Binding, inactivation, and adhesion forces between antimicrobial peptide cecropin P1 and pathogenic E. coli

Strauss, J; Kadilak, Andrea L.; Cronin, Christine; Mello, Charlene M.; Camesano, Terri A.

doi:10.1016/j.colsurfb.2009.08.026

Cited by 66 publications

(73 citation statements)

References 74 publications

(83 reference statements)

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“…Developments in this area were summarized in recent reviews by Costa et al [11] and Onaizi [6]. While previous studies reporting antimicrobial activity of immobilized peptides have tried to elucidate the complex relationship between these factors [12][13][14][15][16][17][18][19], both reviews have highlighted the need for these factors to be studied independently. Currently no systematic study has been carried out to investigate the effects of different peptide conformations on the subsequent activity.…”

Section: Introductionmentioning

confidence: 96%

Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity

et al. 2012

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Section: Introductionmentioning

confidence: 96%

Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity

et al. 2012

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“…The O antigen protrudes into the environment and allows the bacterium to interact with its surroundings. There are 20 serotypes of P. aeruginosa (27), and 14 of those groups also produce the Aband saccharide known as common antigen, which is composed of D-rhamnose sugar polymer and consists of about 23 repeating units (6,47).LPS physical properties such as three-dimensional structure and number of repeating units contribute to bacterial adhesion (3,37,40). P. aeruginosa uses complicated biosynthetic mechanisms for assembly of LPS O antigen; this has been described extensively elsewhere (24).…”

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confidence: 99%

“…LPS physical properties such as three-dimensional structure and number of repeating units contribute to bacterial adhesion (3,37,40). P. aeruginosa uses complicated biosynthetic mechanisms for assembly of LPS O antigen; this has been described extensively elsewhere (24).…”

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confidence: 99%

Relating the Physical Properties of Pseudomonas aeruginosa Lipopolysaccharides to Virulence by Atomic Force Microscopy

et al. 2011

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Lipopolysaccharides (LPS) are an important class of macromolecules that are components of the outer membrane of Gram-negative bacteria such as Pseudomonas aeruginosa. P. aeruginosa contains two different sugar chains, the homopolymer common antigen (A band) and the heteropolymer O antigen (B band), which impart serospecificity. The characteristics of LPS are generally assessed after isolation rather than in the context of whole bacteria. Here we used atomic force microscopy (AFM) to probe the physical properties of the LPS of P. aeruginosa strain PA103 (serogroup O11) in situ. This strain contains a mixture of long and very long polymers of O antigen, regulated by two different genes. For this analysis, we studied the wild-type strain and four mutants, ⌬Wzz1 (producing only very long LPS), ⌬Wzz2 (producing only long LPS), D⌬M (with both the wzz1 and wzz2 genes deleted), and Wzy::GM (producing an LPS core oligosaccharide plus one unit of O antigen). Forces of adhesion between the LPS on these strains and the silicon nitride AFM tip were measured, and the Alexander and de Gennes model of steric repulsion between a flat surface and a polymer brush was used to calculate the LPS layer thickness (which we refer to as length), compressibility, and spacing between the individual molecules. LPS chains were longest for the wild-type strain and ⌬Wzz1, at 170.6 and 212.4 nm, respectively, and these values were not statistically significantly different from one another. Wzy::GM and D⌬M have reduced LPS lengths, at 34.6 and 37.7 nm, respectively. Adhesion forces were not correlated with LPS length, but a relationship between adhesion force and bacterial pathogenicity was found in a mouse acute pneumonia model of infection. The adhesion forces with the AFM probe were lower for strains with LPS mutations, suggesting that the wild-type strain is optimized for maximal adhesion. Our research contributes to further understanding of the role of LPS in the adhesion and virulence of P. aeruginosa.Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen that can cause several different types of infections in both community and health care settings and is especially problematic for immunocompromised and cystic fibrosis patients, as well as burn victims (23,32). Surface structures on the bacterium are related to virulence and the ability to cause infections. They make it possible for P. aeruginosa to attach to a wide range of surfaces, as well as to interact with components of the host (20). The lipopolysaccharide (LPS) is an important virulence factor for P. aeruginosa (25). The structure of LPS consists of lipid A, which anchors the LPS to the outer membrane, the core oligosaccharide, and the highly variable Oantigen side chain, which consists of repeating saccharide units and confers serotype specificity to the bacterium. The O antigen protrudes into the environment and allows the bacterium to interact with its surroundings. There are 20 serotypes of P. aeruginosa (27), and 14 of those groups also produce the Aband saccharide ...

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“…While this interaction was extensively investigated and believed to lead to a host of cytotoxic mechanisms, AMPs were also suggested to be useful as recognition molecules for bacterial detection, both in vitro and in vivo, using radioactive or fluorescent labels (6,24). Recent approaches have further attempted to exploit AMPs as capture molecules (25,26), enabling multitarget detection, as opposed to target-specific detection in antibody-based assays (7). Another approach proposed the use of simple but robust synthetic constructs that mimic the structure and activity of AMPs for efficient bacterial capture in aqueous samples (27).…”

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confidence: 99%

Improved Bacterial Detection Using Immobilized Acyl-Lysyl Oligomers

Marjieh

Meir

Zaknoon

et al. 2015

Appl Environ Microbiol

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The global need to improve bacterial detection in liquid media has motivated multidisciplinary research efforts toward developing new approaches that overcome the shortcomings of traditional techniques. We recently proposed the use of oligomers of acylated lysyls (OAKs) in their resin-linked form (ROAKs) for the efficient, robust, and inexpensive filtration of bacteria. Here, to investigate the potential for the use of ROAKs in downstream applications, we first examined the capacity of ROAKs to capture bacteria as a function of environmental conditions and structure-activity relationships (SARs). We next assessed their ability to release the captured bacteria and then combined both abilities to improve real-time PCR outcomes. ROAKs were able to deplete liquid samples of bacterial content after incubation or continuous flow, illustrating the efficient capture of different bacterial species under a wide range of ionic strength and pH conditions. We also show circumstances for the significant release of captured bacteria, live or dead, for further analysis. Finally, the SAR study revealed a shorter ROAK derivative exhibiting a capture capacity similar to that of the parent construct but the increased recovery of ROAK-bound bacteria, enabling improvement of the detection sensitivity by 20-fold. Collectively, the data support the potential usefulness of a simple, robust, and efficient approach for rapid capture/analysis of bacteria from tap water and, possibly, from more complex media.

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Binding, inactivation, and adhesion forces between antimicrobial peptide cecropin P1 and pathogenic E. coli

Cited by 66 publications

References 74 publications

Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity

Characterization of chemoselective surface attachment of the cationic peptide melimine and its effects on antimicrobial activity

Relating the Physical Properties of Pseudomonas aeruginosa Lipopolysaccharides to Virulence by Atomic Force Microscopy

Improved Bacterial Detection Using Immobilized Acyl-Lysyl Oligomers

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