Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells

Kreft, Burkhard; Marre, R.; Schramm, Uda; Wirth, Reinhard

doi:10.1128/iai.60.1.25-30.1992

Cited by 234 publications

(104 citation statements)

References 23 publications

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“…Computer analyses indicated a possible binding to eukaryotic cells via the two amino acid motifs RGDS and RGDV. Indeed, we could demonstrate binding of E. faecalis to the in vitro cultured pig kidney tubulus cell line LCC-PK, (Kreft et al, 1992). The idea that binding to eukaryotic cells would be mediated via integrins is supported by our observation that addition of the peptide RGDS reduced the binding of E. faecalis by about 34% (Kreft et al, 1992).…”

Section: Identification Of Functional Domainsmentioning

confidence: 60%

“…Indeed, we could demonstrate binding of E. faecalis to the in vitro cultured pig kidney tubulus cell line LCC-PK, (Kreft et al, 1992). The idea that binding to eukaryotic cells would be mediated via integrins is supported by our observation that addition of the peptide RGDS reduced the binding of E. faecalis by about 34% (Kreft et al, 1992). In other cases in which binding to eukarytic cells is mediated via RGDS receptors which belong to the integrin class of surface proteins such binding was reduced from 10% to more than 90% by adding the peptide.…”

Section: Identification Of Functional Domainsmentioning

confidence: 92%

“…During our binding studies of E. faecalis to the in vitro cultured pig kidney tubulus cell line, we realized that the adhesin was induced during the binding assay. It was found that the inducing principle is present in the fetal calf serum used for growth of the eukaryotic cells (Kreft et al, 1992). This substance(s) very clearly is not sex-pheromone-related in that it is heat-sensitive (sex pheromone containing culture superantant of E. faecalis normally is autoclaved for 'stabilization') and possesses an apparent molecular mass greater than 10 kDa.…”

Section: Induction By Serummentioning

confidence: 99%

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The sex pheromone system of Enterococcus faecalis

Wirth¹

1994

European Journal of Biochemistry

120

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The sex pheromone system of Enterococcus faecalis was discovered by observing a clumping reaction of E. faecalis strains during conjugative transfer of plasmids. It was found that only a special type of E. faecalis plasmids, the so-called sex pheromone plasmids, are transferred via this mechanism. Various experiments, especially by the group of D. B. Clewell, led to the formulation of a model describing how the sex pheromone system works. Small linear peptides, the so-called sex pheromones, are excreted by strains not possessing the corresponding sex pheromone plasmid. Donor strains harboring the plasmid do not produce the corresponding sex pheromone; they react to the presence of the peptide by production of a plasmid-encoded adhesin, the so-called aggregation substance. This adhesin allows contact between the non-motile mating partners ; after conjugative transfer of the plasmid, the former recipient possesses and replicates the new plasmid. Thereby the population of E. faecalis strains is shifted to a high percentage of donor strains. This is especially true because a donor strain will still excrete sex pheromones corresponding to plasmids it does not harbor; therefore, such a strain can also function as recipient for other sex pheromone plasmids it does not possess.Various aspects of this unique plasmid collection mechanism have been studied during the last few years. The data indicate that, with the exception of pAM373, all sex pheromone plasmids possess one DNA region which is highly similar to and codes for the adhesin. It is also becoming more and more clear that regulatory functions/proteins are not conserved between different sex pheromone plasmids. Induction of adhesin synthesis needs the action of a regulatory cascade composed of unique features; at the moment we are just beginning to understand this cascade. By sequencing the first structural gene for one of those adhesins, we realized that the aggregation substance might act also as an adhesin for eucaryotic cells, probably by interaction with integrins. At least in the case of the in vitro cultured pig kidney tubulus cell line LLC-PK, this idea could be verified. An interesting aspect of the sex pheromone system of E. faecalis is its evolution. I will discuss the idea that two different components, both of which well might contribute to virulence of the opportunistic pathogenic bacterium, were combined in the species E. faecalis to result in this unique plasmid collection system.Enterococcus faecalis belongs to the bacterial genus Enterococcus which at the moment contains more than 15 valid species. The genus was established in 1984 when 'Streptococcus faecalis' and 'Streptococcus faecium' were transferred from the taxionomically unclearly defined group 'Streptococcus' in the new genus (Schleifer and Kilpper-Balz, 1984). Because of this some of the older literature cited in Abbreviations. ASA1, ASA373, ASCIO and ASPl, aggregation substance encoded by sex pheromone plasmids pAD1, pAM373, pCFlO and pPD1, respectively; ORFX, gene product of ogx (or€ ...

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Section: Identification Of Functional Domainsmentioning

confidence: 60%

Section: Identification Of Functional Domainsmentioning

confidence: 92%

Section: Induction By Serummentioning

confidence: 99%

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The sex pheromone system of Enterococcus faecalis

Wirth¹

1994

European Journal of Biochemistry

120

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“…Besides its role in conjugation, AS has also that of a virulence factor in E. faecalis. Asa1 increased adherence to renal tubular cells [9] and adherence to and survival in human macrophages [10]. Asc10 increased internalization [11] and intracellular survival [12] in polymorphonuclear leukocytes (PMNs).…”

Section: Aggregation Substancementioning

confidence: 99%

Pathogenesis and immunity in enterococcal infections

Sava

Heikens

Hüebner

2010

Clinical Microbiology and Infection

224

152

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Enterococcus faecalis and Enterococcus faecium have emerged as multi-resistant nosocomial pathogens in immunocompromised and critically ill patients. Multi-resistant strains have acquired virulence genes resulting in hospital-adapted clones. The following review summarizes several proteins and carbohydrate- or glycoconjugates that have been identified as putative virulence factors involved in the pathogenesis of enterococcal infections and may be used as targets for alternative therapies. Several studies describing the host immune response against enterococci are also summarized.

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“…Based on the requirement of a quorum for induction of cytolysin expression, and the observed synergy with aggregation substance in the endocarditis model (Chow et al, 1993) [and possibly also as may be inferred from its co-localization with the biofilm-promoting surface adhesin, Esp (Shankar et al, 2002)], a model for the virulent behaviour of enterococci can be formulated as follows. Aggregation substance is known to be induced by factors in serum (Kreft et al, 1992), and its expression is known to induce clumping of E. faecalis aggregates. Alternatively, or in addition, Esp has been shown to promote biofilm formation on abiotic surfaces (Toledo-Arana et al, 2001).…”

Section: Model For the Mechanism Of Cytolysin In Enterococcal Pathogementioning

confidence: 99%

The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells

Coburn¹,

Gilmore²

2003

Cell Microbiol

164

123

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SummaryThe enterococcal cytolysin, a two-peptide lytic system, is a divergent relative of a large family of toxins and bacteriocins secreted by pathogenic and nonpathogenic Gram-positive bacteria. This family includes the lantibiotics and streptolysin S. The enterococcal cytolysin is of interest because its activities enhance enterococcal virulence in infection models and, in epidemiological studies, it has been associated with patient mortality. The cytolysin is lethal for a broad range of prokaryotic and eukaryotic cells, and this activity requires two non-identical, post-translationally modified peptides. The smaller of the two peptides also plays a role in a quorumsensing autoinduction of the cytolysin operon. As a trait that is present in particularly virulent strains of Enterococcus faecalis , including strains that are resistant to multiple antibiotics, it serves as a model for testing the value of developing new virulencetargeting therapeutics. Further, because of the interest in small membrane active peptides as therapeutics themselves, studies of the molecular structure/ activity relationships for the cytolysin peptides are providing insights into the physical basis for prokaryotic versus eukaryotic cell targeting.

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Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells

Cited by 234 publications

References 23 publications

The sex pheromone system of Enterococcus faecalis

The sex pheromone system of Enterococcus faecalis

Pathogenesis and immunity in enterococcal infections

The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells

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