Wales 2567, Australia.
  • Jenkins C; NSW Department of Primary Industries, Private Bag 4008, Narellan, New South Wales 2567, Australia.
  • Padula MP; The ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Djordjevic SP; The ithree institute, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology, Sydney, PO Box 123, Broadway, New South Wales 2007, Australia steven.djordjevic@uts.edu.au.
Open Biol ; 5(1): 140175, 2015 Jan.
Article em En | MEDLINE | ID: mdl-25589579
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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Mycoplasma hyopneumoniae / Leucil Aminopeptidase / Proteínas de Membrana Tipo de estudo: Prognostic_studies Idioma: En Revista: Open Biol Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Austrália
Texto completo
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Mycoplasma hyopneumoniae / Leucil Aminopeptidase / Proteínas de Membrana Tipo de estudo: Prognostic_studies Idioma: En Revista: Open Biol Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Austrália