Iron availability affects entry of Listeria monocytogenes into the enterocytelike cell line Caco-2

Infection and Immunity

Volumn 64, Issue 9, 1996, Pages 3925-3929

  Conte, Maria Pia ^a   Longhi, Catia ^a   Polidoro, Mario ^a   Petrone, Gloria ^a   Buonfiglio, Vincenzo ^a   Santo, Stefano D I ^a   Papi, Elsie ^a   Seganti, Lucilla ^a   Visca, Paolo ^a   Valenti, Piera ^b  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

IRON;

ARTICLE; BACTERIAL VIRULENCE; CONTROLLED STUDY; HUMAN; HUMAN CELL; HYDROPHOBICITY; IRON METABOLISM; IRON TRANSPORT; LISTERIA MONOCYTOGENES; NONHUMAN; PRIORITY JOURNAL;

EID: 9544250393     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.64.9.3925-3929.1996     Document Type: Article

References (38)

1. Adams, T. J., S. Vartivarian, and R. E. Cowart. 1990. Iron acquisition systems of Listeria monocytogenes. Infect. Immun. 58:2715-2718.
2. Bothwell, T. H., R. W. Charlton, J. D. Cook, and C. A. Finch (ed.), 1979. Iron metabolism in man, p. 255-283. Blackwell Scientific Publications, Oxford.
3. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
4. Conlan, J. W., and R. J. North. 1992. Early pathogenesis of infection in the liver with the facultative intracellular bacteria Listeria monocytogenes, Francisella tularensis, and Salmonella typhimurium involves lysis of infected hepatocytes by leukocytes. Infect. Immun. 60:5164-5171.
5. Conte, M. P., C. Longhi, V. Buonfiglio, M. Polidoro, L. Seganti, and P. Valenti. 1994. The effect of iron on the invasiveness of Escherichia coli carrying the inv gene of Yersinia pseudotuberculosis. J. Med. Microbiol. 40: 236-240.
6. Conte, M. P., C. Longhi, G. Petrone, M. Polidoro, P. Valenti, and L. Seganti. 1994. L. monocytogenes infection of Caco-2 cells: role of growth temperature. Res. Microbiol. 145:677-682.
7. Cossart, P., M. F. Vicente, J. Mengaud, F. Baquero, J. C. Perez-Diaz, and P. Berche. 1989. Listeriolysin O is essential for virulence of Listeria monocytogenes: direct evidence obtained by gene complementation. Infect. Immun. 57:3629-3636.
8. Cowart, R. E., and B. G. Foster. 1981. The role of iron in the production of haemolysin by L. monocytogenes. Curr. Microbiol. 6:287-290.
9. Cowart, R. E., and B. G. Foster. 1985. Differential effects of iron on the growth of L. monocytogenes: minimum requirements and mechanism of acquisition. J. Infect. Dis. 151:721-730.
10. Deneer, H. G., V. Healey, and I. Boyschulz. 1995. Reduction of exogenous ferric ion by a surface-associated ferric reductase of Listeria spp. Microbiology 141:1985-1992.
11. Domann, E., J. Wehland, K. Niebuhr, C. Haffner, M. Leimeister-Wächter, and T. Chakraborty. 1993. Detection of a pfrA-independent promoter responsible for listeriolysin gene expression in mutant Listeria monocytogenes strains lacking the PrfA regulator. Infect. Immun. 61:3073-3075.
12. Dominguez Rodriguez, L., J. A. Vazquez Boland, J. F. Fernandez Garayzabal, P. Echalecu Tranchant, E. Gomez-Lucia, E. F. Rodriguez Ferri, and G. Suarez Fernandez. 1986. Microplate technique to determine hemolytic activity for routine typing of Listeria strains. J. Clin. Microbiol. 24:99-103.
13. Dramsi, S., C. Kocks, C. Forestier, and P. Cossart. 1993. Internalin-mediated invasion of epithelial cells by Listeria monocytogenes is regulated by the bacterial growth state, temperature and the pleiotropic activator prfA. Mol. Microbiol. 9:931-941.
14. Finkelstein, R. A., C. V. Sciortino, and M. A. McIntosh. 1983. Role of iron in microbe-host interactions. Rev. Infect. Dis. 5:5759-5777.
15. Freitag, N. E., and D. A. Portnoy. 1994. Dual promoters of the Listeria monocytogenes prfA transnational activator appear essential in vitro but are redundant in vivo. Mol. Microbiol. 12:845-853.
16. Gaillard, J. L., P. Berche, C. Frehel, E. Gouin, and P. Cossart. 1991. Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci. Cell 65:1127-1141.
17. Geoffroy, C., J.-L. Gaillard, J. E. Alouf, and P. Berche. 1987. Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes. Infect. Immun. 55:1641-1646.
18. Griffiths, E. 1989. Iron in biological systems, p. 1-25. In J. J. Bullen and E. Griffiths (ed.), Iron and infection: molecular, physiological and clinical aspects. John Wiley & Sons, New York.
19. Hartford, T., S. O'Brien, P. W. Andrew, D. Jones, and I. S. Roberts. 1993. Utilization of transferrin-bound iron by L. monocytogenes. FEMS Microbiol. Lett. 108:311-318.
20. Laemmll, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
21. Leimeister-Wächter, M., E. Domann, and T. Chakraborty. 1992. The expression of virulence genes in Listeria monocytogenes is thermoregulated. J. Bacteriol. 174:947-952.
22. Litwin, C. M., and S. B. Calderwood. 1993. Role of iron in regulation of virulence genes. Clin. Microbiol. Rev. 6:137-149.
23. Mengaud, J., J. Chenevert, C. Geoffroy, J.-L. Gaillard, and P. Cossart. 1987. Identification of the structural gene encoding the SH-activated hemolysin of Listeria monocytogenes: listeriolysin O is homologous to streptolysin O and pneumolysin. Infect. Immun. 55:3225-3227.
24. Mounier, J., A. Ryter, M. Coquis-Rondon, and P. J. Sansonetti. 1990. Intracellular and cell-to-cell spread of Listeria monocytogenes involves interaction with F-actin in the enterocytelike cell line Caco-2. Infect. Immun. 58:1048-1058.
25. Neilands, J. B. 1981. Iron absorption and transport in microorganisms. Annu. Rev. Nutr. 1:27-46.
26. Neilands, J. B. 1982. Microbial envelope proteins related to iron. Annu. Rev. Microbiol. 36:285-309.
27. Portnoy, D. A. 1994. Cellular biology of Listeria monocytogenes infection, p. 279-293. In V. L. Miller, J. B. Kaper, D. A. Portnoy, and R. R. Isberg (ed.), Molecular genetics of bacterial pathogenesis. American Society for Microbiology, Washington, D.C.
28. Portnoy, D. A., T. Chakraborty, W. Goebel, and P. Cossart. 1992. Molecular determinants of Listeria monocytogenes pathogenesis. Infect. Immun. 60: 1263-1267.
29. Racz, P., K. Tenner, and E. Mero. 1972. Experimental Listeria enteritis. I. An electron microscopic study of the epithelial phase in experimental listeria infection. Lab. Invest. 26:694-700.
30. Racz, P., K. Tenner, and K. Szivessy. 1970. Electron microscopic studies in experimental keratoconjunctivitis listeriosa. Acta Microbiol. Acad. Sci. Hung. 17:221-236.
31. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
32. Sokolovic, Z., J. Riedel, M. Wuenscher, and W. Goebel. 1993. Surface-associated, PrfA-regulated proteins of Listeria monocytogenes synthesized under stress conditions. Mol. Microbiol. 8:219-227.
33. Sword, C. P. 1966. Mechanisms of pathogenesis in Listeria monocytogenes infection. I. Influence of iron. J. Bacteriol. 92:536-542.
34. Tabouret, M., J. De Ryche, and G. Dubray. 1992. Analysis of surface proteins of Listeria in relation to species, serovar and pathogenicity. J. Gen. Microbiol. 138:743-753.
35. Tao, X., N. Schiering, H. Zeng, D. Ringe, and J. R. Murphy. 1994. Iron, DtxR, and the regulation of diphtheria toxin expression. Mol. Microbiol. 14:191-197.
36. Tylewska, S. K., S. Hjertén, and T. Wadström. 1979. Contribution of M protein to hydrophobic surface properties of Streptococcus pyogenes. FEMS Microbiol. Lett. 6:249-253.
37. Valenti, P., P. Visca, G. Antonini, and N. Orsi. 1986. Interaction between lactoferrin and ovotransferrin and Candida cells. FEMS Microbiol. Lett. 33:271-275.
38. Weinberg, E. D. 1984. Iron withholding: a defence against infection and neoplasia. Physiol. Rev. 64:65-102.