About this Biochemistry, Genetics and Molecular Biology article

Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus by Elzbieta Skrzypek; Clarissa Cowan; Susan C. Straley is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

The YopM virulence protein of Yersinia pestis has been described as binding human alpha-thrombin and inhibiting thrombin-induced platelet aggregation in vitro. However, recent studies have shown that a YopM-CyaA fusion protein could be targeted vectorially into eukaryotic cells through the Yersinia type III secretion system. In this study, our objective was to characterize YopM's fate in more detail. We followed YopM in the culture medium and inside infected HeLa cells. We confirmed that the native YopM is targeted into HeLa cells, where it is insensitive to exogenous trypsin. The bacteria must be surface located to target YopM, and YopB and YopD are necessary, whereas the LcrE protein (called also YopN) makes this process more efficient. Immunofluorescence localization revealed that YopM, in contrast to YopE, is not only targeted to the cytoplasm but also trafficks to the cell's nucleus by means of a vesicle-associated pathway that is strongly inhibited by brefeldin A, perturbed by monensin or bafilomycin A1 and dependent upon microtubules (decreased by colchicine and nocodazole). These findings revealed a novel interaction of Yersinia pestis with its eukaryotic host.

Author

Elzbieta Skrzypek; Clarissa Cowan; Susan C. Straley

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0950-382X)

Published

1999

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)