A possible explanation of the germicide effect of carbon dioxide in supercritical state based on molecular-biological evidence

Medical Hypotheses

Volumn 74, Issue 2, 2010, Pages 325-329

  András, Csaba D ^a,b   Csajági, Csaba ^c   Orbán, Csongor K ^a   Albert, Csilla ^a   Ábrahám, Beáta ^a   Miklóssy, Ildikó ^a  

^a Sapientia Hungarian University of Transylvania from Cluj Napoca   (Romania)

^b BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

^c Luminochem Ltd   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; CARBAMOYL METHIONINE TRANSFER RNA; CARBON DIOXIDE; FORMYL METHIONINE TRANSFER RNA; GUANOSINE TRIPHOSPHATE INITIATION FACTOR 2; INITIATION FACTOR 2; METHIONINE TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BACTERICIDAL ACTIVITY; COMPLEX FORMATION; MICROBIAL ACTIVITY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN RNA BINDING; PROTEIN SYNTHESIS INHIBITION; TRANSLATION INITIATION; VISCOSITY;

ANTI-BACTERIAL AGENTS; BACTERIAL PHYSIOLOGICAL PHENOMENA; BACTERIAL PROTEINS; CARBON DIOXIDE; CELL SURVIVAL; MODELS, BIOLOGICAL; PRESSURE; SIGNAL TRANSDUCTION; STERILIZATION;

BACTERIA (MICROORGANISMS); MAMMALIA; PROKARYOTA;

EID: 72649099493     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2009.08.043     Document Type: Article

References (52)

1. Hubert P., and Vitzthum O.G. Fluid extraction of hops, spices, and tobacco with supercritical gases. Angew Chem Int Ed Engl 17 10 (1978) 710-715
2. Simándi B., and Sawinsky J. Novel industrial applications of supercritical fluids. Oil Soap Cosmet (in Hungarian) 51 special issue (2002) 3-9
3. Jung J., and Perrut M. Particle design using supercritical fluids: literature and patent survey. J Supercrit Fluids 20 3 (2001) 179-219
4. Reverchon E., and Adami R. Nanomaterials and supercritical fluids. J Supercrit Fluids 37 1 (2006) 1-22
5. Spilimbergo S., Elvassore R., and Bertucco A. Microbial inactivation by high-pressure. J Supercrit Fluids 22 1 (2002) 55-63
6. 2 on total microbial populations and bacterial spores in raw milk. J Dairy Sci 89 3 (2006) 872-881
7. Dillow A.K., Dehghani F., Hrkach J.S., Foster N.R., and Langer R. Bacterial inactivation by using near- and supercritical carbon dioxide. Proc Natl Acad Sci 96 18 (1999) 10344-10348
8. Fages J., Poirier B., Barbier Y., et al. Viral inactivation of human bone tissue using supercritical fluid extraction. ASAIO J 44 4 (1998) 289-293
9. White A., Burns D., and Christensen T.W. Effective terminal sterilization using supercritical carbon dioxide. J Biotechnol 123 4 (2006) 504-515
10. 2 treatment. Biotechnol Bioeng 92 4 (2005) 447-451
11. 2. Biotechnol Bioeng 84 6 (2003) 627-638
12. Zhang J., Davis T.A., Matthews M.A., Drews M.J., LaBerge M., and An H.Y. Sterilization using high-pressure carbon dioxide. J Supercrit Fluids 38 3 (2006) 354-372
13. Garcia-Gonzalez L., Geeraerd A.H., Spilimbergo S., et al. High pressure carbon dioxide inactivation of microorganisms in foods: the past, the present and the future. Int J Food Microbiol 117 1 (2007) 1-28
14. Cars O., Högberg L.D., Murray M., et al. Meeting the challenge of antibiotic resistance. Br Med J 337 7673 (2008) 726-728
15. Watanabe T., Furukawa S., Kawarai T., Wachi M., Ogihara H., and Yamasaki M. Cytoplasmic acidification may occur in high-pressure carbon dioxide-treated Escherichia coli K12. Biosci Biotechnol Biochem 71 10 (2007) 2522-2526
16. Kim S.R., Rhee M.S., Kim B.C., and Kim K.H. Modeling the inactivation of Escherichia coli O157:H7 and generic Escherichia coli by supercritical carbon dioxide. Int J Food Microbiol 118 1 (2007) 52-61
17. 2 technology: microbial and enzyme inactivation, and effects on food quality. J Food Sci 71 1 (2006) R1-R11
18. Myasnikov A.G., Marzi S., Simonetti A., et al. Conformational transition of initiation factor 2 from the GTP- to GDP-bound state visualized on the ribosome. Nat Struct Mol Biol 12 12 (2005) 1145-1149
19. Laursen B.S., Sørensen H.P., Mortensen K.K., and Petersen H.S. Initiation of protein synthesis in bacteria. Microbiol Mol Biol Rev 69 1 (2005) 101-123
20. Simonetti A., Marzi S., Jenner L., et al. A structural view of translation initiation in bacteria. Cell Mol Life Sci 66 3 (2009) 423-436
21. Spurio R., Brandi L., Caserta E., et al. The C-terminal subdomain (IF2 C-2) contains the entire fMet-tRNA binding site of initiation factor IF2. J Biol Chem 275 4 (2000) 2447-2454
22. fMet binding site of initiation factor IF2. EMBO J 19 19 (2000) 5233-5240
23. Antoun A., Pavlov M.Y., Andersson K., Tenson T., and Ehrenberg M. The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis. EMBO J 22 20 (2003) 5593-5601
24. Allen G.S., Zavialov A.V., Gursky R., Ehrenberg M., and Frank J. The solution structure of a translation initiation complex from E. coli at 13.8 Å. Cell 121 5 (2005) 703-712
25. Kamat S., Critchley G., Beckman E.J., and Russell A.J. Biocatalytic synthesis of acrylates in organic solvents and supercritical fluids: 3. Does carbon dioxide covalently modify enzymes?. Biotechnol Bioeng 46 1 (1995) 610-620
26. Hitzler M.G., Smail F.R., Ross S.K., and Poliakoff M. Selective catalytic hydrogenation of organic compounds in supercritical fluids as a continuous process. Org Proc Res Dev 2 3 (1998) 137-146
27. Cameron D., Thompson J., March P.E., and Dahlberg A.E. Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome. J Mol Biol 319 1 (2002) 27-35
28. Brandi L., Marzi S., Fabretti A., et al. The translation initiation functions of IF2: targets for thiostrepton inhibition. J Mol Biol 335 4 (2004) 881-894
29. Dutka S., Meinnel T., Lazennec C., Mechulam Y., and Blanquet S. Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase. Nucl Acids Res 21 17 (1993) 4025-4030
30. fMet and fMet-AMP with the C-terminal domain of Thermus thermophilus translation initiation factor 2. Eur J Biochem 267 13 (2000) 4290-4299
31. Gross M., Lehle K., Jaenicke R., and Nierhaus K.H. Pressure-induced dissociation of ribosomes and elongation cycle intermediates. Stabilizing conditions and identification of the most sensitive functional state. Eur J Biochem 218 2 (1993) 463-468
32. Niven G.W., Miles C.A., and Mackey B.M. The effects of hydrostatic pressure on ribosome conformation in Escherichia coli: an in vivo study using differential scanning calorimetry. Microbiology 145 2 (1999) 419-425
33. Abe F. Exploration of the effects of high hydrostatic pressure on microbial growth, physiology and survival: perspectives from piezophysiology. Biosci Biotechnol Biochem 71 10 (2007) 2347-2357
34. 2 treatment. Innov Food Sci Emerg Technol 4 2 (2003) 161-165
35. Black E.P., Setlow P., Hocking A.D., et al. Response of spores to high-pressure processing. Comp Rev Food Sci Food Safety 6 4 (2007) 103-119
36. Steiner-Mosonyi M., Creuzenet C., Keates R.A.B., Strub B.R., and Mangroo D. The Pseudomonas aeruginosa initiation factor IF-2 is responsible for formylation-independent protein initiation in P. aeruginosa. J Biol Chem 279 50 (2004) 52262-52269
37. Fratte S.D., Piubelli C., and Domenici E. Development of a high-throughput scintillation proximity assay for the identification of C-domain translational initiation factor 2 inhibitors. J Biomol Screen 7 6 (2002) 541-546
38. Marintchev A., and Wagner G. Translation initiation: structures, mechanisms and evolution. Q Rev Biophys 37 3/4 (2004) 197-284
39. 2 at moderate temperatures. Biotechnol Bioeng 102 2 (2009) 569-576
40. Wu Y., Yao S.J., and Guan Y.X. Inactivation of microorganisms in carbon dioxide at elevated pressure and ambient temperature. Ind Eng Chem Res 46 19 (2007) 6345-6352
41. Marzi S., Knight W., Brandi L., et al. Ribosomal localization of translation initiation factor IF2. RNA 9 8 (2003) 958-969
42. Marshall R.A., Aitken C.E., Dorywalska M., and Puglisi J.D. Translation at the single-molecule level. Annu Rev Biochem 77 (2008) 177-203
43. Blanchard S.C. Single-molecule observations of ribosome function. Curr Opin Struct Biol 19 1 (2009) 103-109
44. Grigoriadou C., Marzi S., Kirillov S., Gualerzi C.O., and Cooperman B.S. A quantitative kinetic scheme for 70S translation initiation complex formation. J Mol Biol 373 3 (2007) 562-572
45. Marshall R.A., Aitken C.E., and Puglisi J.D. GTP hydrolysis by IF2 guides progression of the ribosome into elongation. Mol Cell 1 35 (2009) 37-47
46. Qin H., Grigoriadou C., and Cooperman B.S. Interaction of IF2 with the ribosomal GTPase-associated center during 70S initiation complex formation. Biochemistry 48 22 (2009) 4699-4706
47. Dorywalska M., Blanchard S.C., Gonzalez R.L., Kim H.D., Chu S., and Puglisi J.D. Site-specific labeling of the ribosome for single-molecule spectroscopy. Nucl Acids Res 33 1 (2005) 182-189
48. Simonetti A., Marzi S., Myasnikov A.G., et al. Structure of the 30S translation initiation complex. Nature 455 7211 (2008) 416-420
49. Harms J.M., Bartels H., Schlünzen F., and Yonath A. Antibiotics acting on the translational machinery. J Cell Sci 116 8 (2003) 1391-1393
50. Spahn C.M.T., and Prescott C.D. Throwing a spanner in the works: antibiotics and the translation apparatus. J Mol Med 74 8 (1996) 423-439
51. Brandi L., Fabbretti A., La Teana A., et al. Specific, efficient, and selective inhibition of prokaryotic translation initiation by a novel peptide antibiotic. Proc Natl Acad Sci 103 1 (2006) 39-44
52. (fMet) by aminoglycosides. Bioorg Med Chem Lett 13 6 (2003) 993-996