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Background  The serine proteases HtrA/DegP secreted by the human gastrointestinal pathogens  Helicobacter pylori  ( H. pylori ) and  Campylobacter jejuni  ( C. jejuni ) cleave the mammalian cell adhesion protein E-cadherin to open intercellular adhesions. A wide range of bacteria also expresses the HtrA/DegP homologs DegQ and/or DegS, which significantly differ in structure and function.    Methods  E-cadherin shedding was investigated in infection experiments with the Gram-negative pathogens  H. pylori , enteropathogenic  Escherichia coli  (EPEC),  Salmonella enterica  subsp. Enterica ( S.  Typhimurium),  Yersinia enterocolitica  ( Y. enterocolitica ), and  Proteus mirabilis  ( P. mirabilis ), which express different combinations of HtrAs. Annotated wild-type  htrA / degP ,  degQ  and  degS  genes were cloned and proteolytically inactive mutants were generated by a serine—to—alanine exchange in the active center. All HtrA variants were overexpressed and purified to compare their proteolytic activities in casein zymography and in vitro E-cadherin cleavage experiments.    Results  Infection of epithelial cells resulted in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin (NTF) in the supernatants of infected cells. Importantly, comparing the caseinolytic and E-cadherin cleavage activities of HtrA/DegP, DegQ and DegS proteins revealed that DegP and DegQ homologs from  H. pylori ,  S.  Typhimurium,  Y. enterocolitica , EPEC and  P. mirabilis , but not activated DegS, cleaved E-cadherin as a substrate in vitro.    Conclusions  These data indicate that E-cadherin cleavage is confined to HtrA/DegP and DegQ proteins representing an important prevalent step in bacterial pathogenesis.    Electronic supplementary material  The online version of this article (doi:10.1186/s12964-016-0153-y) contains supplementary material, which is available to authorized users.

HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogens