Characterisation of the Bordetella pertussis secretome under different media.

Luu, LDW; Octavia, S; Zhong, L; Raftery, M; Sintchenko, V; Lan, R

Characterisation of the Bordetella pertussis secretome under different media.

Luu, LDW Octavia, S Zhong, L Raftery, M Sintchenko, V Lan, R

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Publisher:: Elsevier
Publication Type:: Journal Article
Citation:: Journal of Proteomics, 2017, 158, pp. 43-51
Issue Date:: 2017-03-31

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Field	Value	Language
dc.contributor.author	Luu, LDW
dc.contributor.author	Octavia, S
dc.contributor.author	Zhong, L
dc.contributor.author	Raftery, M
dc.contributor.author	Sintchenko, V
dc.contributor.author	Lan, R
dc.date.accessioned	2022-09-06T03:57:10Z
dc.date.available	2017-02-14
dc.date.available	2022-09-06T03:57:10Z
dc.date.issued	2017-03-31
dc.identifier.citation	Journal of Proteomics, 2017, 158, pp. 43-51
dc.identifier.issn	1874-3919
dc.identifier.issn	1876-7737
dc.identifier.uri	http://hdl.handle.net/10453/161419
dc.description.abstract	Our understanding of the Bordetella pertussis secretome remains limited including the role of different growth conditions in the secretome. In this study the secretome of L1423, a clinical isolate from the 2008-2012 Australian epidemic, cultured on Stainer-Scholte (SS) and Thalen-IJssel (THIJS) media for 12h was characterised using liquid chromatography-mass spectrometry (LC-MS/MS). In the supernatant, LC-MS/MS identified 260 proteins with 143 bioinformatically predicted to be secreted. Eighty percent of proteins were identified in both media. Proteins secreted were functionally associated with cell surface (41%), pathogenicity (16%) and transport (17%). The most abundant proteins identified were pathogenic proteins including toxins (PtxA and CyaA), adhesins (TcfA) and type III secretion (T3SS) proteins. There were 46 proteins found uniquely in THIJS including 8 virulence associated proteins. These included T3SS proteins, adhesins (FhaL and FhaS) and a putative toxin (BP1251). Nine proteins were found uniquely in SS and these were metabolic and transport-related proteins. None of the unique proteins detected in SS were known to be virulence associated. This study found that THIJS promotes secretion of virulence factors based on the number of unique virulence proteins found and may be a growth media of choice for the study of B. pertussis virulence and vaccine development. BIOLOGICAL SIGNIFICANCE: Over the past two decades, the number of B. pertussis notifications has risen despite vaccination. There is a greater need to understand the biology behind B. pertussis infections. The secretome of B. pertussis in two different media was characterised using LC-MS/MS. The results showed that THIJS promotes secretion of importance virulence factors which may be important for the development of vaccines.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	Elsevier
dc.relation.ispartof	Journal of Proteomics
dc.relation.isbasedon	10.1016/j.jprot.2017.02.010
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	0601 Biochemistry and Cell Biology, 0607 Plant Biology
dc.subject.classification	Analytical Chemistry
dc.subject.classification	Biochemistry & Molecular Biology
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Bordetella pertussis
dc.subject.mesh	Culture Media
dc.subject.mesh	Proteome
dc.subject.mesh	Proteomics
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Bordetella pertussis
dc.subject.mesh	Culture Media
dc.subject.mesh	Proteome
dc.subject.mesh	Proteomics
dc.subject.mesh	Bordetella pertussis
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Proteome
dc.subject.mesh	Culture Media
dc.subject.mesh	Proteomics
dc.title	Characterisation of the Bordetella pertussis secretome under different media.
dc.type	Journal Article
utslib.citation.volume	158
utslib.location.activity	Netherlands
utslib.for	0601 Biochemistry and Cell Biology
utslib.for	0607 Plant Biology
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
utslib.copyright.status	closed_access	*
pubs.consider-herdc	false
dc.date.updated	2022-09-06T03:57:08Z
pubs.publication-status	Published
pubs.volume	158

Abstract:

Our understanding of the Bordetella pertussis secretome remains limited including the role of different growth conditions in the secretome. In this study the secretome of L1423, a clinical isolate from the 2008-2012 Australian epidemic, cultured on Stainer-Scholte (SS) and Thalen-IJssel (THIJS) media for 12h was characterised using liquid chromatography-mass spectrometry (LC-MS/MS). In the supernatant, LC-MS/MS identified 260 proteins with 143 bioinformatically predicted to be secreted. Eighty percent of proteins were identified in both media. Proteins secreted were functionally associated with cell surface (41%), pathogenicity (16%) and transport (17%). The most abundant proteins identified were pathogenic proteins including toxins (PtxA and CyaA), adhesins (TcfA) and type III secretion (T3SS) proteins. There were 46 proteins found uniquely in THIJS including 8 virulence associated proteins. These included T3SS proteins, adhesins (FhaL and FhaS) and a putative toxin (BP1251). Nine proteins were found uniquely in SS and these were metabolic and transport-related proteins. None of the unique proteins detected in SS were known to be virulence associated. This study found that THIJS promotes secretion of virulence factors based on the number of unique virulence proteins found and may be a growth media of choice for the study of B. pertussis virulence and vaccine development. BIOLOGICAL SIGNIFICANCE: Over the past two decades, the number of B. pertussis notifications has risen despite vaccination. There is a greater need to understand the biology behind B. pertussis infections. The secretome of B. pertussis in two different media was characterised using LC-MS/MS. The results showed that THIJS promotes secretion of importance virulence factors which may be important for the development of vaccines.

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http://hdl.handle.net/10453/161419