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PMID: 1705028 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 4 ·1991-02-15 ·Pages 1187-91

Bliska JB, Guan KL, Dixon JE, Falkow S

Abstract

The plasmid-encoded YopH protein is a protein-tyrosine phosphatase (PTPase; EC 3.1.3.48) that is essential for Yersinia virulence. We have investigated the molecular basis for the role of PTPase activity in Yersinia pathogenesis. Allelic recombination was employed to introduce a defined mutation into the yopH plasmid gene. Conversion of the essential Cys-403 to Ala in the catalytic domain of the protein abolished YopH PTPase activity and significantly reduced the virulence of Yersinia pseudotuberculosis in a murine infection model. 32P-labeled phosphotyrosine-containing proteins were immunoprecipitated from extracts of Y. pseudotuberculosis-infected cell monolayers and analyzed by SDS/PAGE to assess the impact of YopH on host protein phosphorylation. Major proteins of 200, 120, and 60 kDa were dephosphorylated in macrophages associated with wild-type Y. pseudotuberculosis. Selective removal of phosphate from the 120- and 60-kDa proteins was shown to be specific to the YopH PTPase activity. Phagocytosis of the bacteria was not required for this dephosphorylation activity, suggesting that YopH is functionally expressed by extracellular bacteria. These observations indicate that the essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation.

Related Genes
yop51 yopH
MeSH Terms
Animals Cell Line Escherichia coli/genetics Gene Expression Kinetics Macrophages Mice Mutagenesis, Site-Directed Phosphates/metabolism Phosphoprotein Phosphatases/genetics Phosphotyrosine Plasmids Protein Tyrosine Phosphatases Recombination, Genetic Restriction Mapping Substrate Specificity Tyrosine/analogs & derivatives,metabolism Virulence Yersinia pseudotuberculosis/genetics,metabolism,pathogenicity
Chemicals
Phosphates Phosphotyrosine Tyrosine Phosphoprotein Phosphatases Protein Tyrosine Phosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bliska J B
Department of Microbiology and Immunology, Stanford University School of Medicine, CA 94305.
Guan K L
Dixon J E
Falkow S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.4.1187
Published
1991-02-15
Pages
1187-91
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC50982
Subset
IM
Grants
PHS HHS · 18849 · United States
NIAID NIH HHS · AI07851-01 · United States
NIAID NIH HHS · AI26195 · United States
External Links
PubMed source DOI: 10.1073/pnas.88.4.1187 PMC Full Text View journal details
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