ArticlePloS one2010
Designed coiled-coil peptides inhibit the type three secretion system of enteropathogenic Escherichia coli.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
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- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- Sigma Factor SigB Is Crucial to Mediate Staphylococcus aureus Adaptation during Chronic Infections.PLoS pathogens · 2015Article
- Antibiotic adjuvants: diverse strategies for controlling drug-resistant pathogens.Chemical biology & drug design · 2015Article
- The bacterial type III secretion system as a target for developing new antibiotics.Chemical biology & drug design · 2015Article
- Clade 8 and Clade 6 Strains of Escherichia coli O157:H7 from Cattle in Argentina have Hypervirulent-Like Phenotypes.PloS one · 2015Article
- Azithromycin Reduces the Production of α-hemolysin and Biofilm Formation in Staphylococcus aureus.Indian journal of microbiology · 2014Article
- Mechanism of the Rpn13-induced activation of Uch37.Protein & cell · 2014Article
- EscE and EscG are cochaperones for the type III needle protein EscF of enteropathogenic Escherichia coli.Journal of bacteriology · 2013Article
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- Flavone reduces the production of virulence factors, staphyloxanthin and α-hemolysin, in Staphylococcus aureus.Current microbiology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are two categories of E. coli strains associated with human disease. A major virulence factor of both pathotypes is the expression of a type three secretion system (TTSS), responsible for their ability to adhere to gut mucosa causing a characteristic attaching and effacing lesion (A/E). The TTSS translocates effector proteins directly into the host cell that subvert mammalian cell biochemistry. METHODS/PRINCIPAL
findingsWe examined synthetic peptides designed to inhibit the TTSS. CoilA and CoilB peptides, both representing coiled-coil regions of the translocator protein EspA, and CoilD peptide, corresponding to a coiled-coil region of the needle protein EscF, were effective in inhibiting the TTSS dependent hemolysis of red blood cells by the EPEC E2348/69 strain. CoilA and CoilB peptides also reduced the formation of actin pedestals by the same strain in HEp-2 cells and impaired the TTSS-mediated protein translocation into the epithelial cell. Interestingly, CoilA and CoilB were able to block EspA assembly, destabilizing the TTSS and thereby Tir translocation. This blockage of EspA polymerization by CoilA or CoilB peptides, also inhibited the correct delivery of EspB and EspD as detected by immunoblotting. Interestingly, electron microscopy of bacteria incubated with the CoilA peptide showed a reduction of the length of EspA filaments.
conclusionsOur data indicate that coiled-coil peptides can prevent the assembly and thus the functionality of the TTSS apparatus and suggest that these peptides could provide an attractive tool to block EPEC and EHEC pathogenesis.
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