Sökning: WFRF:(Wolf M.)
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YopH of Yersinia ps...
YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis.
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Andersson, K (författare)
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- Carballeira Suarez, N (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Lundgren
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Magnusson, K E (författare)
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visa fler...
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Persson, C (författare)
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Stendahl, O (författare)
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- Wolf-Watz, H (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet),Wolf-Watz
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- Fällman, M (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Fällman
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visa färre...
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(creator_code:org_t)
- 1996
- 1996
- Engelska.
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Ingår i: Molecular Microbiology. - 0950-382X .- 1365-2958. ; 20:5, s. 1057-69
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
Stäng
- 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.
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