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Comparative analysis of type III effector translocation by Yersinia pseudotuberculosis expressing native LcrV or PcrV from Pseudomonas aeruginosa.
Umeå University, Faculty of Medicine, Molecular Biology.
Umeå University, Faculty of Medicine, Molecular Biology.
Umeå University, Faculty of Medicine, Molecular Biology.
Umeå University, Faculty of Medicine, Molecular Biology.
2003 (English)In: Journal of Infectious Diseases, ISSN 0022-1899, E-ISSN 1537-6613, Vol. 188, no 2, 239-249 p.Article in journal (Refereed) Published
Description
Abstract [en]

The homologues LcrV of Yersinia species and PcrV of Pseudomonas aeruginosa are pore-forming components. When expressed in a Yersinia lcrV background, PcrV formed smaller pores in infected erythrocyte membranes, correlating to a lowered translocation of Yersinia effectors. To understand this phenomenon, cytotoxins exoenzyme S of P. aeruginosa and YopE of Yersinia were introduced into a Yersinia background without Yop effectors but expressing LcrV or PcrV. Comparable translocation of each substrate indicated that substrate recognition by LcrV/PcrV is not a regulator of translocation. Yersinia harboring pcrV coexpressed with its native operon efficiently translocated effectors into HeLa cell monolayers and formed large LcrV-like pores in erythrocyte membranes. Thus, a PcrV complex with native P. aeruginosa translocon components is required to form fully functional pores for complete complementation of effector translocation in Yersinia.

Place, publisher, year, edition, pages
2003. Vol. 188, no 2, 239-249 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:umu:diva-4144DOI: 10.1086/376452PubMedID: 12854079OAI: oai:DiVA.org:umu-4144DiVA: diva2:143125
Available from: 2004-10-06 Created: 2004-10-06 Last updated: 2017-12-14Bibliographically approved
In thesis
1. Type III secretion- the various functions of the translocon operon in bacterial pathogenesis
Open this publication in new window or tab >>Type III secretion- the various functions of the translocon operon in bacterial pathogenesis
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In order to establish colonisation of a human host, pathogenic Yersinia use a type III protein secretion system to directly intoxicate host immune cells. Activation of this system requires target cell contact and is a highly regulated process. Both the intoxication and regulation events depend on the lcrGVHyopBD translocon operon, which is highly conserved in many bacterial pathogens. In this study, the role of individual operon members was analysed and functional domains identified by using the highly homologous pcrGVHpopBD operon of P. aeruginosa as a comparative tool.

Yersinia spp. and P. aeruginosa were shown to form translocation pores of a similar size that promoted equally efficient protein delivery. A strong dependency on interactions between native translocator(s) in protein delivery was revealed, suggesting that each pathogen has delicately fine-tuned this process to suit its own infection niche. In particular, the C-terminus of YopD was shown to possess functional specificity for effector delivery in Yersinia that could not be conferred by the comparable region in homologous PopD. Moreover, a role for LcrV and PcrV in substrate recognition during the protein delivery process was excluded.

The N-terminus of LcrH was recognized as a unique regulatory domain, mediating formation of LcrH-YscY regulatory complexes in Yersinia, while equivalent complexes with analogous proteins were not formed in P. aeruginosa. These results compliment the idea that a negative regulatory pathway involving LcrH, YopD, LcrQ and YscY is unique to Yersinia.

Finally, PcrH was identified as a new member of the translocator class of chaperones, being essential for assembly of a functional PopB/PopD mediated translocon in P. aeruginosa. However, in contrast to the other members of this family, PcrH was dispensable for type III regulation. Moreover, both LcrH and PcrH were shown to possess tetratricopeptide repeats crucial for their chaperone function. One tetratricopeptide repeat mutant in LcrH was even isolated that failed to secrete both YopB and YopD substrates, even though stability was maintained. This demonstrates for the first time that LcrH has a role in substrate secretion in addition to its critical role in promoting substrate stability.

Place, publisher, year, edition, pages
Umeå: Molekylärbiologi, 2004. 82 p.
Keyword
Molecular biology, Yersinia, Pseudomonas aeruginosa, type III secretion, chaperone, translocation, regulation, lcrGVHyopBD, pcrGVHpopBD, Molekylärbiologi
National Category
Biochemistry and Molecular Biology
Research subject
Molecular Biology
Identifiers
urn:nbn:se:umu:diva-331 (URN)91-7305-712-6 (ISBN)
Public defence
2004-11-05, Major Groove, 6L, NUS, Umeå Universitet, 90187, Umeå, 09:00
Opponent
Supervisors
Available from: 2004-10-06 Created: 2004-10-06Bibliographically approved
2. Type III Secretion Mediated Translocation of Effector Exoenzymes by Pseudomonas aeruginosa
Open this publication in new window or tab >>Type III Secretion Mediated Translocation of Effector Exoenzymes by Pseudomonas aeruginosa
2003 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Injektion av gifter via typ III sekretionssystemet hos bakterien Pseudomonas aeruginosa
Publisher
52 p.
Keyword
Cell and molecular biology, Pseudomonas aeruginosa, type III secretion system, ExoS, ExoT, PcrV, PcrG, PopB, PopD, PopN, type IV pili, Cell- och molekylärbiologi
National Category
Biochemistry and Molecular Biology
Research subject
Molecular Biology
Identifiers
urn:nbn:se:umu:diva-174 (URN)91-7305-545-X (ISBN)
Public defence
2003-11-28, Major Groove, 6L, Norrlands Universitetssjukhus, Umeå, 09:00 (English)
Opponent
Supervisors
Available from: 2003-12-23 Created: 2003-12-23 Last updated: 2010-02-24Bibliographically approved

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