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Pathogenic E. coli Cause Global Decreases in Ubiquitylated Host Cell Proteins
Author(s) -
Lin Ann E.,
Guttman Julian A
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.523.9
Subject(s) - ubiquitin , biology , extracellular , microbiology and biotechnology , plasmid , ubiquitin ligase , genetics , gene
Enteropathogenic E. coli (EPEC) infections cause severe infantile diarrhea, leading to high mortality in developing countries. These pathogens extensively alter normal host cell functions while remaining extracellular. Ubiquitylation is a widespread post‐translational regulatory system that governs a wide range of cellular events. This process relies on a heierarchical relay system, comprised of E1, E2 and E3 enzymes. Effects of EPEC on the host ubiquitin‐conjugation process have remained elusive. Thus, we sought to test the hypothesis that EPEC alter normal ubiquitylation signaling pathways during their infections. To test this, we infected epithelial cells with EPEC and monitored ubiquitylated protein levels by immunoblotting. We found that the presence of a large plasmid within EPEC called the E. coli adherence factor (EAF) caused a significant decrease in the overall levels of ubiquitylated host proteins. This occurred with a concomitant loss of host E1 activating enzymes, which are essential for initiating the ubiquitylation cascade. We conclude that EPEC exploits E1 enzymes to influence global protein regulatory cascades that are crucial for normal cellular functions. This novel strategy highlights that pathogens can exploit key targets to influence overall protein regulatory systems that are needed for normal cellular functions and disease progression. Grant Funding Source : CIHR