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

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 ami...
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Autor*in:	Veronica M. Jarocki [verfasserIn] Jerran Santos [verfasserIn] Jessica L. Tacchi [verfasserIn] Benjamin B. A. Raymond [verfasserIn] Ania T. Deutscher [verfasserIn] Cheryl Jenkins [verfasserIn] Matthew P. Padula [verfasserIn] Steven P. Djordjevic [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	adhesin dna-binding protein plasminogen-binding protein heparin-binding protein leucine aminopeptidase moonlighting protein

Übergeordnetes Werk:	In: Open Biology - The Royal Society, 2012, 5(2015), 1
Übergeordnetes Werk:	volume:5 ; year:2015 ; number:1

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1098/rsob.140175

Katalog-ID:	DOAJ069200920

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spelling	10.1098/rsob.140175 doi (DE-627)DOAJ069200920 (DE-599)DOAJab1300e372e14bbeaeafff28ffd5c982 DE-627 ger DE-627 rakwb eng QH301-705.5 Veronica M. Jarocki verfasserin aut MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. adhesin dna-binding protein plasminogen-binding protein heparin-binding protein leucine aminopeptidase moonlighting protein Biology (General) Jerran Santos verfasserin aut Jessica L. Tacchi verfasserin aut Benjamin B. A. Raymond verfasserin aut Ania T. Deutscher verfasserin aut Cheryl Jenkins verfasserin aut Matthew P. Padula verfasserin aut Steven P. Djordjevic verfasserin aut In Open Biology The Royal Society, 2012 5(2015), 1 (DE-627)669884146 (DE-600)2630944-0 20462441 nnns volume:5 year:2015 number:1 https://doi.org/10.1098/rsob.140175 kostenfrei https://doaj.org/article/ab1300e372e14bbeaeafff28ffd5c982 kostenfrei https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140175 kostenfrei https://doaj.org/toc/2046-2441 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2005 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 1
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allfieldsGer	10.1098/rsob.140175 doi (DE-627)DOAJ069200920 (DE-599)DOAJab1300e372e14bbeaeafff28ffd5c982 DE-627 ger DE-627 rakwb eng QH301-705.5 Veronica M. Jarocki verfasserin aut MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. adhesin dna-binding protein plasminogen-binding protein heparin-binding protein leucine aminopeptidase moonlighting protein Biology (General) Jerran Santos verfasserin aut Jessica L. Tacchi verfasserin aut Benjamin B. A. Raymond verfasserin aut Ania T. Deutscher verfasserin aut Cheryl Jenkins verfasserin aut Matthew P. Padula verfasserin aut Steven P. Djordjevic verfasserin aut In Open Biology The Royal Society, 2012 5(2015), 1 (DE-627)669884146 (DE-600)2630944-0 20462441 nnns volume:5 year:2015 number:1 https://doi.org/10.1098/rsob.140175 kostenfrei https://doaj.org/article/ab1300e372e14bbeaeafff28ffd5c982 kostenfrei https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140175 kostenfrei https://doaj.org/toc/2046-2441 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2005 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 1
allfieldsSound	10.1098/rsob.140175 doi (DE-627)DOAJ069200920 (DE-599)DOAJab1300e372e14bbeaeafff28ffd5c982 DE-627 ger DE-627 rakwb eng QH301-705.5 Veronica M. Jarocki verfasserin aut MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. adhesin dna-binding protein plasminogen-binding protein heparin-binding protein leucine aminopeptidase moonlighting protein Biology (General) Jerran Santos verfasserin aut Jessica L. Tacchi verfasserin aut Benjamin B. A. Raymond verfasserin aut Ania T. Deutscher verfasserin aut Cheryl Jenkins verfasserin aut Matthew P. Padula verfasserin aut Steven P. Djordjevic verfasserin aut In Open Biology The Royal Society, 2012 5(2015), 1 (DE-627)669884146 (DE-600)2630944-0 20462441 nnns volume:5 year:2015 number:1 https://doi.org/10.1098/rsob.140175 kostenfrei https://doaj.org/article/ab1300e372e14bbeaeafff28ffd5c982 kostenfrei https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140175 kostenfrei https://doaj.org/toc/2046-2441 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2005 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 1
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authorswithroles_txt_mv	Veronica M. Jarocki @@aut@@ Jerran Santos @@aut@@ Jessica L. Tacchi @@aut@@ Benjamin B. A. Raymond @@aut@@ Ania T. Deutscher @@aut@@ Cheryl Jenkins @@aut@@ Matthew P. Padula @@aut@@ Steven P. Djordjevic @@aut@@
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callnumber-first	Q - Science
author	Veronica M. Jarocki
spellingShingle	Veronica M. Jarocki misc QH301-705.5 misc adhesin misc dna-binding protein misc plasminogen-binding protein misc heparin-binding protein misc leucine aminopeptidase misc moonlighting protein misc Biology (General) MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
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topic_title	QH301-705.5 MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae adhesin dna-binding protein plasminogen-binding protein heparin-binding protein leucine aminopeptidase moonlighting protein
topic	misc QH301-705.5 misc adhesin misc dna-binding protein misc plasminogen-binding protein misc heparin-binding protein misc leucine aminopeptidase misc moonlighting protein misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc adhesin misc dna-binding protein misc plasminogen-binding protein misc heparin-binding protein misc leucine aminopeptidase misc moonlighting protein misc Biology (General)
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title	MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
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title_full	MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
author_sort	Veronica M. Jarocki
journal	Open Biology
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author_browse	Veronica M. Jarocki Jerran Santos Jessica L. Tacchi Benjamin B. A. Raymond Ania T. Deutscher Cheryl Jenkins Matthew P. Padula Steven P. Djordjevic
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author-letter	Veronica M. Jarocki
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title_sort	mhj_0461 is a multifunctional leucine aminopeptidase on the surface of mycoplasma hyopneumoniae
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title_auth	MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
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.
abstractGer	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.
abstract_unstemmed	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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title_short	MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae
url	https://doi.org/10.1098/rsob.140175 https://doaj.org/article/ab1300e372e14bbeaeafff28ffd5c982 https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140175 https://doaj.org/toc/2046-2441
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author2	Jerran Santos Jessica L. Tacchi Benjamin B. A. Raymond Ania T. Deutscher Cheryl Jenkins Matthew P. Padula Steven P. Djordjevic
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up_date	2024-07-03T22:02:58.584Z
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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. 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MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae

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