TY  - JOUR
AB  - Several immunoglobulin-binding proteins of Escherichia coli (Eib) have been isolated from both non-pathogenic and pathogenic E. coli strains. Shiga toxin (Stx)-producing E. coli (STEC) contain eibG either as a single gene or in combination with eibC, while other E. coli strains harbour single or multiple eib genes. The Eib proteins bind human immunoglobulins in a non-immune manner and contribute to bacterial chain-like adherence to human epithelial cells. In this study, the EibG expression in several STEC strains was analysed under different environmental conditions. STEC produced high levels of EibG in complex media and lower levels in low-grade and minimal media under static growth conditions. This characteristic was independent on the Eib subtypes. Microscopically, EibG-expressing STEC exhibited chain formation and aggregation in all employed media, while aggregates were only visible after growth in complex medium. Once expressed, EibG proteins demonstrate high stability during prolonged incubation. Our findings indicate that the regulation of the expression of Eib proteins is highly complex, although the protein levels vary among STEC strains. However, positive upregulation conditions generally result in distinct phenotypes of the isolates.
AU  - Rubin, Dennis
AU  - Zhang, Wenlan
AU  - Karch, Helge
AU  - Kuczius, Thorsten
DA  - 2017-04-29
DO  - 10.3390/toxins9050153
KW  - regulation
KW  - expression
KW  - immunoglobulin-binding protein G
KW  - Shiga toxin-producing Escherichia coli
LA  - eng
N1  - Toxins 9 (2017) 5, 153, 1-13
N1  - Finanziert durch den Open-Access-Publikationsfonds 2017 der Westfälischen Wilhelms-Universität Münster (WWU Münster).
PY  - 2017-04-29
TI  - Distinct Expression of Immunoglobulin-Binding Proteins in Shiga Toxin-Producing Escherichia coli Implicates High Protein Stability and a Characteristic Phenotype
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:6-97119524079
Y2  - 2024-11-22T06:58:17
ER  -