Microbial Biofilms: Their Development and Significance for Medical Device—Related Infections

Habash, Marc; Reid, Gregor

doi:10.1177/00912709922008506

Cited by 244 publications

(155 citation statements)

References 95 publications

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“…Bacterial infections on implanted medical devices such as catheters and pacemakers can lead to serious complications and often device removal because the adherent bacterial can form a biofilm, which provides a protective environment for bacteria against antibiotics and immune responses (Costerton et al, 1999;Habash & Reid, 1999).…”

Section: Introductionmentioning

confidence: 99%

Surface-immobilised antimicrobial peptoids

et al. 2008

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Surface modification techniques that create surfaces capable of killing adherent bacteria are promising solutions to infections associated with implantable medical devices. Antimicrobial peptoid oligomers (ampetoids) that were designed to mimic helical antimicrobial peptides were synthesized with a peptoid spacer chain to allow mobility and an adhesive peptide moiety for easy and robust immobilization onto substrates. TiO 2 substrates were modified with the ampetoids and subsequently backfilled with an antifouling polypeptoid polymer in order to create polymer surface coatings composed of both antimicrobial (active) and antifouling (passive) peptoid functionalities. Confocal microscopy images show that the membranes of adherent E. coli were damaged after 2 h exposure to the modified substrates, suggesting that ampetoids retain antimicrobial properties even when immobilized onto substrates.

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Section: Introductionmentioning

confidence: 99%

Surface-immobilised antimicrobial peptoids

et al. 2008

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“…The formation of biofilms represents a common strategy by which bacteria resist mechanical and chemical clearance mechanisms of the host (13)(14)(15). Biofilms can facilitate the persistence and recurrence of infections (16,17), lead to the colonization of medical devices with resistant organisms (18,19), and increase transmission of foodborne illnesses (20). It is therefore important to understand the mechanism of curli biogenesis to develop treatments and therapeutic agents in biofilm-related infections (21).…”

mentioning

confidence: 99%

Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation

Krezel

Cusumano

Pinkner

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of Escherichia coli, as well as many other enteric bacteria, and are involved in cell colonization and biofilm formation. CsgE is a periplasmic accessory protein that plays a crucial role in curli biogenesis. CsgE binds to both CsgA and the nonameric pore protein CsgG. The CsgG-CsgE complex is the curli secretion channel and is essential for the formation of the curli fibril in vivo. To better understand the role of CsgE in curli formation, we have determined the solution NMR structure of a double mutant of CsgE (W48A/F79A) that appears to be similar to the wild-type (WT) protein in overall structure and function but does not form mixed oligomers at NMR concentrations similar to the WT. The well-converged structure of this mutant has a core scaffold composed of a layer of two α-helices and a layer of three-stranded antiparallel β-sheet with flexible N and C termini. The structure of CsgE fits well into the cryoelectron microscopy density map of the CsgG-CsgE complex. We highlight a striking feature of the electrostatic potential surface in CsgE structure and present an assembly model of the CsgG-CsgE complex. We suggest a structural mechanism of the interaction between CsgE and CsgA. Understanding curli formation can provide the information necessary to develop treatments and therapeutic agents for biofilm-related infections and may benefit the prevention and treatment of amyloid diseases. CsgE could establish a paradigm for the regulation of amyloidogenesis because of its unique role in curli formation.biofilm formation | intrinsically disordered protein | aggregation | protein-protein interaction | CsgG

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“…Curli can bind a variety of host proteins, can mediate host cell adhesion and invasion, and are involved in colonization and biofilm formation (7)(8)(9)(10)(11). Bacterial biofilms constitute a protected mode of growth against environmental stresses and immune defense, causing high tolerance for antimicrobials, which results in persistent infections (12)(13)(14)(15)(16).…”

mentioning

confidence: 99%

The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism

Crick

Pinkner

Ford

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Curli are extracellular proteinaceous functional amyloid aggregates produced by Escherichia coli , Salmonella spp., and other enteric bacteria. Curli mediate host cell adhesion and invasion and play a critical role in biofilm formation. Curli filaments consist of CsgA, the major subunit, and CsgB, the minor subunit. In vitro, purified CsgA and CsgB exhibit intrinsically disordered properties, and both are capable of forming amyloid fibers similar in morphology to those formed in vivo. However, in vivo, CsgA alone cannot form curli fibers, and CsgB is required for filament growth. Thus, we studied the aggregation of CsgA and CsgB both alone and together in vitro to investigate the different roles of CsgA and CsgB in curli formation. We found that though CsgA and CsgB individually are able to self-associate to form aggregates/fibrils, they do so using different mechanisms and with different kinetic behavior. CsgB rapidly forms structured oligomers, whereas CsgA aggregation is slower and appears to proceed through large amorphous aggregates before forming filaments. Substoichiometric concentrations of CsgB induce a change in the mechanism of CsgA aggregation from that of forming amorphous aggregates to that of structured intermediates similar to those of CsgB alone. Oligomeric CsgB accelerated the aggregation of CsgA, in contrast to monomeric CsgB, which had no effect. The structured β-strand oligomers formed by CsgB serve as nucleators for CsgA aggregation. These results provide insights into the formation of curli in vivo, especially the nucleator function of CsgB.

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Microbial Biofilms: Their Development and Significance for Medical Device—Related Infections

Cited by 244 publications

References 95 publications

Surface-immobilised antimicrobial peptoids

Surface-immobilised antimicrobial peptoids

Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation

The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism

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