Virulence determination

Handbook of Listeria Monocytogenes

Volumn , Issue , 2008, Pages 241-270

  Roche, Sylvie M ^a   Velge, Philippe ^a   Liu, Dongyou ^b  

^a UR1282   (France)

^b MISSISSIPPI STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 78650003936     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (149)

1. Farber, J.M. and Peterkin, P.I., Listeria monocytogenes, a food-borne pathogen, Microbiol. Rev., 55, 476, 1991.
2. Cossart, P. and Lecuit, M., Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement: Bacterial factors, cellular ligands and signaling, EMBO J., 17, 3797, 1998.
3. Vazquez-Boland, J.A. et al., Listeria pathogenesis and molecular virulence determinants, Clin. Microbiol. Rev., 14, 584, 2001.
4. Conner, D.E. et al., Pathogenicity of food-borne, environmental and clinical isolates of Listeria monocytogenes in mice, J. Food Sci., 54, 1553, 1989.
5. Tabouret, M. et al., Pathogenicity of Listeria monocytogenes isolates in immunocompromised mice in relation to listeriolysin production, J. Med. Microbiol., 34, 13, 1991.
6. Van Langendonck, N. et al., Tissue culture assays using Caco-2 cell line differentiate virulent from nonvirulent Listeria monocytogenes strains, J. Appl. Microbiol., 85, 337, 1998.
7. Roche, S.M. et al., Assessment of the virulence of Listeria monocytogenes: Agreement between a plaque-forming assay with HT-29 cells and infection of immunocompetent mice, Int. J. Food Microbiol., 68, 33, 2001.
8. Glaser, P. et al., Comparative genomics of Listeria species, Science, 294, 849, 2001.
9. Nelson, K.E. et al., Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species, Nucleic Acids Res., 32, 2386, 2004.
10. Knudsen, G.M., Olsen, J.E., and Dons, L., Characterization of DegU, a response regulator in Listeria monocytogenes, involved in regulation of motility and contributes to virulence, FEMS Microbiol. Lett., 240, 171, 2004.
11. Williams, T. et al., Response regulator DegU of Listeria monocytogenes regulates the expression of flagella-specific genes, FEMS Microbiol. Lett., 252, 287, 2005.
12. Dubail, I. et al., Identification of an essential gene of Listeria monocytogenes involved in teichoic acid biogenesis, J. Bacteriol., 188, 6580, 2006.
13. Shen, A. and Higgins, D.E., The MogR transcriptional repressor regulates nonhierarchical expression of flagellar motility genes and virulence in Listeria monocytogenes, PLoS Pathog., 2, e30, 2006.
14. Stack, H.M. et al., Role for HtrA in stress induction and virulence potential in Listeria monocytogenes, Appl. Environ. Microbiol., 71, 4241, 2005.
15. Autret, N. et al., Identification of the agr locus of Listeria monocytogenes: Role in bacterial virulence, Infect. Immun., 71, 4463, 2003.
16. Liu, D. et al., Characterization of virulent and avirulent Listeria monocytogenes strains by PCR amplification of putative transcriptional regulator and internalin genes, J. Med. Microbiol., 52, 1065, 2003.
17. Sabet, C. et al., LPXTG protein InlJ, a newly identified internalin involved in Listeria monocytogenes virulence, Infect. Immun., 73, 6912, 2005.
18. Liu, D. et al., Listeria monocytogenes serotype 4b strains belonging to lineages I and III possess distinct molecular features, J. Clin. Microbiol., 44, 214, 2006.
19. Kreft, J. and Vazquez-Boland, J.A., Regulation of virulence genes in Listeria, Int. J. Med. Microbiol., 291, 145, 2001.
20. Wiedmann, M. et al., General stress transcription factor sigma(B) and its role in acid tolerance and virulence of Listeria monocytogenes, J. Bacteriol., 180, 3650, 1998.
21. Kallipolitis, B.H. et al., CesRK, a two-component signal transduction system in Listeria monocytogenes, responds to the presence of cell wall-acting antibiotics and affects beta-lactam resistance, Antimicrob. Agents Chemother., 47, 3421, 2003.
22. Mandin, P. et al., VirR, a response regulator critical for Listeria monocytogenes virulence, Mol. Microbiol., 57, 1367, 2005.
23. Flanary, P.L. et al., Insertional inactivation of the Listeria monocytogenes cheYA operon abolishes response to oxygen gradients and reduces the number of flagella, Can. J. Microbiol., 45, 646, 1999.
24. Dons, L. et al., Role of flagellin and the two-component CheA/CheY system of Listeria monocytogenes in host cell invasion and virulence, Infect. Immunol., 72, 3237, 2004.
25. Archambaud, C. et al., Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes, Mol. Microbiol., 56, 383, 2005.
26. Dramsi, S. et al., FbpA, a novel multifunctional Listeria monocytogenes virulence factor, Mol. Microbiol., 53, 639, 2004.
27. Milohanic, E. et al., The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor, Mol. Microbiol., 39, 1212, 2001.
28. Gaillard, J.L. et al., Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from Gram-positive cocci, Cell, 65, 1127, 1991.
29. Bergmann, B. et al., InlA- but not InlB-mediated internalization of Listeria monocytogenes by nonphagocytic mammalian cells needs the support of other internalins, Mol. Microbiol., 43, 557, 2002.
30. Garandeau, C. et al., The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence, Infect. Immun., 70, 1382, 2002.
31. Bierne, H. et al., Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence, Mol. Microbiol., 43, 869, 2002.
32. Dramsi, S. et al., Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family, Mol. Microbiol., 16, 251, 1995.
33. Bierne, H. and Cossart, P., InlB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor, J. Cell Sci., 115, 3357, 2002.
34. Engelbrecht, F. et al., A new prfa-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins, Mol. Microbiol., 21, 823, 1996.
35. Lingnau, A. et al., Identification and purification of novel internalin-related proteins in Listeria monocytogenes and Listeria ivanovii, Infect. Immun., 64, 1002, 1996.
36. Dramsi, S. et al., Identification of four new members of the internalin multigene family of Listeria monocytogenes EGD, Infect. Immun., 65, 1615, 1997.
37. Raffelsbauer, D. et al., The gene cluster inlC2DE of Listeria monocytogenes contains additional new internalin genes and is important for virulence in mice, Mol. Gen. Genet., 260, 144, 1998.
38. Kuhn, M. and Goebel, W., Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells, Infect. Immun., 57, 55, 1989.
39. Reglier-Poupet, H. et al., Identification of LpeA, a PsaA-like membrane protein that promotes cell entry by Listeria monocytogenes, Infect. Immun., 71, 474, 2003.
40. Cabanes, D. et al., Auto, a surface associated autolysin of Listeria monocytogenes required for entry into eukaryotic cells and virulence, Mol. Microbiol., 51, 1601, 2004.
41. Cabanes, D. et al., Gp96 is a receptor for a novel Listeria monocytogenes virulence factor, Vip, a surface protein, EMBO J., 2005.
42. Wang, L. and Lin, M., Identification of IspC, an 86-kilodalton protein target of humoral immune response to infection with Listeria monocytogenes serotype 4b, as a novel surface autolysin, J. Bacteriol., 189, 2046, 2007.
43. Gaillard, J.L., Berche, P., and Sansonetti, P., Transposon mutagenesis as a tool to study the role of hemolysin in the virulence of Listeria monocytogenes, Infect. Immun., 52, 50, 1986.
44. Cossart, P. et al., Listeriolysin O is essential for virulence of Listeria monocytogenes: Direct evidence obtained by gene complementation, Infect. Immun., 57, 3629, 1989.
45. Borezee, E. et al., SvpA, a novel surface virulence-associated protein required for intracellular survival of Listeria monocytogenes, Microbiology, 147, 2913, 2001.
46. Geoffroy, C. et al., Purification and characterization of an extracellular 29-kilodalton phospholipase C from Listeria monocytogenes, Infect. Immun., 59, 2382, 1991.
47. Marquis, H., Doshi, V., and Portnoy, D.A., The broad-range phospholipase c and a metalloprotease mediate listeriolysin o-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells, Infect. Immun., 63, 4531, 1995.
48. Schluter, D. et al., Phosphatidylcholine-specific phospholipase c from Listeria monocytogenes is an important virulence factor in murine cerebral listeriosis, Infect. Immun., 66, 5930, 1998.
49. Raveneau, J. et al., Reduced virulence of a Listeria monocytogenes phospholipase-deficient mutant obtained by transposon insertion into the zinc metalloprotease gene, Infect. Immun., 60, 916, 1992.
50. Poyart, C. et al., The zinc metalloprotease of Listeria monocytogenes is required for maturation of phosphatidylcholine phospholipase-c-Direct evidence obtained by gene complementation, Infect. Immun., 61, 1576, 1993.
51. Goetz, M. et al., Microinjection and growth of bacteria in the cytosol of mammalian host cells, Proc. Natl. Acad. Sci. USA, 98, 12221, 2001.
52. Chico-Calero, I. et al., Hpt, a bacterial homolog of the microsomal glucose-6-phosphate translocase, mediates rapid intracellular proliferation in Listeria, Proc. Natl. Acad. Sci. USA, 99, 431, 2002.
53. O’Riordan, M., Moors, M.A., and Portnoy, D.A., Listeria intracellular growth and virulence require host-derived lipoic acid, Science, 302, 462, 2003.
54. Kocks, C. et al., L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein, Cell, 68, 521, 1992.
55. Dussurget, O. et al., Listeria monocytogenes bile salt hydrolase is a PrfA-regulated virulence factor involved in the intestinal and hepatic phases of listeriosis, Mol. Microbiol., 45, 1095, 2002.
56. Christiansen, J.K. et al., The RNA-binding protein Hfq of Listeria monocytogenes: Role in stress tolerance and virulence, J. Bacteriol., 186, 3355, 2004.
57. Rouquette, C. et al., The ClpC ATPase of Listeria monocytogenes is a general stress protein required for virulence and promoting early bacterial escape from the phagosome of macrophages, Mol. Microbiol., 27, 1235, 1998.
58. Nair, S. et al., ClpE, a novel member of the HSP100 family, is involved in cell division and virulence of Listeria monocytogenes, Mol. Microbiol., 31, 185, 1999.
59. Gaillot, O. et al., The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes, Mol. Microbiol., 35, 1286, 2000.
60. Mohamed, W. et al., The ferritin-like protein Frm is a target for the humoral immune response to Listeria monocytogenes and is required for efficient bacterial survival, Mol. Genet. Genomics, 275, 344, 2006.
61. Archambaud, C. et al., Control of Listeria superoxide dismutase by phosphorylation, J. Biol. Chem., 2006.
62. Mackaness, G.B., Cellular resistance to infection, J. Exp. Med., 116, 381, 1962.
63. Mackaness, G.B. and Hill, W.C., The effect of antilymphocyte globulin on cell-mediated resistance to infection, J. Exp. Med., 129, 993, 1969.
64. Brosch, R. et al., Virulence heterogeneity of Listeria monocytogenes strains from various sources (food, human, animal) in immunocompetent mice and its association with typing characteristics, J. Food Prot., 56, 296, 1993.
65. Pine, L., Malcolm, G.B., and Plikaytis, B.D., Listeria monocytogenes intragastric and intraperitoneal approximate 50% lethal doses for mice are comparable, but death occurs earlier by intragastric feeding, Infect. Immun., 58, 2940, 1990.
66. Munder, A. et al., Pulmonary microbial infection in mice: Comparison of different application methods and correlation of bacterial numbers and histopathology, Exp. Toxicol. Pathol., 54, 127, 2002.
67. Audurier, A. et al., Experimental infection of mice with Listeria monocytogenes and L. innocua, Ann. Inst. Pasteur Microbiol., 131 B, 47, 1980.
68. Stams, A., Studies in cases of experimental eye infections with Listeria monocytogenes, Albrecht Von Graefes Arch. Klin. Exp. Ophthalmol., 173, 1, 1967.
69. Schluter, D. et al., Intracerebral targets and immunomodulation of murine Listeria monocytogenes meningoencephalitis, J. Neuropathol. Exp. Neurol., 55, 14, 1996.
70. Nishikawa, S. et al., Systemic dissemination by intrarectal infection with Listeria monocytogenes in mice, Microbiol. Immunol., 42, 325, 1998.
71. Reed, L.J. and Muench, H., A simple method of estimating fifty per cent endpoints, Am. J. Hyg., 27, 493, 1938.
72. Welkos, S. and O’Brien, A., Determination of median lethal and infectious doses in animal model systems, Methods Enzymol., 235, 29, 1994.
73. Finney, D.J., Probit analyses, 3rd ed., Cambridge University Press, London, 1971.
74. Roche, S.M. et al., Experimental validation of low virulence in field strains of Listeria monocytogenes, Infect. Immun., 71, 3429, 2003.
75. Liu, D., Listeria monocytogenes: Comparative interpretation of mouse virulence assay, FEMS Microbiol. Lett., 233, 159, 2004.
76. Mandel, T.E. and Cheers, C., Resistance and susceptibility of mice to bacterial infection: Histopathology of listeriosis in resistant and susceptible strains, Infect. Immun., 30, 851, 1980.
77. Gray, M.L. and Killinger, A.H., Listeria monocytogenes and listeric infections, Bacteriol. Rev., 30, 309, 1966.
78. Pohjanvirta, R. and Huttunen, T., Some aspects of murine experimental listeriosis, Acta Vet. Scand., 26, 563, 1985.
79. Lecuit, M. and Cossart, P., Genetically modified animal models for human infections: The Listeria paradigm, Trends Mol. Med., 8, 537, 2002.
80. Lecuit, M. et al., A single amino acid in E-cadherin responsible for host specificity towards the human pathogen Listeria monocytogenes, EMBO J., 18, 3956, 1999.
81. Cheers, C. et al., Use of recombinant viruses to deliver cytokines influencing the course of experimental bacterial infection, Immunol. Cell Biol., 77, 324, 1999.
82. Stelma, G.N. et al., Pathogenicity test for Listeria monocytogenes using immunocompromised mice, J. Clin. Microbiol., 25, 2085, 1987.
83. Lecuit, M. et al., A transgenic model for listeriosis: Role of internalin in crossing the intestinal barrier, Science, 292, 1722, 2001.
84. Khelef, N. et al., Species specificity of the Listeria monocytogenes InlB protein, Cell Microbiol., 8, 457, 2006.
85. Barbour, A.H., Rampling, A., and Hormaeche, C.E., Variation in the infectivity of Listeria monocytogenes isolates following intragastric inoculation of mice, Infect. Immun., 69, 4657, 2001.
86. Murray, E.G.D., Webb, R.A., and Swann, M.B.R., A disease of rabbits characterized by a large mononuclear leucocytosis, caused by a hitherto undescribed bacillus Bacterium monocytogenes, J. Pathol. Bacteriol., 29, 407, 1926.
87. Waseem, M., Vahidy, R., and Khan, M.A., Correlation between production of listeriolysin O by variants of Listeria monocytogenes and their virulence for rabbits, Zentralbl. Bakteriol., 282, 384, 1995.
88. Pron, B. et al., Comprehensive study of the intestinal stage of listeriosis in a rat ligated ileal loop system, Infect. Immun., 66, 747, 1998.
89. Anton, W., Kritish-experimenteller Beitrag zur Biologie des Bakterium monocytogenes. Mit besonderer Berücksichtigung seiner Beziehung zur infektiösen Mononukleose des Menschen, Zentralbl. Bakteriol., 131, 89, 1934.
90. Paterson, J.S., Experimental infection of the chick embryo with organisms of the genus Listerella, J. Pathol. Bacteriol., 51, 437, 1940.
91. Basher, H.A. et al., Pathogenesis and growth of Listeria monocytogenes in fertile hens’ eggs, Zentralbl. Bakteriol. Mikrobiol. Hyg. [A], 256, 477, 1984.
92. Notermans, S. et al., The chick embryo test agrees with the mouse bio-assay for assessment of the pathogenicity of Listeria species, Lett. Appl. Microbiol., 13, 161, 1991.
93. Norrung, B. and Andersen, J.K., Variations in virulence between different electrophoretic types of Listeria monocytogenes, Lett. Appl. Microbiol., 30, 228, 2000.
94. Norton, D.M. et al., Molecular studies on the ecology of Listeria monocytogenes in the smoked fish processing industry, Appl. Environ. Microbiol., 67, 198, 2001.
95. Avery, S.M. and Buncic, S., Differences in pathogenicity for chick embryos and growth kinetics at 37°C between clinical and meat isolates of Listeria monocytogenes previously stored at 4°C, Int. J. Food Microbiol., 34, 319, 1997.
96. Olier, M. et al., Assessment of the pathogenic potential of two Listeria monocytogenes human fecal carriage isolates, Microbiology, 148, 1855, 2002.
97. Cappelier, J.M. et al., Avirulent viable but nonculturable cells of Listeria monocytogenes need the presence of an embryo to be recovered in egg yolk and regain virulence after recovery, Vet. Res., 38, 573, 2007.
98. Lebrun, M. et al., Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells, Mol. Microbiol., 21, 579, 1996.
99. Portnoy, D.A., Jacks, P.S., and Hinrichs, D.J., Role of hemolysin for the intracellular growth of Listeria monocytogenes, J. Exp. Med., 167, 1459, 1988.
100. Smith, G.A. et al., The two distinct phospholipases c of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread, Infect. Immun., 63, 4231, 1995.
101. Bhunia, A.K. et al., A six-hour in vitro virulence assay for Listeria monocytogenes using myeloma and hybridoma cells from murine and human sources, Microb. Patholog., 16, 99, 1994.
102. Sun, A.N., Camilli, A., and Portnoy, D.A., Isolation of Listeria monocytogenes small plaque mutants defective for intracellular growth and cell-to-cell spread, Infect. Immun., 58, 3770, 1990.
103. Farber, J.M. and Speirs, J.I., Potential use of continuous cell lines to distinguish between pathogenic and nonpathogenic Listeria spp., J. Clin. Microbiol., 25, 1463, 1987.
104. Gaillard, J.L. et al., In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2, Infect. Immun., 55, 2822, 1987.
105. Pine, L. et al., Cytopathogenic effects in enterocytelike Caco-2 cells differentiate virulent from avirulent Listeria strains, J. Clin. Microbiol., 29, 990, 1991.
106. Lecuit, M. et al., A role for alpha- and beta-catenins in bacterial uptake, Proc. Natl. Acad. Sci. USA, 97, 10008, 2000.
107. Grundling, A., Gonzalez, M.D., and Higgins, D.E., Requirement of the Listeria monocytogenes broad-range phospholipase PC-PLC during infection of human epithelial cells, J. Bacteriol., 185, 6295, 2003.
108. Meyer, D.H. et al., Differences in invasion and adherence of Listeria monocytogenes with mammalian gut cells, Food Microbiol., 9, 115, 1992.
109. Milohanic, E. et al., Sequence and binding activity of the autolysin-adhesin Ami from epidemic Listeria monocytogenes 4b, Infect. Immun., 72, 4401, 2004.
110. Singh, R. et al., Fusion to listeriolysin O and delivery by Listeria monocytogenes enhances the immunogenicity of HER-2/neu and reveals subdominant epitopes in the FVB/N mouse, J. Immun., 175, 3663, 2005.
111. Suarez, M. et al., A role for ActA in epithelial cell invasion by Listeria monocytogenes, Cell Microbiol., 3, 853, 2001.
112. Pentecost, M. et al., Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion, PLoS Pathol., 2, e3, 2006.
113. Braun, L., Ohayon, H., and Cossart, P., The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells, Mol. Microbiol., 27, 1077, 1998.
114. Barry, R.A. et al., Pathogenicity and immunogenicity of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread, Infect. Immun., 60, 1625, 1992.
115. Nichterlein, T. and Hof, H., Effect of various antibiotics on Listeria monocytogenes multiplying in L-929 cells, Infection, 19, S234, 1991.
116. Devenish, J.A. and Schiemann, D.A., HeLa cell infection by Yersinia enterocolitica: Evidence for lack of intracellular multiplication and development of a new procedure for quantitative expression of infectivity, Infect. Immun., 32, 48, 1981.
117. Velge, P. et al., Cell immortalization enhances Listeria monocytogenes invasion, Med. Microbiol. Immunol., 183, 145, 1994.
118. Drevets, D.A. et al., Gentamicin kills intracellular Listeria monocytogenes, Infect. Immun., 62, 1994. 2222.
119. Roche, S.M. et al., Investigation of specific substitutions in virulence genes characterizing phenotypic groups of low-virulence field strains of Listeria monocytogenes, Appl. Environ. Microbiol., 71, 6039, 2005.
120. Velge, P. et al., A naturally occurring mutation K220T in the pleiotropic activator PrfA of Listeria monocytogenes results in a loss of virulence due to decreasing DNA-binding affinity, Microbiology, 153, 995, 2007.
121. Autret, N. et al., Identification of new genes involved in the virulence of Listeria monocytogenes by signature-tagged transposon mutagenesis, Infect. Immun., 69, 2054, 2001.
122. Mansfield, B.E. et al., Exploration of host-pathogen interactions using Listeria monocytogenes and Drosophila melanogaster, Cell Microbiol., 5, 901, 2003.
123. Thomsen, L.E. et al., Caenorhabditis elegans is a model host for Listeria monocytogenes, Appl. Environ. Microbiol., 72, 1700, 2006.
124. Cheng, L.W. et al., Use of RNA interference in Drosophila S2 cells to identify host pathways controlling compartmentalization of an intracellular pathogen, Proc. Natl. Acad. Sci. USA, 102, 13646, 2005.
125. Agaisse, H. et al., Genome-wide RNAi screen for host factors required for intracellular bacterial infection, Science, 309, 1248, 2005.
126. Seeliger, H.P.R. and Höhne, K., Serotyping of Listeria monocytogenes and related species. In Methods in microbiology, Bergan, T. and Norris, J.R., eds., Academic Press, Inc., New York, 1979, 31.
127. Rocourt, J., Jacquet, C., and Reilly, A., Epidemiology of human listeriosis and seafoods, Int. J. Food Microbiol., 62, 197, 2000.
128. Rocourt, J., Taxonomy of the Listeria genus and typing of L. monocytogenes, Pathol. Biol., 44, 749, 1996.
129. Ortiz-Rivera, R.R., Swaminathan, B., and Fields, P.I., Identification of flagellar antigens of Listeria monocytogenes by sequence-specific amplification of flaA alleles, in IV International Meeting on Bacterial Epidemiological Markers, Helsinor, Denmark, 10-13 September, 1997, S102.
130. Doumith, M. et al., Differentiation of the major Listeria monocytogenes serovars by multiplex PCR, J. Clin. Microbiol., 42, 3819, 2004.
131. Czuprynski, C.J., Faith, N.G., and Steinberg, H., Ability of the Listeria monocytogenes strain Scott A to cause systemic infection in mice infected by the intragastric route, Appl. Environ. Microbiol., 68, 2893, 2002.
132. Jeffers, G.T. et al., Comparative genetic characterization of Listeria monocytogenes isolates from human and animal listeriosis cases, Microbiology, 147, 1095, 2001.
133. Swaminathan, B. et al., Pulsenet: The molecular subtyping network for food-borne bacterial disease surveillance, United States, Emerg. Infect. Dis., 7, 382, 2001.
134. Kathariou, S. et al., Levels of Listeria monocytogenes hemolysin are not directly proportional to virulence in experimental infections of mice, Infect. Immun., 56, 534, 1988.
135. Jacquet, C. et al., Expression of ActA, Ami, InlB, and listeriolysin O in Listeria monocytogenes of human and food origin, Appl. Environ. Microbiol., 68, 616, 2002.
136. Kathariou, S., Listeria monocytogenes virulence and pathogenicity, a food safety perspective, J. Food Prot., 65, 1811, 2002.
137. Jacquet, C. et al., A molecular marker for evaluating the pathogenic potential of food-borne Listeria monocytogenes, J. Infect. Dis., 189, 2094, 2004.
138. Cheers, C. et al., Resistance and susceptibility of mice to bacterial infection: Course of listeriosis in resistant or susceptible mice, Infect. Immun., 19, 763, 1978.
139. Mengaud, J. et al., Pleiotropic control of Listeria monocytogenes virulence factors by a gene that is autoregulated, Mol. Microbiol., 5, 2273, 1991.
140. Wernars, K. et al., Suitability of the prfA gene, which encodes a regulator of virulence genes in Listeria monocytogenes, in the identification of pathogenic Listeria spp., Appl. Environ. Microbiol., 58, 765, 1992.
141. Bhunia, A.K. et al., Frozen stored murine hybridoma cells can be used to determine the virulence of Listeria monocytogenes, J. Clin. Microbiol., 33, 3349, 1995.
142. Nishibori, T. et al., Correlation between the presence of virulence-associated genes as determined by PCR and actual virulence to mice in various strains of Listeria spp., Microbiol. Immunol., 39, 343, 1995.
143. Wiedmann, M. et al., Ribotypes and virulence gene polymorphisms suggest three distinct Listeria monocytogenes lineages with differences in pathogenic potential, Infect. Immun., 65, 2707, 1997.
144. Jaradat, Z.W., Schutze, G.E., and Bhunia, A.K., Genetic homogeneity among Listeria monocytogenes strains from infected patients and meat products from two geographic locations determined by phenotyping, ribotyping and PCR analysis of virulence genes, Int. J. Food Microbiol., 76, 1, 2002.
145. Borucki, M.K. et al., Selective discrimination of Listeria monocytogenes epidemic strains by a mixedgenome DNA microarray compared to discrimination by pulsed-field gel electrophoresis, ribotyping, and multilocus sequence typing, J. Clin. Microbiol., 42, 5270, 2004.
146. Liu, D., Identification, subtyping and virulence determination of Listeria monocytogenes, an important food-borne pathogen, J. Med. Microbiol., 55, 645, 2006.
147. Liu, D. et al., A multiplex PCR for species- and virulence-specific determination of Listeria monocytogenes, J. Microbiol. Methods, 71, 133, 2007.
148. Chakraborty, T. et al., Naturally occurring virulence-attenuated isolates of Listeria monocytogenes capable of inducing long-term protection against infection by virulent strains of homologous and heterologous serotypes, FEMS Immunol. Med. Microbiol., 10, 1, 1994.
149. Gracieux, P. et al., Hypovirulent Listeria monocytogenes strains are less frequently recovered than virulent strains on PALCAM and Rapid’ L. mono media, Int. J. Food Microbiol., 83, 133, 2003.