Inducible Expression of Enterococcus Faecalis Aggregation Substance Surface Protein Facilitates Bacterial Internalization by Cultured Enterocytes

Overview

Journal Infect Immun

Publisher American Society for Microbiology

Specialty Allergy & Immunology

Date 2000 Nov 18

PMID 11083854

Citations 20

Authors

C L Wells

E A Moore

J A Hoag

H Hirt

G M Dunny

S L Erlandsen

Affiliations

Soon will be listed here.

Abstract

Aggregation substance (AS) is an Enterococcus faecalis surface protein that may contribute to virulence. Using a recently described system for controlled expression of AS in E. faecalis and the heterologous host Lactococcus lactis, experiments were designed to assess the effect of AS on bacterial internalization by HT-29 and Caco-2 enterocytes. AS expression was associated with increased internalization of E. faecalis by HT-29 enterocytes and of L. lactis by HT-29 and Caco-2 enterocytes. Compared to enterocytes cultivated under standard conditions, either cultivation in hypoxia or 1-h pretreatment of enterocytes with calcium-free medium resulted in increased internalization of both E. faecalis and L. lactis (with and without AS expression). Also, AS expression augmented these increases when E. faecalis was incubated with pretreated HT-29 enterocytes and when L. lactis was incubated with pretreated Caco-2 and HT-29 enterocytes. These data indicated that AS might facilitate E. faecalis internalization by cultured enterocytes.

Citing Articles

Enterococcal-host interactions in the gastrointestinal tract and beyond.

Madani W, Ramos Y, Cubillos-Ruiz J, Morales D FEMS Microbes. 2024; 5:xtae027.

PMID: 39391373 PMC: 11466040. DOI: 10.1093/femsmc/xtae027.

: an overlooked cell invader.

Archambaud C, Nunez N, da Silva R, Kline K, Serror P Microbiol Mol Biol Rev. 2024; 88(3):e0006924.

PMID: 39239986 PMC: 11426025. DOI: 10.1128/mmbr.00069-24.

Virulence and Resistant Traits Associated with Its Permanence in the Hospital Environment.

Geraldes C, Tavares L, Gil S, Oliveira M Antibiotics (Basel). 2022; 11(7).

PMID: 35884110 PMC: 9311936. DOI: 10.3390/antibiotics11070857.

Let Me Upgrade You: Impact of Mobile Genetic Elements on Enterococcal Adaptation and Evolution.

Johnson C, Sheriff E, Duerkop B, Chatterjee A J Bacteriol. 2021; 203(21):e0017721.

PMID: 34370561 PMC: 8508098. DOI: 10.1128/JB.00177-21.

Artificial Sweeteners Negatively Regulate Pathogenic Characteristics of Two Model Gut Bacteria, and .

Shil A, Chichger H Int J Mol Sci. 2021; 22(10).

PMID: 34063332 PMC: 8156656. DOI: 10.3390/ijms22105228.

References

Rakita R, Vanek N, Mee M, Mariscalco M, Dunny G, Snuggs M . Enterococcus faecalis bearing aggregation substance is resistant to killing by human neutrophils despite phagocytosis and neutrophil activation. Infect Immun. 1999; 67(11):6067-75. PMC: 96994. DOI: 10.1128/IAI.67.11.6067-6075.1999. View

Vanek N, Simon S, Mariscalco M, Dunny G, Rakita R . Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism. FEMS Immunol Med Microbiol. 1999; 26(1):49-60. DOI: 10.1111/j.1574-695X.1999.tb01371.x. View

Hirt H, Erlandsen S, Dunny G . Heterologous inducible expression of Enterococcus faecalis pCF10 aggregation substance asc10 in Lactococcus lactis and Streptococcus gordonii contributes to cell hydrophobicity and adhesion to fibrin. J Bacteriol. 2000; 182(8):2299-306. PMC: 111281. DOI: 10.1128/JB.182.8.2299-2306.2000. View

Huet C, Coudrier E, Louvard D . Absorptive and mucus-secreting subclones isolated from a multipotent intestinal cell line (HT-29) provide new models for cell polarity and terminal differentiation. J Cell Biol. 1987; 105(1):345-57. PMC: 2114933. DOI: 10.1083/jcb.105.1.345. View

Kreft B, Marre R, Schramm U, Wirth R . Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells. Infect Immun. 1992; 60(1):25-30. PMC: 257498. DOI: 10.1128/iai.60.1.25-30.1992. View

Bhat M, Wang L, Malanga C, Ma J, Rojanasakul Y . Regulation of tight junction permeability by calcium mediators and cell cytoskeleton in rabbit tracheal epithelium. Pharm Res. 1993; 10(7):991-7. DOI: 10.1023/a:1018906504944. View

Chow J, Thal L, Perri M, Vazquez J, Donabedian S, Clewell D . Plasmid-associated hemolysin and aggregation substance production contribute to virulence in experimental enterococcal endocarditis. Antimicrob Agents Chemother. 1993; 37(11):2474-7. PMC: 192412. DOI: 10.1128/AAC.37.11.2474. View

Armitage W, Juss B, Easty D . Response of epithelial (MDCK) cell junctions to calcium removal and osmotic stress is influenced by temperature. Cryobiology. 1994; 31(5):453-60. DOI: 10.1006/cryo.1994.1055. View

Olmsted S, Dunny G, Erlandsen S, Wells C . A plasmid-encoded surface protein on Enterococcus faecalis augments its internalization by cultured intestinal epithelial cells. J Infect Dis. 1994; 170(6):1549-56. DOI: 10.1093/infdis/170.6.1549. View

10.

Dunny G, Leonard B, Hedberg P . Pheromone-inducible conjugation in Enterococcus faecalis: interbacterial and host-parasite chemical communication. J Bacteriol. 1995; 177(4):871-6. PMC: 176677. DOI: 10.1128/jb.177.4.871-876.1995. View

11.

Coque T, Patterson J, Steckelberg J, Murray B . Incidence of hemolysin, gelatinase, and aggregation substance among enterococci isolated from patients with endocarditis and other infections and from feces of hospitalized and community-based persons. J Infect Dis. 1995; 171(5):1223-9. DOI: 10.1093/infdis/171.5.1223. View

12.

Wells C, van de Westerlo E, Jechorek R, Erlandsen S . Exposure of the lateral enterocyte membrane by dissociation of calcium-dependent junctional complex augments endocytosis of enteric bacteria. Shock. 1995; 4(3):204-10. DOI: 10.1097/00024382-199509000-00009. View

13.

Huycke M, Gilmore M . Frequency of aggregation substance and cytolysin genes among enterococcal endocarditis isolates. Plasmid. 1995; 34(2):152-6. DOI: 10.1006/plas.1995.9992. View

14.

Wells C, van de Westerlo E, Jechorek R, Feltis B, Wilkins T, Erlandsen S . Bacteroides fragilis enterotoxin modulates epithelial permeability and bacterial internalization by HT-29 enterocytes. Gastroenterology. 1996; 110(5):1429-37. DOI: 10.1053/gast.1996.v110.pm8613048. View

15.

Wells C, VandeWesterlo E, Jechorek R, Erlandsen S . Effect of hypoxia on enterocyte endocytosis of enteric bacteria. Crit Care Med. 1996; 24(6):985-91. DOI: 10.1097/00003246-199606000-00019. View

16.

Schlievert P, Gahr P, Assimacopoulos A, Dinges M, Stoehr J, Harmala J . Aggregation and binding substances enhance pathogenicity in rabbit models of Enterococcus faecalis endocarditis. Infect Immun. 1998; 66(1):218-23. PMC: 107880. DOI: 10.1128/IAI.66.1.218-223.1998. View

17.

Jett B, Atkuri R, Gilmore M . Enterococcus faecalis localization in experimental endophthalmitis: role of plasmid-encoded aggregation substance. Infect Immun. 1998; 66(2):843-8. PMC: 107981. DOI: 10.1128/IAI.66.2.843-848.1998. View

18.

Berti M, Candiani G, Kaufhold A, Muscholl A, Wirth R . Does aggregation substance of Enterococcus faecalis contribute to development of endocarditis?. Infection. 1998; 26(1):48-53. DOI: 10.1007/BF02768756. View

19.

Wells C, van de Westerlo E, Jechorek R, Haines H, Erlandsen S . Cytochalasin-induced actin disruption of polarized enterocytes can augment internalization of bacteria. Infect Immun. 1998; 66(6):2410-9. PMC: 108218. DOI: 10.1128/IAI.66.6.2410-2419.1998. View

20.

Dupont H, Montravers P, Mohler J, Carbon C . Disparate findings on the role of virulence factors of Enterococcus faecalis in mouse and rat models of peritonitis. Infect Immun. 1998; 66(6):2570-5. PMC: 108240. DOI: 10.1128/IAI.66.6.2570-2575.1998. View