YopH dephosphorylates Cas and Fyn-binding protein in macrophages
1999 (English)In: Microbial Pathogenesis, ISSN 0882-4010, E-ISSN 1096-1208, Vol. 27, no 4, 231-242 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
1999. Vol. 27, no 4, 231-242 p.
Yersinia pseudotuberculosis, phagocytosis, Cas, FYB, focal complexes, PTPase
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:umu:diva-3442DOI: 10.1006/mpat.1999.0301PubMedID: 10502464OAI: oai:DiVA.org:umu-3442DiVA: diva2:142137