Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.

Berry, IJ; Widjaja, M; Jarocki, VM; Steele, JR; Padula, MP; Djordjevic, SP

Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.

Berry, IJ Widjaja, M Jarocki, VM Steele, JR Padula, MP Djordjevic, SP

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Publisher:: Springer Science and Business Media LLC
Publication Type:: Journal Article
Citation:: Scientific reports, 2021, 11, (1), pp. 6743
Issue Date:: 2021-03-24

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Field	Value	Language
dc.contributor.author	Berry, IJ
dc.contributor.author	Widjaja, M
dc.contributor.author	Jarocki, VM
dc.contributor.author	Steele, JR
dc.contributor.author	Padula, MP
dc.contributor.author	Djordjevic, SP
dc.date.accessioned	2021-03-30T16:42:25Z
dc.date.available	2021-02-23
dc.date.available	2021-03-30T16:42:25Z
dc.date.issued	2021-03-24
dc.identifier.citation	Scientific reports, 2021, 11, (1), pp. 6743
dc.identifier.issn	2045-2322
dc.identifier.issn	2045-2322
dc.identifier.uri	http://hdl.handle.net/10453/147686
dc.description.abstract	Mycoplasma pneumoniae is a significant cause of pneumonia and post infection sequelae affecting organ sites distant to the respiratory tract are common. It is also a model organism where extensive 'omics' studies have been conducted to gain insight into how minimal genome self-replicating organisms function. An N-terminome study undertaken here identified 4898 unique N-terminal peptides that mapped to 391 (56%) predicted M. pneumoniae proteins. True N-terminal sequences beginning with the initiating methionine (iMet) residue from the predicted Open Reading Frame (ORF) were identified for 163 proteins. Notably, almost half (317; 46%) of the ORFS derived from M. pneumoniae strain M129 are post-translationally modified, presumably by proteolytic processing, because dimethyl labelled neo-N-termini were characterised that mapped beyond the predicted N-terminus. An analysis of the N-terminome describes endoproteolytic processing events predominately targeting tryptic-like sites, though cleavages at negatively charged residues in P1' (D and E) with lysine or serine/alanine in P2' and P3' positions also occurred frequently. Surfaceome studies identified 160 proteins (23% of the proteome) to be exposed on the extracellular surface of M. pneumoniae. The two orthogonal methodologies used to characterise the surfaceome each identified the same 116 proteins, a 72% (116/160) overlap. Apart from lipoproteins, transporters, and adhesins, 93/160 (58%) of the surface proteins lack signal peptides and have well characterised, canonical functions in the cell. Of the 160 surface proteins identified, 134 were also targets of endo-proteolytic processing. These processing events are likely to have profound implications for how the host immune system recognises and responds to M. pneumoniae.
dc.format	Electronic
dc.language	eng
dc.publisher	Springer Science and Business Media LLC
dc.relation.ispartof	Scientific reports
dc.relation.isbasedon	10.1038/s41598-021-86217-y
dc.rights	info:eu-repo/semantics/closedAccess
dc.title	Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae.
dc.type	Journal Article
utslib.citation.volume	11
utslib.location.activity	England
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access	*
dc.date.updated	2021-03-30T16:42:21Z
pubs.issue	1
pubs.publication-status	Published
pubs.volume	11
utslib.citation.issue	1

Abstract:

Mycoplasma pneumoniae is a significant cause of pneumonia and post infection sequelae affecting organ sites distant to the respiratory tract are common. It is also a model organism where extensive 'omics' studies have been conducted to gain insight into how minimal genome self-replicating organisms function. An N-terminome study undertaken here identified 4898 unique N-terminal peptides that mapped to 391 (56%) predicted M. pneumoniae proteins. True N-terminal sequences beginning with the initiating methionine (iMet) residue from the predicted Open Reading Frame (ORF) were identified for 163 proteins. Notably, almost half (317; 46%) of the ORFS derived from M. pneumoniae strain M129 are post-translationally modified, presumably by proteolytic processing, because dimethyl labelled neo-N-termini were characterised that mapped beyond the predicted N-terminus. An analysis of the N-terminome describes endoproteolytic processing events predominately targeting tryptic-like sites, though cleavages at negatively charged residues in P1' (D and E) with lysine or serine/alanine in P2' and P3' positions also occurred frequently. Surfaceome studies identified 160 proteins (23% of the proteome) to be exposed on the extracellular surface of M. pneumoniae. The two orthogonal methodologies used to characterise the surfaceome each identified the same 116 proteins, a 72% (116/160) overlap. Apart from lipoproteins, transporters, and adhesins, 93/160 (58%) of the surface proteins lack signal peptides and have well characterised, canonical functions in the cell. Of the 160 surface proteins identified, 134 were also targets of endo-proteolytic processing. These processing events are likely to have profound implications for how the host immune system recognises and responds to M. pneumoniae.

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http://hdl.handle.net/10453/147686