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Interactions between Yersinia pseudotuberculosis and host cells - role of invasin and YopH
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). (Lundgren)
1999 (English)Doctoral thesis, comprehensive summary (Other academic)
Place, publisher, year, edition, pages
Umeå: Umeå universitet , 1999. , 72 p.
Series
Umeå University medical dissertations, ISSN 0346-6612 ; 634
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:umu:diva-65079ISBN: 91-7191-732-2 (print)OAI: oai:DiVA.org:umu-65079DiVA: diva2:603244
Public defence
Föreläsningssalen, Institutionen för mikrobiologi, Umeå universitet, Umeå (English)
Opponent
Supervisors
Note

retroaktiv registrering

Available from: 2013-02-06 Created: 2013-02-05 Last updated: 2013-02-06Bibliographically approved
List of papers
1. Invasin of Yersinia pseudotuberculosis activates human peripheral B cells.
Open this publication in new window or tab >>Invasin of Yersinia pseudotuberculosis activates human peripheral B cells.
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1996 (English)In: Infection and Immunity, ISSN 0019-9567, E-ISSN 1098-5522, Vol. 64, no 3, 829-35 p.Article in journal (Refereed) Published
Abstract [en]

The Yersinia pseudotuberculosis cell surface-located protein invasin was found to promote binding between the pathogen and resting peripheral B cells via beta 1 integrin receptors (CD29). B cells responded by expressing several activation markers and by growing, In contrast, T cells did not react, although these cells express CD29. An isogenic invA mutant failed to activate B cells. The mutation could be complemented by providing the invA+ gene in trans. Purified invasin alone did not activate B cells, although it was able to block the binding of bacteria to the cells.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:umu:diva-61472 (URN)8641788 (PubMedID)
Available from: 2012-11-15 Created: 2012-11-15 Last updated: 2017-12-07
2. Yersinia invasin, a bacterial beta1-integrin ligand, is a potent inducer of lymphocyte motility and migration to collagen type IV and fibronectin.
Open this publication in new window or tab >>Yersinia invasin, a bacterial beta1-integrin ligand, is a potent inducer of lymphocyte motility and migration to collagen type IV and fibronectin.
1997 (English)In: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 159, no 4, 1853-9 p.Article in journal (Refereed) Published
Abstract [en]

The Yersinia pseudotuberculosis invasin protein was found to be a potent inducer of pseudopodia formation and chemotactic and haptotactic migration in human T lymphocytes. Checkerboard analysis confirmed that migration was directional. The Yersinia invasin triggered migration of otherwise poorly migratory normal T cells on fibronectin and in particular on collagen type IV, and augmented the migration of leukemic T cell lines on these components. Invasin-induced lymphocyte migration was inhibited by staurosporin that selectively prevented pseudopodia formation but, noteworthy, augmented adhesion. The motogenic and attractant properties of invasin (Inv) were mediated via beta1-integrins, as shown by lack of effect of Inv on the motility of a beta1-integrin-negative lymphoid cell line and inhibition of invasin-induced lymphocyte motility by anti-beta1 Abs. Inv was markedly more effective than the extracellular matrix components fibronectin, collagen type IV, and laminin, which also interact with lymphocyte beta1-integrins, with respect to induction of pseudopodia, chemotaxis, and haptotaxis. Thus, Yersinia invasin is a model ligand for induction of lymphocyte motility via beta1-integrins. The extraordinary capacity of Inv to trigger and guide T lymphocyte motility and potentiate lymphocyte migration to extracellular matrix components may be of pathogenetic significance for the movement of lymphocytes to extraintestinal sites secondary to Yersinia infection.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:umu:diva-61475 (URN)9257849 (PubMedID)
Available from: 2012-11-15 Created: 2012-11-15 Last updated: 2017-12-07
3. YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis.
Open this publication in new window or tab >>YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis.
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1996 (English)In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 20, no 5, 1057-69 p.Article in journal (Refereed) Published
Abstract [en]

The PTPase YopH of Yersinia is essential to the ability of these bacteria to block phagocytosis. Wild-type Yersinia pseudotuberculosis, but not the yopH mutant strain, resisted phagocytosis by J774 cells. Ingestion of a yopH mutant was dependent on tyrosine kinase activity. Transcomplementation with wild-type yopH restored the anti-phagocytic effect, whereas introduction of the gene encoding the catalytically inactive yopHC403A was without effect. The PTPase inhibitor orthovanadate impaired the anti-phagocytic effect of the wild-type strain, further demonstrating the importance of bacteria-derived PTPase activity for this event. The ability to resist phagocytosis indicates that the effect of the bacterium is immediately exerted when it becomes associated with the phagocyte. Within 30 s after the onset of infection, wild-type Y. pseudotuberculosis caused a YopH-dependent dephosphorylation of phosphotyrosine proteins in J774 cells. Furthermore, interaction of the cells with phagocytosable strains led to a rapid and transient increase in tyrosine phosphorylation of paxillin and some other proteins, an event dependent on the presence of the bacterial surface-located protein invasin. Co-infection with the phagocytosable strain and the wild-type strain abolished the induction of tyrosine phosphorylation. Taken together, the present findings demonstrate an immediate YopH-mediated dephosphorylation of macrophage phosphotyrosine proteins, suggesting that this PTPase acts by preventing early phagocytosis-linked signalling in the phagocyte.

Identifiers
urn:nbn:se:umu:diva-65076 (URN)8809758 (PubMedID)
Available from: 2013-02-05 Created: 2013-02-05 Last updated: 2017-12-06
4. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
Open this publication in new window or tab >>The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
1997 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 16, no 9, 2307-2318 p.Article in journal (Refereed) Published
Abstract [en]

Pathogenic Yersinia resist uptake by eukaryotic cells by a mechanism involving the virulence protein YopH, a protein tyrosine phosphatase. We show that p130Cas and FAK are phosphorylated and recruited to peripheral focal complexes during bacterial uptake in HeLa cells. The inactive form of YopH interacts with the tyrosine phosphorylated forms of FAK and p130Cas and co-localizes with these proteins in focal adhesions. On the other hand, the presence of active YopH results in inhibition of uptake, dephosphorylation of p130Cas and FAK, and disruption of peripheral focal complexes. We suggest that p130Cas and FAK are substrates for YopH and that the dephosphorylation of these proteins impairs the uptake of Yersinia pseudotuberculosis into HeLa cells.

Keyword
FAK, focal adhesions, p130Cas, Yersinia, YopH
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-33371 (URN)10.1093/emboj/16.9.2307 (DOI)9171345 (PubMedID)
Available from: 2010-04-22 Created: 2010-04-22 Last updated: 2017-12-12Bibliographically approved
5. YopH dephosphorylates Cas and Fyn-binding protein in macrophages
Open this publication in new window or tab >>YopH dephosphorylates Cas and Fyn-binding protein in macrophages
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1999 (English)In: Microbial Pathogenesis, ISSN 0882-4010, E-ISSN 1096-1208, Vol. 27, no 4, 231-242 p.Article in journal (Refereed) Published
Abstract [en]

The tyrosine phosphatase YopH is an essential virulence effector of pathogenic Yersinia spp. YopH, which is translocated from extracellularly located bacteria into interacting target cells, blocks phagocytosis by professional phagocytes. We show here that immunoprecipitation of YopH from lysates of J774 cells infected with Y. pseudotuberculosis expressing an inactive form of YopH resulted in co-precipitation of certain phosphotyrosine proteins. The association between the inactive YopH and phosphotyrosine proteins in the 120 kDa range was rapid and could be detected after 2 min of infection. The proteins were identified as the docking proteins Cas and Fyn-binding protein (FYB). Upon infection of J774 cells with Y. pseudotuberculosis lacking YopH expression both of these proteins became tyrosine phosphorylated. Moreover, this infection caused recruitment of Cas to peripheral focal complexes, and FYB was relocalized to areas surrounding these structures. Both Cas and FYB became dephosphorylated upon infection with Y. pseudotuberculosis expressing active YopH, and this was associated with disruption of focal complexes. With regard to the previous identification of Cas and focal complexes as targets of YopH in HeLa cells, the present study supports an important role for these targets in a general mechanism of bacterial uptake. Copyright 1999 Academic Press.

Keyword
Yersinia pseudotuberculosis, phagocytosis, Cas, FYB, focal complexes, PTPase
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:umu:diva-3442 (URN)10.1006/mpat.1999.0301 (DOI)10502464 (PubMedID)
Available from: 2004-01-30 Created: 2004-01-30 Last updated: 2013-02-06Bibliographically approved

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