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Plasminogen activator Pla of Yersinia pestis utilizes murine DEC-205 (CD205) as a receptor to promote dissemination
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). (Hans Wolf-Watz)
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2008 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 283, no 46, 31511-21 p.Article in journal (Refereed) Published
Abstract [en]

Yersinia pestis, a Gram-negative bacterium that causes bubonic and pneumonic plague, is able to rapidly disseminate to other parts of its mammalian hosts. Y. pestis expresses plasminogen activator (PLA) on its surface, which has been suggested to play a role in bacterial dissemination. It has been speculated that Y. pestis hijacks antigen-presenting cells, such as macrophages (MPhis) and dendritic cells, to be delivered to lymph nodes to initiate dissemination and infection. Both alveolar MPhis and pulmonary dendritic cells express a C-type lectin receptor, DEC-205 (CD205), which mediates antigen uptake and presentation. However, no ligand has been identified for DEC-205. In this study, we show that the invasion of alveolar MPhisby Y. pestis depends both in vitro and in vivo on the expression of PLA. DEC-205-expressing MPhis and transfectants, but not their negative counterparts, phagocytosed PLA-expressing Y. pestis and Escherichia coli K12 more efficiently than PLA-negative controls. The interactions between PLA-expressing bacteria and DEC-205-expressing transfectants or alveolar MPhis could be inhibited by an anti-DEC-205 antibody. Importantly, the blockage of the PLA-DEC-205 interaction reduced the dissemination of Y. pestis in mice. In conclusion, murine DEC-205 is a receptor for PLA of Y. pestis, and this host-pathogen interaction appears to play a key role in promoting bacterial dissemination.

Place, publisher, year, edition, pages
2008. Vol. 283, no 46, 31511-21 p.
National Category
Microbiology in the medical area
URN: urn:nbn:se:umu:diva-33948DOI: 10.1074/jbc.M804646200PubMedID: 18650418OAI: diva2:318867
Available from: 2010-05-11 Created: 2010-05-11 Last updated: 2010-06-03Bibliographically approved
In thesis
1. Outer membrane proteins of Yersinia pestis: Ail and OmpA
Open this publication in new window or tab >>Outer membrane proteins of Yersinia pestis: Ail and OmpA
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

A vast number of studies have been completed on the virulence determinants of Yersinia spp.; however, the focus of many of these studies has been on the virulence plasmid and the plasmid-encoded Type three secretion system. Nevertheless, many chromosomal genes whose products are directly involved in virulence have also been identified. Some of these critical virulence determinants are outer membrane proteins. Outer membrane proteins of Gram-negative bacteria often have important physiological roles; however, some have also been found to be important for pathogenesis. In this thesis, we investigated two Yersinia. pestis outer membrane proteins, Ail and OmpA, and their roles in virulence. We provide evidence that Y. pestis Ail is a highly expressed outer membrane protein that is absolutely essential for Y. pestis to resist the killing action of the complement system present in human blood and tissues, as well as the blood and tissues of other mammalian hosts. Furthermore, Ail was important for virulence in a Y. pestis-Canorhabditis elegans model of infection.The work in this thesis also provided the first evidence that another surface-exposed outer membrane protein, termed OmpA, is required for both Yersinia pseudotuberculosis and Y. pestis to survive and proliferate intracellularly in macrophages. Finally, we provide evidence that Y. pestis has a functional small RNA MicA that controls the expression of OmpA. This is the first demonstration of sRNA-mediated regulation of a Yersinia virulence factor. This work has paved the way for future studies on the role of outer membrane proteins in virulence, particularly the role of Ail and OmpA.

Place, publisher, year, edition, pages
Umeå: Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet), Umeå universitet, 2010. 89 p.
Doctoral thesis / Umeå University, Department of Molecular Biology
Yersinia pestis, outer membrane proteins, Ail, ompA
National Category
Microbiology in the medical area
Research subject
Immunology; Microbiology; Infectious Diseases
urn:nbn:se:umu:diva-33956 (URN)978-91-7459-030-2 (ISBN)
Public defence
2010-06-03, Molekylärbiologi, Major Groove, Byggnad 6L, Umeå universitet, Umeå, 10:00 (English)
Available from: 2010-05-12 Created: 2010-05-11 Last updated: 2010-05-18Bibliographically approved

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