CtHtrA: The lynchpin of the chlamydial surface and a promising therapeutic target

Marsh, JW; Ong, VA; Lott, WB; Timms, P; Tyndall, JDA; Huston, WM

CtHtrA: The lynchpin of the chlamydial surface and a promising therapeutic target

Marsh, JW

Ong, VA Lott, WB Timms, P Tyndall, JDA Huston, WM

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Publication Type:: Journal Article
Citation:: Future Microbiology, 2017, 12 (9), pp. 817 - 829
Issue Date:: 2017-07-01

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Field	Value	Language
dc.contributor.author	Marsh, JW https://orcid.org/0000-0003-4681-1012	en_US
dc.contributor.author	Ong, VA	en_US
dc.contributor.author	Lott, WB	en_US
dc.contributor.author	Timms, P	en_US
dc.contributor.author	Tyndall, JDA	en_US
dc.contributor.author	Huston, WM https://orcid.org/0000-0002-0879-1287	en_US
dc.date.available	2020-05-25T19:10:11Z
dc.date.issued	2017-07-01	en_US
dc.identifier.citation	Future Microbiology, 2017, 12 (9), pp. 817 - 829	en_US
dc.identifier.issn	1746-0913	en_US
dc.identifier.uri	http://hdl.handle.net/10453/103985
dc.description.abstract	© 2017 Future Medicine Ltd. Chlamydia trachomatis is the most prevalent sexually transmitted bacterial infection worldwide and the leading cause of preventable blindness. Reports have emerged of treatment failure, suggesting a need to develop new antibiotics to battle Chlamydia infection. One possible candidate for a new treatment is the protease inhibitor JO146, which is an effective anti-Chlamydia agent that targets the CtHtrA protein. CtHtrA is a lynchpin on the chlamydial cell surface due to its essential and multifunctional roles in the bacteria's stress response, replicative phase of development, virulence and outer-membrane protein assembly. This review summarizes the current understanding of CtHtrA function and presents a mechanistic model that highlights CtHtrA as an effective target for anti-Chlamydia drug development.	en_US
dc.relation.ispartof	Future Microbiology	en_US
dc.relation.isbasedon	10.2217/fmb-2017-0017	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Chlamydia trachomatis	en_US
dc.subject.mesh	Chlamydia Infections	en_US
dc.subject.mesh	Serine Endopeptidases	en_US
dc.subject.mesh	Dipeptides	en_US
dc.subject.mesh	Bacterial Outer Membrane Proteins	en_US
dc.subject.mesh	Virulence Factors	en_US
dc.subject.mesh	Protease Inhibitors	en_US
dc.subject.mesh	Anti-Bacterial Agents	en_US
dc.subject.mesh	Models, Biological	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Organophosphonates	en_US
dc.title	CtHtrA: The lynchpin of the chlamydial surface and a promising therapeutic target	en_US
dc.type	Journal Article
utslib.citation.volume	9	en_US
utslib.citation.volume	12	en_US
utslib.for	1108 Medical Microbiology	en_US
utslib.for	0605 Microbiology	en_US
pubs.embargo.period	Not known	en_US
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
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	open_access
pubs.issue	9	en_US
pubs.publication-status	Published	en_US
pubs.volume	12	en_US

Abstract:

© 2017 Future Medicine Ltd. Chlamydia trachomatis is the most prevalent sexually transmitted bacterial infection worldwide and the leading cause of preventable blindness. Reports have emerged of treatment failure, suggesting a need to develop new antibiotics to battle Chlamydia infection. One possible candidate for a new treatment is the protease inhibitor JO146, which is an effective anti-Chlamydia agent that targets the CtHtrA protein. CtHtrA is a lynchpin on the chlamydial cell surface due to its essential and multifunctional roles in the bacteria's stress response, replicative phase of development, virulence and outer-membrane protein assembly. This review summarizes the current understanding of CtHtrA function and presents a mechanistic model that highlights CtHtrA as an effective target for anti-Chlamydia drug development.

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http://hdl.handle.net/10453/103985