Veterinary Medicine International

Copyright © 2017 Carolina Gallego et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

1. F. Dziva, A. P. Muhairwa, M. Bisgaard, and H. Christensen, “Diagnostic and typing options for investigating diseases associated with Pasteurella multocida,” Veterinary Microbiology, vol. 128, no. 1-2, pp. 1–22, 2008. View at Publisher · View at Google Scholar · View at Scopus
2. E. Kawamoto, T. Sawada, and T. Maruyama, “Evaluation of transport media for Pasteurella multocida isolates from rabbit nasal specimens,” Journal of Clinical Microbiology, vol. 35, no. 8, pp. 1948–1951, 1997. View at Google Scholar · View at Scopus
3. H. Takashima, H. Sakai, T. Yanai, and T. Masegi, “Detection of antibodies against Pasteurella multocida using immunohistochemical staining in an outbreak of rabbit pasteurellosis,” The Journal of Veterinary Medical Science, vol. 63, no. 2, pp. 171–174, 2001. View at Publisher · View at Google Scholar · View at Scopus
4. Z. Jaglic, E. Jeklova, L. Leva et al., “Experimental study of pathogenicity of Pasteurella multocida serogroup F in rabbits,” Veterinary Microbiology, vol. 126, no. 1–3, pp. 168–177, 2008. View at Publisher · View at Google Scholar · View at Scopus
5. A. B. J. Stahel, R. K. Hoop, P. Kuhnert, and B. M. Korczak, “Phenotypic and genetic characterization of Pasteurella multocida and related isolates from rabbits in Switzerland,” Journal of Veterinary Diagnostic Investigation, vol. 21, no. 6, pp. 793–802, 2009. View at Publisher · View at Google Scholar · View at Scopus
6. M. Jacques, “Role of lipo-oligosaccharides and lipopolysaccharides in bacterial adherence,” Trends in Microbiology, vol. 4, no. 10, pp. 408–410, 1996. View at Publisher · View at Google Scholar · View at Scopus
7. S. N. Abraham, B. L. Bishop, N. Sharon, and I. Ofek, “Adhesion of bacteria to mucosal surfaces,” Mucosal Immunology, Two-Volume Set, pp. 35–48, 2005. View at Publisher · View at Google Scholar · View at Scopus
8. E. Fadda and R. J. Woods, “Molecular simulations of carbohydrates and protein-carbohydrate interactions: motivation, issues and prospects,” Drug Discovery Today, vol. 15, no. 15-16, pp. 596–609, 2010. View at Publisher · View at Google Scholar · View at Scopus
9. S. Sattin and A. Bernardi, “Glycoconjugates and glycomimetics as microbial anti-adhesives,” Trends in Biotechnology, vol. 34, no. 6, pp. 483–495, 2016. View at Publisher · View at Google Scholar · View at Scopus
10. M. Jacques, M. Kobisch, M. Belanger, and F. Dugal, “Virulence of capsulated and noncapsulated isolates of Pasteurella multocida and their adherence to porcine respiratory tract cells and mucus,” Infection and Immunity, vol. 61, no. 11, pp. 4785–4792, 1993. View at Google Scholar · View at Scopus
11. E. T. Reitschel, T. Kirikae, F. U. Shade et al., “Bacterial endotoxin: molecular relationships of structure to activity and function,” The FASEB Journal, vol. 8, no. 2, pp. 217–225, 1994. View at Google Scholar · View at Scopus
12. C. Erridge, E. Bennett-Guerrero, and I. R. Poxton, “Structure and function of lipopolysaccharides,” Microbes and Infection, vol. 4, no. 8, pp. 837–851, 2002. View at Publisher · View at Google Scholar · View at Scopus
13. L. N. López-Bojórquez, A. Z. Dehesa, and G. Reyes-Terán, “Molecular mechanisms involved in the pathogenesis of septic shock,” Archives of Medical Research, vol. 35, no. 6, pp. 465–479, 2004. View at Publisher · View at Google Scholar · View at Scopus
14. C. Risco, J. L. Carrascosa, and M. A. Bosch, “Uptake and subcellular distribution of Escherichia coli lipopolysaccharide by isolated rat Type II pneumocytes,” Journal of Histochemistry and Cytochemistry, vol. 39, no. 5, pp. 607–615, 1991. View at Publisher · View at Google Scholar · View at Scopus
15. M. W. Hornef, B. H. Normark, A. Vandewalle, and S. Normark, “Intracellular recognition of lipopolysaccharide by toll-like receptor 4 in intestinal epithelial cells,” The Journal of Experimental Medicine, vol. 198, no. 8, pp. 1225–1235, 2003. View at Publisher · View at Google Scholar · View at Scopus
16. D. Bravo, A. Hoare, A. Silipo et al., “Different sugar residues of the lipopolysaccharide outer core are required for early interactions of Salmonella enterica serovars Typhi and Typhimurium with epithelial cells,” Microbial Pathogenesis, vol. 50, no. 2, pp. 70–80, 2011. View at Publisher · View at Google Scholar · View at Scopus
17. P.-C. Chang, C.-J. Wang, C.-K. You, and M.-C. Kao, “Effects of a HP0859 (rfaD) knockout mutation on lipopolysaccharide structure of Helicobacter pylori 26695 and the bacterial adhesion on AGS cells,” Biochemical and Biophysical Research Communications, vol. 405, no. 3, pp. 497–502, 2011. View at Publisher · View at Google Scholar · View at Scopus
18. M. Bélanger, S. Rioux, B. Foiry, and M. Jacques, “Affinity for porcine respiratory tract mucus is found in some isolates of Actinobacillus pleuropneumoniae,” FEMS Microbiology Letters, vol. 97, no. 1-2, pp. 119–125, 1992. View at Publisher · View at Google Scholar · View at Scopus
19. E. L. Fletcher, S. M. J. Fleiszig, and N. A. Brennan, “Lipopolysaccharide in adherence of Pseudomonas aeruginosa to the cornea and contact lenses,” Investigative Ophthalmology & Visual Science, vol. 34, no. 6, pp. 1930–1936, 1993. View at Google Scholar · View at Scopus
20. S. K. Gupta, R. S. Berk, S. Masinick, and L. D. Hazlett, “Pili and lipopolysaccharide of Pseudomonas aeruginosa bind to the glycolipid asialo GM1,” Infection and Immunity, vol. 62, no. 10, pp. 4572–4579, 1994. View at Google Scholar · View at Scopus
21. G. B. Pier, N. L. Koles, G. Meluleni, K. Hatano, and M. Pollack, “Specificity and function of murine monoclonal antibodies and immunization- induced human polyclonal antibodies to lipopolysaccharide subtypes of Pseudomonas aeruginosa serogroup 06,” Infection and Immunity, vol. 62, no. 4, pp. 1137–1143, 1994. View at Google Scholar · View at Scopus
22. A. Venable, M. Mitalipova, I. Lyons et al., “Lectin binding profiles of SSEA-4 enriched, pluripotent human embryonic stem cell surfaces,” BMC Developmental Biology, vol. 5, article no. 15, 2005. View at Publisher · View at Google Scholar · View at Scopus
23. J. Yang, Y. Zhao, and F. Shao, “Non-canonical activation of inflammatory caspases by cytosolic LPS in innate immunity,” Current Opinion in Immunology, vol. 32, pp. 78–83, 2015. View at Publisher · View at Google Scholar · View at Scopus
24. F. Kopp, S. Kupsch, and A. B. Schromm, “Lipopolysaccharide-binding protein is bound and internalized by host cells and colocalizes with LPS in the cytoplasm: implications for a role of LBP in intracellular LPS-signaling,” Biochimica et Biophysica Acta&Molecular Cell Research, vol. 1863, no. 4, pp. 660–672, 2016. View at Publisher · View at Google Scholar · View at Scopus
25. T. Hatfaludi, K. Al-Hasani, J. D. Boyce, and B. Adler, “Outer membrane proteins of Pasteurella multocida,” Veterinary Microbiology, vol. 144, no. 1-2, pp. 1–17, 2010. View at Publisher · View at Google Scholar · View at Scopus
26. K. M. Townsend, J. D. Boyce, J. Y. Chung, A. J. Frost, and B. Adler, “Genetic organization of Pasteurella multocida cap loci and development of a multiplex capsular PCR typing system,” Journal of Clinical Microbiology, vol. 39, no. 3, pp. 924–929, 2001. View at Publisher · View at Google Scholar · View at Scopus
27. S. L. Brockmeier and K. B. Register, “Expression of the dermonecrotic toxin by Bordetella bronchiseptica is not necessary for predisposing to infection with toxigenic Pasteurella multocida,” Veterinary Microbiology, vol. 125, no. 3-4, pp. 284–289, 2007. View at Publisher · View at Google Scholar · View at Scopus
28. D. J. Halloy, N. A. Kirschvink, J. Mainil, and P. G. Gustin, “Synergistic action of E. coli endotoxin and Pasteurella multocida type A for the induction of bronchopneumonia in pigs,” Veterinary Journal, vol. 169, no. 3, pp. 417–426, 2005. View at Publisher · View at Google Scholar · View at Scopus
29. D. Bernet, H. Schmidt, W. Meier, P. Burkhardt-Holm, and T. Wahli, “Histopathology in fish: proposal for a protocol to assess aquatic pollution,” Journal of Fish Diseases, vol. 22, no. 1, pp. 25–34, 1999. View at Publisher · View at Google Scholar · View at Scopus
30. O. Westphal and K. Jann, “Bacterial lipopolysaccharides: extraction with phenol-water further applications of this procedure,” Methods in Carbohydrate Chemistry, vol. 5, p. 9, 1965. View at Google Scholar
31. D. Gualtero, J. E. Castellanos, and G. I. Lafaurie, “Porphyromonas gingivalis libre de polisacáridos utilizando cromatografía de alta resolución sephacryl S-200,” Acta Biológica Colombiana, vol. 13, no. 3, pp. 147–160, 2008. View at Google Scholar
32. P. Esquinas, “Comparación ultraestructural de fosa nasal y nasofaringe de Conejos sanos y enfermos con el síndrome de neumonía enzoótica,” in Abstracts IV Reunión Anual de Patología, 2004. View at Google Scholar
33. C. Gallego, A. M. Middleton, N. Martínez, S. Romero, and C. Iregui, “Interaction of Bordetella bronchiseptica and its lipopolysaccharide with in vitro culture of respiratory nasal epithelium,” Veterinary Medicine International, vol. 2013, Article ID 347086, 9 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
34. T. G. Pistole, “Interaction of bacteria and fungi with lectins and lectin-like substances,” Annual Review of Microbiology, vol. 35, pp. 85–112, 1981. View at Publisher · View at Google Scholar · View at Scopus
35. M. D. Abràmofff, P. J. Magalhães, and S. J. Ram, “Image processing with ImageJ Part II,” Biophotonics International, vol. 11, no. 7, pp. 36–43, 2005. View at Google Scholar
36. S. E. Wong, C. E. Winbanks, C. S. Samuel, and T. D. Hewitson, “Lectin histochemistry for light and electron microscopy,” Methods in Molecular Biology, vol. 611, pp. 103–114, 2010. View at Publisher · View at Google Scholar · View at Scopus
37. R. Martínez, N. Martinez, and M. V. Martinez, Diseño de Experimentos en Ciencias Agropecuarias y Biológicas con SAS, SPSS, R Y STATISTIX, Fondo Nacional Universitario—Institución Auxiliar del Cooperativismo, 2011.
38. M. Harper, F. St Michael, M. John et al., “Pasteurella multocida heddleston serovar 3 and 4 strains share a common lipopolysaccharide biosynthesis locus but display both inter- and intrastrain lipopolysaccharide heterogeneity,” Journal of Bacteriology, vol. 195, no. 21, pp. 4854–4864, 2013. View at Publisher · View at Google Scholar · View at Scopus
39. K. Le Blay, P. Gueirard, N. Guiso, and R. Chaby, “Antigenic polymorphism of the lipopolysaccharides from human and animal isolates of Bordetella bronchiseptica,” Microbiology, vol. 143, no. 4, pp. 1433–1441, 1997. View at Publisher · View at Google Scholar · View at Scopus
40. E. T. Harvill, A. Preston, P. A. Cotter, A. G. Allen, D. J. Maskell, and J. F. Miller, “Multiple roles for Bordetella lipopolysaccharide molecules during respiratory tract infection,” Infection and Immunity, vol. 68, no. 12, pp. 6720–6728, 2000. View at Publisher · View at Google Scholar · View at Scopus
41. M. Harper, F. St Michael, M. John et al., “Pasteurella multocida Heddleston serovars 1 and 14 express different lipopolysaccharide structures but share the same lipopolysaccharide biosynthesis outer core locus,” Veterinary Microbiology, vol. 150, no. 3-4, pp. 289–296, 2011. View at Publisher · View at Google Scholar · View at Scopus
42. M. Harper, J. D. Boyce, and B. Adler, “Pasteurella multocida pathogenesis: 125 years after Pasteur,” FEMS Microbiology Letters, vol. 265, no. 1, pp. 1–10, 2006. View at Publisher · View at Google Scholar · View at Scopus
43. J. C. Hodgson, “Endotoxin and mammalian host responses during experimental disease,” Journal of Comparative Pathology, vol. 135, no. 4, pp. 157–175, 2006. View at Publisher · View at Google Scholar · View at Scopus
44. K. Singh, J. W. Ritchey, and A. W. Confer, “Mannheimia haemolytica: bacterial-host interactions in bovine Pneumonia,” Veterinary Pathology, vol. 48, no. 2, pp. 338–348, 2011. View at Publisher · View at Google Scholar · View at Scopus
45. P. Patiño, Efectos morfológicos y distribución del lipopolisacárido de Pasteurella multocida en el tracto respiratorio de conejos expuestos intranasalmente [M.S. thesis], Universidad Nacional de Colombia, 2016.
46. R. Y. Hampton and C. R. H. Raetz, “Macrophage catabolism of lipid A is regulated by endotoxin stimulation,” Journal of Biological Chemistry, vol. 266, no. 29, pp. 19499–19509, 1991. View at Google Scholar · View at Scopus
47. P. G. Adams, L. Lamoureux, K. L. Swingle, H. Mukundan, and G. A. Montaño, “Lipopolysaccharide-induced dynamic lipid membrane reorganization: tubules, perforations, and stacks,” Biophysical Journal, vol. 106, no. 11, pp. 2395–2407, 2014. View at Publisher · View at Google Scholar · View at Scopus
48. M. P. Carrillo, N. M. Martinez, M. D. P. Patiño, and C. A. Iregui, “Inhibition of pasteurella multocida adhesion to rabbit respiratory epithelium using lectins,” Veterinary Medicine International, vol. 2015, Article ID 365428, 10 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
49. E. T. Rietschel and H. Brade, “Bacterial endotoxins,” Scientific American, vol. 267, no. 2, pp. 54–61, 1992. View at Google Scholar · View at Scopus
50. I. W. Devoe and J. E. Gilchrist, “Release of endotoxin in the form of cell wall blebs during in vitro growth of Neisseria meningitidis,” Journal of Experimental Medicine, vol. 138, no. 5, pp. 1156–1167, 1973. View at Publisher · View at Google Scholar · View at Scopus
51. H. Al-Haj Ali, T. Sawada, H. Hatakeyama, Y. Katayama, N. Ohtsuki, and O. Itoh, “Invasion of chicken embryo fibroblast cells by avian Pasteurella multocida,” Veterinary Microbiology, vol. 104, no. 1-2, pp. 55–62, 2004. View at Publisher · View at Google Scholar · View at Scopus
52. T. O. Schaffner, J. Hinds, K. A. Gould et al., “A point mutation in cpsE renders Streptococcus pneumoniae nonencapsulated and enhances its growth, adherence and competence,” BMC Microbiology, vol. 14, no. 1, article no. 210, 2014. View at Publisher · View at Google Scholar · View at Scopus
53. P. Esquinas, L. Botero, M. D. P. Patiño, C. Gallego, and C. Iregui, “Ultrastructural comparison of the nasal epithelia of healthy and naturally affected rabbits with pasteurella multocida A,” Veterinary Medicine International, vol. 2013, Article ID 321390, 8 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
54. N. Mukaida, Y. Ishikawa, N. Ikeda et al., “Novel insight into molecular mechanism of endotoxin shock: biochemical analysis of LPS receptor signaling in a cell-free system targeting NF-κB and regulation of cytokine production/action through β2 integrin in vivo,” Journal of Leukocyte Biology, vol. 59, no. 2, pp. 145–151, 1996. View at Google Scholar · View at Scopus
55. M. Yarim, S. Karahan, and N. Kabakci, “Immunohistochemical investigation of CD14 in experimental rabbit pneumonic pasteurellosis,” Revue de Medecine Veterinaire, vol. 156, no. 1, pp. 13–19, 2005. View at Google Scholar · View at Scopus
56. M. Lu, A. W. Varley, S. Ohta, J. Hardwick, and R. S. Munford, “Host inactivation of bacterial lipopolysaccharide prevents prolonged tolerance following gram-negative bacterial infection,” Cell Host and Microbe, vol. 4, no. 3, pp. 293–302, 2008. View at Publisher · View at Google Scholar · View at Scopus
57. J. Pugin, C.-C. Schürer-Maly, D. Leturcq, A. Moriarty, R. J. Ulevitch, and P. S. Tobias, “Lipopolysaccharide activation of human endothelial and epithelial cells is mediated by lipopolysaccharide-binding protein and soluble CD14,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 7, pp. 2744–2748, 1993. View at Publisher · View at Google Scholar · View at Scopus
58. A. Haziot, E. Ferrero, F. Köntgen et al., “Resistance to endotoxin shock and reduced dissemination of gram-negative bacteria in CD14-deficient mice,” Immunity, vol. 4, no. 4, pp. 407–414, 1996. View at Publisher · View at Google Scholar · View at Scopus
59. T. Vasselon, E. Mailman, R. Thieringer, and P. A. Detmers, “Internalization of monomeric lipopolysaccharide occurs after transfer out of cell surface CD14,” Journal of Experimental Medicine, vol. 190, no. 4, pp. 509–521, 1999. View at Publisher · View at Google Scholar · View at Scopus
60. L. Guillott, S. Medjane, K. Le-Barillec et al., “Response of human pulmonary epithelial cells to lipopolysaccharide involves toll-like receptor 4 (TLR4)-dependent signaling pathways: evidence for an intracellular compartmentalization of TLR4,” Journal of Biological Chemistry, vol. 279, no. 4, pp. 2712–2718, 2004. View at Publisher · View at Google Scholar · View at Scopus
61. C. M. Greene and N. G. McElvaney, “Toll-like receptor expression and function in airway epithelial cells,” Archivum Immunologiae et Therapiae Experimentalis, vol. 53, no. 5, pp. 418–427, 2005. View at Google Scholar · View at Scopus
62. S. W. Wong, M.-J. Kwon, A. M. K. Choi, H.-P. Kim, K. Nakahira, and D. H. Hwang, “Fatty acids modulate toll-like receptor 4 activation through regulation of receptor dimerization and recruitment into lipid rafts in a reactive oxygen species-dependent manner,” Journal of Biological Chemistry, vol. 284, no. 40, pp. 27384–27392, 2009. View at Publisher · View at Google Scholar · View at Scopus
63. A. B. Lentsch and P. A. Ward, “Regulation of experimental lung inflammation,” Respiration Physiology, vol. 128, no. 1, pp. 17–22, 2001. View at Publisher · View at Google Scholar · View at Scopus
64. C.-C. Tsai, M.-T. Lin, J.-J. Wang, J.-F. Liao, and W.-T. Huang, “The antipyretic effects of baicalin in lipopolysaccharide-evoked fever in rabbits,” Neuropharmacology, vol. 51, no. 4, pp. 709–717, 2006. View at Publisher · View at Google Scholar · View at Scopus
65. B. A. Mizock, “The multiple organ dysfunction syndrome,” Disease-a-Month, vol. 55, no. 8, pp. 476–526, 2009. View at Publisher · View at Google Scholar · View at Scopus
66. O. S. Ali, L. Adamu, F. F. J. Abdullah et al., “Alterations in interleukin-1β and interleukin-6 in mice inoculated through the oral routes using graded doses of p. multocida type b: 2 and its lipopolysaccharide,” American Journal of Animal and Veterinary Sciences, vol. 10, no. 1, pp. 1–8, 2015. View at Publisher · View at Google Scholar · View at Scopus
67. F. Yan, W. Li, H. Jono et al., “Reactive oxygen species regulate Pseudomonas aeruginosa lipopolysaccharide-induced MUC5AC mucin expression via PKC-NADPH oxidase-ROS-TGF-α signaling pathways in human airway epithelial cells,” Biochemical and Biophysical Research Communications, vol. 366, no. 2, pp. 513–519, 2008. View at Publisher · View at Google Scholar · View at Scopus
68. P.-R. Burgel, E. Escudier, A. Coste et al., “Relation of epidermal growth factor receptor expression to goblet cell hyperplasia in nasal polyps,” Journal of Allergy and Clinical Immunology, vol. 106, no. 4, pp. 705–712, 2000. View at Publisher · View at Google Scholar · View at Scopus
69. K. Takeyama, J. V. Fahy, and J. A. Nadel, “Relationship of epidermal growth factor receptors to goblet cell production in human bronchi,” American Journal of Respiratory and Critical Care Medicine, vol. 163, no. 2, pp. 511–516, 2001. View at Publisher · View at Google Scholar · View at Scopus
70. J. H. Kim, S. Y. Lee, S. M. Bak et al., “Effects of matrix metalloproteinase inhibitor on LPS-induced goblet cell metaplasia,” American Journal of Physiology—Lung Cellular and Molecular Physiology, vol. 287, no. 1, pp. L127–L133, 2004. View at Publisher · View at Google Scholar · View at Scopus
71. W. Li, F. Yan, H. Zhou et al., “P. aeruginosa lipopolysaccharide-induced MUC5AC and CLCA3 expression is partly through Duox1 in vitro and in vivo,” PLoS ONE, vol. 8, no. 5, Article ID e63945, 2013. View at Publisher · View at Google Scholar · View at Scopus
72. C. D. Bingle, K. Wilson, H. Lunn et al., “Human LPLUNC1 is a secreted product of goblet cells and minor glands of the respiratory and upper aerodigestive tracts,” Histochemistry and Cell Biology, vol. 133, no. 5, pp. 505–515, 2010. View at Publisher · View at Google Scholar · View at Scopus
73. L. Bingle and C. D. Bingle, “Distribution of human PLUNC/BPI fold-containing (BPIF) proteins,” Biochemical Society Transactions, vol. 39, no. 4, pp. 1023–1027, 2011. View at Publisher · View at Google Scholar · View at Scopus
74. J. A. Bartlett, B. J. Hicks, J. M. Schlomann, S. Ramachandran, W. M. Nauseef, and P. B. McCray, “PLUNC is a secreted product of neutrophil granules,” Journal of Leukocyte Biology, vol. 83, no. 5, pp. 1201–1206, 2008. View at Publisher · View at Google Scholar · View at Scopus
75. B. Ghafouri, E. Kihlström, C. Tagesson, and M. Lindahl, “PLUNC in human nasal lavage fluid: multiple isoforms that bind to lipopolysaccharide,” Biochimica et Biophysica Acta, vol. 1699, no. 1-2, pp. 57–63, 2004. View at Publisher · View at Google Scholar · View at Scopus