Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity

Farnaud, Sébastien; Spiller, Claire E.; Moriarty, Laura C.; Patel, Alpesh; Gant, Vanya; Odell, Edward; Evans, Robert W.

doi:10.1111/j.1574-6968.2004.tb09482.x

Cited by 84 publications

(51 citation statements)

References 30 publications

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“…Based upon these observations, it can be concluded that hydrophobic peptide-LPS interaction is essential for an efficient transport across the bacterial outer membrane, but that LA does not act as a specific activity modulating binding site of the hexapeptides. This is in accordance with observations with lactoferricin peptides suggesting that the tight fatty acid packing in LA is not the primary site of interaction [130]. …”

Section: Influence Of Lipid Composition Upon Bindingsupporting

confidence: 80%

Cationic Antimicrobial Peptides

Phoenix

Dennison

Harris

2013

Antimicrobial Peptides

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Section: Influence Of Lipid Composition Upon Bindingsupporting

confidence: 80%

Cationic Antimicrobial Peptides

Phoenix

Dennison

Harris

2013

Antimicrobial Peptides

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“…The OPSs provide a steric hindrance for the access of antimicrobial peptides to inner LPS targets (9,30,47,67). The serotype O:9 OPS, however, similarly to that of serotype O:3 (67), plays a minor role in the polymyxin B resistance.…”

Section: Discussionmentioning

confidence: 99%

Characterization and Biological Role of the O-Polysaccharide Gene Cluster ofYersinia enterocoliticaSerotype O:9

et al. 2007

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Yersinia enterocolitica serotype O:9 is a gram-negative enteropathogen that infects animals and humans. The role of lipopolysaccharide (LPS) in Y. enterocolitica O:9 pathogenesis, however, remains unclear. The O:9 LPS consists of lipid A to which is linked the inner core oligosaccharide, serving as an attachment site for both the outer core (OC) hexasaccharide and the O-polysaccharide (OPS; a homopolymer of N-formylperosamine). In this work, we cloned the OPS gene cluster of O:9 and identified 12 genes organized into four operons upstream of the gnd gene. Ten genes were predicted to encode glycosyltransferases, the ATP-binding cassette polysaccharide translocators, or enzymes required for the biosynthesis of GDP-N-formylperosamine. The two remaining genes within the OPS gene cluster, galF and galU, were not ascribed a clear function in OPS biosynthesis; however, the latter gene appeared to be essential for O:9. The biological functions of O:9 OPS and OC were studied using isogenic mutants lacking one or both of these LPS parts. We showed that OPS and OC confer resistance to human complement and polymyxin B; the OPS effect on polymyxin B resistance could be observed only in the absence of OC.Yersinia enterocolitica serotypes O:3, O:5,27, O:8, and O:9 include strains that infect both humans and animals (16). Pathogenesis of these strains is associated with the presence of common virulence factors encoded on the chromosome and on pYV, the Yersinia virulence plasmid (73). Despite the genetic and phenotypic similarity, however, the serotypes display epidemiological and host range differences (17,22). Biotyping and serotyping based on the antigenic O-polysaccharide (OPS or O-antigen) are important in studying Y. enterocolitica infections. OPS is a distal part of lipopolysaccharide (LPS), which is the major component of the outer membrane of gram-negative bacteria (55,63). In addition to OPS, LPS comprises lipid A, a hydrophobic membrane anchor, and a core oligosaccharide, divided into a lipid A-proximal inner core and an outer core (OC). The latter typically provides the attachment site for the polymeric OPS (55). Heteropolymeric OPSs, such as that of Y. enterocolitica serotype O:8 (63), are the most frequent among gram-negative bacteria; they are made up of identical oligosaccharide repeat units comprising three to eight different monosaccharides (55). Y. enterocolitica serotypes O:3 and O:9, however, display a homopolymeric OPS composed of singlesugar repeating units of 6-deoxy-L-altrose or N-formylperosamine, respectively (24, 41). Furthermore, the structures of the O:3 and O:9 core oligosaccharides are identical (51, 63). They both have a branching hexasaccharide termed OC which in genetic and biosynthetic terms resembles more closely a nonpolymerized O unit than the classical hexose-containing OC of Escherichia coli or Salmonella species (67, 68). The linkage of both the OC and the homopolymeric OPS to the inner core is a unique feature shared between serotypes O:3 and O:9. The O:9 OPS is identical to that of Bru...

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“…LPS is on the surface of the gram-negative bacteria, making it the first barrier of the bacterial cell wall. It is believed that positively charged cationic peptides can interact with the negatively charged LPS leading to the insertion of the peptides into the membranes (19,25,42). Such cationic peptides are present in egg albumen.…”

Section: Discussionmentioning

confidence: 99%

Identification of Genes Associated with Survival ofSalmonella entericaSerovar Enteritidis in Chicken Egg Albumen

Clavijo

Loui

Andersen

et al. 2006

Appl Environ Microbiol

115

119

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Salmonella enterica consists of over 2,000 serovars that are major causes of morbidity and mortality associated with contaminated food. Despite similarities among serovars of Salmonella enterica, many demonstrate unique host specificities, epidemiological characteristics, and clinical manifestations. One of the unique epidemiological characteristics of the serovar Enteritidis is that it is the only bacterium routinely transmitted to humans through intact chicken eggs. Therefore, Salmonella enterica serovar Enteritidis must be able to persist inside chicken eggs to be transmitted to humans, and its survival in egg is important for its transmission to the human population. The ability of Salmonella enterica serovar Enteritidis to survive in and transmit through eggs may have contributed to its drastically increased prevalence in the 1980s and 1990s. In the present study, using transposon-mediated mutagenesis, we have identified genes important for the association of Salmonella enterica serovar Enteritidis with chicken eggs. Our results indicate that genes involved in cell wall structural and functional integrity, and nucleic acid and amino acid metabolism are important for Salmonella enterica serovar Enteritidis to persist in egg albumen. Two regions unique to Salmonella enterica serovar Enteritidis were also identified, one of which enhanced the survival of a Salmonella enterica serovar Typhimurium isolate in egg albumen. The implication of our results to the serovar specificity of Salmonella enterica is also explored in the present study.

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Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity

Cited by 84 publications

References 30 publications

Cationic Antimicrobial Peptides

Cationic Antimicrobial Peptides

Characterization and Biological Role of the O-Polysaccharide Gene Cluster ofYersinia enterocoliticaSerotype O:9

Identification of Genes Associated with Survival ofSalmonella entericaSerovar Enteritidis in Chicken Egg Albumen

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