1. Coenye T, Vandamme P. Diversity and signi-ficance of Burkholderia species occupying diverse ecological niches. Environ Microbiol 2003;5:719-29. doi:10.1046/j.1462-2920.2003.00471.x. 2. Stone R. Infectious disease. Racing to defuse a bacterial time bomb. Science 2007; 317:1022-24. doi: 10.1126/science.317.5841.1022. 3. Lee YH, Chen Y, Ouyang X, Gan YH. Identi-fication of tomato plant as a novel host model for Burkholderia pseudomallei. BMC microbiol 2010;10:1. doi: 10.1186/1471-2180-10-28. 4. Wuthiekanun V, Suputtamongkol Y, Simpson AJH, Kanaphun P, White NJ. Value of throat swab in diagnosis of melioidosis. J clin microbiol 2001; 39: 3801-2. doi.org/10.1128/JCM.39.10.3801-3802.2001. 5. Cheng AC, Currie BJ. Melioidosis: epidemiology, pathophysiology and management. Clin microbiol rev 2005;18: 383-416. doi.org/10.1128/CMR.18.2.383-416.2005. 6. Wongtrakoongate P, Mongkoldhumrongkul N, Chaijan S, Kamchonwongpaisan S, Tung-pradabkul S. Comparative proteomic profiles and the potential markers between Burkholderia pseudomallei and Burkholderia thailandensis. Mol cell probe 2007;21: 81-91. doi.org/10.1016/j.mcp.2006.08.006. 7. Cruz-Migoni A, Hautbergue GM, Artymiuk PJ, Baker PJ, Bokori-Brown M, Chang C-T, et al. A Burkholderia pseudomallei toxin inhibits helicase activity of translation factor eIF4A. Science 2011; 334: 821-4. doi: 10.1126/science.1211915. 8. Medina-Bolivar F, Wright R, Funk V, Sentz D, Barroso L, Wilkins TD, et al. A non-toxic lectin for antigen delivery of plant-based mucosal vaccines. Vaccine 2003;21:997-1005. doi.org/10.1016/S0264-410X(02)00551-0 9. Akbari M, Saadati M, Honari H, Mohammad Ghorbani H. IpaD-loaded N-trimethyl Chitosan Nanoparticles Can Efficiently Protect Guinea Pigs against Shigella Flexneri. Iran J Immunol 2019; 16: 212-24. doi.org/10.22034/iji.2019.80272. 10. Abkar M, Fasihi-Ramandi M, Kooshki H, Sahebghadam LA. Oral immunization of mice with Omp31-loaded N-trimethyl chitosan nanoparticles induces high protection against Brucella melitensis infection. Int J Nanomedicine 2017;12: 8769-78. doi: 10.2147/IJN.S149774. 11. Masoudi M, Honari H, Abdollah M. Expression of Blf1-Stx B Gene Cassette in E. coli and Investigation Antibody Titer in Mice. J Shahid Sadoughi Uni Med Sci 2017;24: 876-86. 12. Masoudi M, Honari H, Etemadaubi M, Abdollah M. Comparison of the Titers of Produced Antibodies against BLF1 and BLF1-STxB Recombinant Proteins in Laboratory Rats. J Ilam Uni Med Sci 2019;26: 111-21. doi: 10.29252/sjimu.26.6.111. 13. Bollag D.M, Rozycki MD, Edelstein SJ. Protein methods. Wileyliss NY. 1996. 14. Daniel MB, Rozycki MD, Edelstein S. J. Affinity chromatography. Protein methods. New York: Wiley-Liss, 1996. 15. Walsh MJ, Dodd JE, Hautbergue GM. Ribosome-inactivating proteins: Potent poisons and molecular tools. Virulence 2013; 4: 774-84. doi.org/10.4161/viru.26399. 16. Rotz LD, Khan AS, Lillibridge SR, Ostroff SM, Hughes JM . Public health assessment of potential biological terrorism agents. Emerg Infect Dis 2002; 8: 225-30. doi: 10.3201/eid0802.010164. 17. Malina A, Cencic R, Pelletier J. Targeting translation dependence in cancer. Oncotarget. 2011; 2:76-88. doi: 10.18632/oncotarget.218. 18. Currie BJ. Melioidosis and Burkholderia pseudo-mallei: progress in epidemiology, diagnosis, treatment and vaccination. Curr Opin Infect Dis 2022;35:517-23. doi: 10.1097/QCO.0000000000000869. 19. German RR. Updated guidelines for evaluating public health surveillance systems. MMWR Recomm Rep 2001. 50:1-35. 20. Clemens J, Kotloff K, Kay BA. Generic protocol to estimate the burden of Shigella diarrhoea and dysenteric mortality. Citeseer,1999. 21. Dutta Sh, Dutta D, Dutta P, Matsushita Sh, Kumar Bhattacharya S, Yoshida SH. Shigella dysenteriae serotype 1, Kolkata, India. Emerg Infect Dis 2003; 9:1471-74. doi: 10.3201/eid0911.020652. 22. Imai Y, Ishikawa T, Tanikawa T, Nakagami H, Maekawa T, Kurohane K. Production of IgA monoclonal antibody against Shiga toxin binding subunits employing nasal-associated lymphoid tissue. J Immunol Methods 2005; 302:125-35. doi:org/10.1016/j.jim.2005.05.007. 23. Marcato P, Griener TP, Mulvey GL, Armstrong GD. Recombinant Shiga toxin B-subunit-keyhole limpet hemocyanin conjugate vaccine protects mice from Shigatoxemia. Infect Immun 2005;73:6523-29. doi:org/10.1128/IAI.73.10.6523-6529.2005. 24. Tsuji T, Shimizu T, Sasaki K, Tsukamoto K, Arimitsu H, Ochi S. et al. A nasal vaccine comprising B-subunit derivative of Shiga toxin 2 for cross-protection against Shiga toxin types 1 and 2. Vaccine 2008;26:2092-9. doi:org/10.1016/j.vaccine.2008.02.034. 25. Fujii J, Naito M, Yutsudo T, Matsumoto S, Heatherly DP, Yamada T, et al. Protection by a recombinant Mycobacterium bovis Bacillus Calmette-Guerin vaccine expressing Shiga toxin 2 B subunit against Shiga toxin-producing Escherichia coli in mice. Clin Vaccine Immunol 2012;19:1932-7. doi:org/10.1128/CVI.00473-12. 26. Xu R. Particle characterization: light scattering methods. Vol. 13. Springer Science & Business Media. 2001. 27. Ghalavand M, Saadati M, Salimian J, Abbasi E, Ahmadi A. Synthesis and Immunogenicity Evaluation of Tetanus Toxoid Encapsulated Trimethyl Chitosan Nanoparticles. J Mazandaran Uni Med Sci 2017;26:54-62. 28. Malik A, Gupta M, Mani R, Gogoi H, Bhatnagar R. Trimethyl chitosan nanoparticles encapsulated protective antigen protects the mice against anthrax. Front Immunol 2018; 20: 562. doi.org/10.3389/fimmu.2018.00562 29. Soleimani N, Mohabati-Mobarez A, Atyabi F, Hasan-Saraf Z, Haghighi MA. Preparation of chitosan nanoparticles carrying recombinant Helicobacter pylori neutrophil-activating protein. J Mazandaran Uni Med Sci 2014; 23:134-44.
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