Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae

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 o...

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Autores principales:	Iain J. Berry, Michael Widjaja, Veronica M. Jarocki, Joel R. Steele, Matthew P. Padula, Steven P. Djordjevic
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b6ce397eb1f54279928c55652021054d
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spelling	oai:doaj.org-article:b6ce397eb1f54279928c55652021054d2021-12-02T14:02:54ZProtein cleavage influences surface protein presentation in Mycoplasma pneumoniae10.1038/s41598-021-86217-y2045-2322https://doaj.org/article/b6ce397eb1f54279928c55652021054d2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86217-yhttps://doaj.org/toc/2045-2322Abstract 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.Iain J. BerryMichael WidjajaVeronica M. JarockiJoel R. SteeleMatthew P. PadulaSteven P. DjordjevicNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Iain J. Berry Michael Widjaja Veronica M. Jarocki Joel R. Steele Matthew P. Padula Steven P. Djordjevic Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
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.
format	article
author	Iain J. Berry Michael Widjaja Veronica M. Jarocki Joel R. Steele Matthew P. Padula Steven P. Djordjevic
author_facet	Iain J. Berry Michael Widjaja Veronica M. Jarocki Joel R. Steele Matthew P. Padula Steven P. Djordjevic
author_sort	Iain J. Berry
title	Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
title_short	Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
title_full	Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
title_fullStr	Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
title_full_unstemmed	Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
title_sort	protein cleavage influences surface protein presentation in mycoplasma pneumoniae
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b6ce397eb1f54279928c55652021054d
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Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae

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