Maltoporins and maltose-binding proteins of Yersinia enterocolitica

Abstract

Two components of the

The level of Yop proteins secreted by Yersinia enterocolitica is changed in maltose mutants

“…PulD is the protein involved in the secretion of pullulanase whose expression is induced by growth in the presence of this sugar and it is positively regulated by MalT protein [23]. Our preliminary studies on the maltose induction of LamB and MBP proteins of Y. enterocolitica indicate that the MalT regulator exists in Y. enterocolitica [12]. The explanation for the role of the maltose system in the secretion of Yop proteins needs further experimental analysis.…”

“…It is likely that other still unidenti¢ed regulons (maltose regulon) of Y. enterocolitica may assist in the ¢ne-tuning of virulence genes required for successful infection. We have previously identi¢ed two components of the Y. enterocolitica maltose transport system, maltoporin (OmpM) and maltose binding proteins (MBPs), analogous to LamB and MBP of Escherichia coli, respectively [12,13]. The aim of this work was to determine whether the maltose system could a¡ect the production and secretion of Yop proteins, virulence factors of Y. enterocolitica.…”

Production of Escherichia coli LamB protein in Yersinia enterocolitica

“…2, lanes 4, 6, 7). The differences in apparent M, between the chromosomally coded LamB protein and OmpM were previously observed [9]. To determine the receptor ability of LamB protein expressed in the OM of Y. enterocolitica an adsorption experiment was performed.…”

“…Major outer membrane (OM) proteins have been identified in Y enterocolitica that are physicochemically and functionally similar to the OmpA, OmpF and OmpC of E. coli [6-81. Recently, an inducible major OmpM protein of Y. enterocolitica analogous to the maltoporin LamB (the receptor for h phage) of E. coli [9] was described. The OmpM protein of Y. enterocoliticu differed from the LamB protein of E. coli in that the M, of LamB monomer was 47392 [21] whereas the apparent M, of OmpM was only 43 000, and that the OmpM did not serve as a receptor for A phage.…”

The level of Yop proteins secreted byYersinia enterocoliticais changed in maltose mutants

“…It is likely that other still unidentified regulons (maltose regulon) of Y. enterocolitica may assist in the fine‐tuning of virulence genes required for successful infection. We have previously identified two components of the Y. enterocolitica maltose transport system, maltoporin (OmpM) and maltose binding proteins (MBPs), analogous to LamB and MBP of Escherichia coli , respectively [12,13]. The aim of this work was to determine whether the maltose system could affect the production and secretion of Yop proteins, virulence factors of Y. enterocolitica .…”