Microarray analysis of the transcriptome of the Escherichia coli (E. coli) regulated by cinnamaldehyde (CMA)

References

• Balaguer, M. P., Lopez-Carballo, G., Catala, R., Gavara, R., & Hernandez-Munoz, P. (2013). Antifungal properties of gliadin films incorporating cinnamaldehyde and application in active food packaging of bread and cheese spread foodstuffs. International Journal of Food Microbiology, 166(3), 369–377. doi:10.1016/j.ijfoodmicro.2013.08.012
   PubMed Web of Science ®Google Scholar
• Barker, C. S., & Samatey, F. A. (2012). Cross-complementation study of the flagellar type III export apparatus membrane protein FlhB. PLos ONE, 7(8), e44030. doi:10.1371/journal.pone.0044030
   Google Scholar
• Bearth, A., Cousin, M. E., & Siegrist, M. (2014). The consumer’s perception of artificial food additives: Influences on acceptance, risk and benefit perceptions. Food Quality and Preference, 38, 14–23. doi:10.1016/j.foodqual.2014.05.008
   Web of Science ®Google Scholar
• Calloni, G., Chen, T., Schermann, S. M., Chang, H., Genevaux, P., Agostini, F., … Hartl, F. U. (2012). DnaK functions as a central hub in the E. coli chaperone network. Cell Reports, 1(3), 251–264. doi:10.1016/j.celrep.2011.12.007
   PubMed Web of Science ®Google Scholar
• Carocho, M., Morales, P., & Ferreira, I. C. F. R. (2015). Natural food additives: Quo vadis? Trends in Food Science & Technology, 45(2), 284–295. doi:10.1016/j.tifs.2015.06.007
   Web of Science ®Google Scholar
• Chaban, B., Hughes, H. V., & Beeby, M. (2015). The flagellum in bacterial pathogens: For motility and a whole lot more. Seminars in Cell & Developmental Biology, 46, 91–103. doi:10.1016/j.semcdb.2015.10.032
   PubMed Web of Science ®Google Scholar
• Charbon, G., Wang, J., Brustad, E., Schultz, P. G., Horwich, A. L., Jacobs-Wagner, C., & Chapman, E. (2011). Localization of GroEL determined by in vivo incorporation of a fluorescent amino acid. Bioorganic & Medicinal Chemistry Letters, 21(20), 6067–6070. doi:10.1016/j.bmcl.2011.08.057
   PubMed Web of Science ®Google Scholar
• Chingaté, S., Delgado, G., Salaza, L. M., & Soto, C. Y. (2015). The ATPase activity of the mycobacterial plasma membrane is inhibited by the LL37-analogous peptide LLAP. Peptides, 71, 222–228. doi:10.1016/j.peptides.2015.07.021
   PubMed Web of Science ®Google Scholar
• Claret, L., & Hughes, C. (2002). Interaction of the atypical prokaryotic transcription activator FlhD2C2 with early promoters of the flagellar gene hierarchy. Journal of Molecular Biology, 321(2), 185–199. doi:10.1016/S0022-2836(02)00600-9
   PubMed Web of Science ®Google Scholar
• Denyer, S. P. (1990). Mechanisms of action of antibacterial biocides. International Biodeterioration & Biodegradation, 36(3), 227–245. doi:10.1016/0964-8305(96)00015-7
   Web of Science ®Google Scholar
• Ellis, R. J., & Hartl, F. U. (1996). Protein folding in the cell: Competing models of chaperonin function. Faseb Journal, 10, 20–26.
   PubMed Web of Science ®Google Scholar
• Feng, M., Yong, Q., Wang, W., Kuang, H., Wang, L., & Xu, C. (2013). Development of a monoclonal antibody-based ELISA to detect Escherichia coli O157:H7. Food and Agricultural Immunology, 24(4), 481–487. doi:10.1080/09540105.2012.716026
   Web of Science ®Google Scholar
• Goh, D. J. W., How, J. A., Lim, J. Z. R., Ng, W. C., Oon, J. S. H., Lee, K. C., … Ling, M. H. T. (2012). Gradual and step-wise halophilization enables Escherichia coli ATCC 8739 to adapt to 11% NaCl. Electronic Physician, 4(3), 527–535.
   Google Scholar
• Goñi, P., López, P., Sánchez, C., Gómez-Lusa, R., Becerrila, R., & Nerín, C. (2009). Antimicrobial activity in the vapour phase of a combination of cinnamon and clove essential oils. Food Chemistry, 116(4), 982–989. doi:10.1016/j.foodchem.2009.03.058
   Web of Science ®Google Scholar
• Gragerov, A., Nudler, E., Komissarova, N., Gaitanaris, G. A., Gottesman, M. E., & Nikiforov, V. (1992). Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 89, 10341–10344. doi: 10.1073/pnas.89.21.10341
   PubMed Web of Science ®Google Scholar
• Graubner, W., Schierhorn, A., & Bruser, T. (2006). DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone. Journal of Biological Chemistry, 282(10), 7116–7124. doi:10.1074/jbc.M608235200
   Web of Science ®Google Scholar
• Grigoroudis, A. I., McInnes, C., Premnathc, P. N., & Kontopidis, G. (2015). Efficient soluble expression of active recombinant human cyclin A2 mediated by E. coli molecular chaperones. Protein Expression and Purification, 113, 8–16. doi:10.1016/j.pep.2015.01.013
   PubMed Web of Science ®Google Scholar
• Grimshaw, J. P. A., Siegenthaler, R. K., Züger S., Schonfeld, H.- J., Z’graggen, B. R., & Christen, P. (2005). The heat-sensitive Escherichia coli grpE280 phenotype: Impaired interaction of GrpE(G122D) with DnaK. Journal of Molecular Biology, 353(4), 888–896. doi:10.1016/j.jmb.2005.08.069
   PubMed Web of Science ®Google Scholar
• Kim, J. S., Her, J. Y., & Lee, K. G. (2015). Formation and reduction of carcinogenic furan in various model systems containing food additives. Food Chemistry, 189, 108–113. doi:10.1016/j.foodchem.2014.10.128
   PubMed Web of Science ®Google Scholar
• Kong, D., Liu, L., Xing, C., Kuang, H., & Xu, C. (2015). Sensitive and highly specific detection of Cronobacter sakazakii based on monoclonal sandwich ELISA. Food and Agricultural Immunology, 26(4), 566–576. doi:10.1080/09540105.2014.998634
   Web of Science ®Google Scholar
• Lee, C. H., Oon, J. S. H., Lee, K. C., & Ling, M. H. T. (2012). Escherichia coli ATCC 8739 adapts to the presence of sodium chloride, monosodium glutamate, and benzoic acid after extended culture. ISRN Microbiology. doi:10.5402/2012/965356
   Google Scholar
• Minamino, T. (2014). Protein export through the bacterial flagellar type III export pathway. Biochimica et Biophysica Acta, 1843, 1642–1648. doi:10.1016/j.bbamcr.2013.09.005
   PubMed Web of Science ®Google Scholar
• Mizuno, S., Amida, H., Kobayashi, N., Aizawa, S., & Tate, S. (2011). The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar Type III secretion apparatus. Journal of Molecular Biology, 409(4), 558–573. doi:10.1016/j.jmb.2011.04.008
   PubMed Web of Science ®Google Scholar
• Moleyar, V., & Narasimham, P. (1992). Antibacterial activity of essential oil components. International Journal of Food Microbiology, 16(4), 337–342. doi: 10.1016/0168-1605(92)90035-2
   PubMed Web of Science ®Google Scholar
• National Committee for Clinical Laboratory Standards (NCCLS). (1997). Reference method for broth dilution antifungal susceptibility testing of yeasts. Proposed standard M27-A. National Committee for Clinical Laboratory Standards, Villanova.
   Google Scholar
• Pallen, M. J., Penn, C. W., & Chaudhuri, R. R. (2005). Bacterial flagellar diversity in the post-genomic era. Trends in Microbiology, 13(4), 143–149. doi:10.1016/j.tim.2005.02.008
   PubMed Web of Science ®Google Scholar
• Sajó, R., Liliom, K., Muskotál, A., Klein, Á., Závodszky, P., Vonderviszt, F., & Dobó, J. (2014). Soluble components of the flagellar export apparatus, FliI, FliJ, and FliH, do not deliver flagellin, the major filament protein, from the cytosol to the export gate. Biochimca et Biophysica Acta, 1843, 2414–2423. doi:10.1016/j.bbamcr.2014.07.004
   PubMed Web of Science ®Google Scholar
• Seong, I. S., Oh, J. Y., Leea, J. W., Tanaka, K., & Chung, C. H. (2000). The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli. FEBS Letters, 477, 224–229. doi:10.1016/S0014-5793(00)01808-1
   PubMed Web of Science ®Google Scholar
• Shen, S., Zhang, T., Yuan, Y., Lin, S., Xu, J., & Ye, H. (2015). Effects of cinnamaldehyde on Escherichia coli and Staphylococcus aureus membrane. Food Control, 47, 196–202. doi:10.1016/j.foodcont.2014.07.003
   Web of Science ®Google Scholar
• Shin, D. H., Yoo, S. J., Shim, Y. K., Seol, J. H., Kang, M., & Chung, C. H. (1996). Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli. FEBS Letters, 398, 151–154. doi:10.1016/S0014-5793(96)01223-9
   PubMed Web of Science ®Google Scholar
• Sun-Wada, G. H., & Wada, Y. (2015). Role of vacuolar-type proton ATPase in signal transduction. Biochimca et Biophysica Acta, 1847(10), 1166–1172. doi:10.1016/j.bbabio.2015.06.010
   PubMed Web of Science ®Google Scholar
• Svennerholm, A. M., & Steele, D. (2004). Progress in enteric vaccine development. Best Practice Research Clinical Gastroenterology, 18(2), 421–445. doi:10.1053/ybega.2004.451
   PubMed Web of Science ®Google Scholar
• Terashima, H., Kojima, S., & Homma, M. (2008). Chapter 2 flagellar motility in bacteria: Structure and function of flagellar motor. International Review of Cell and Molecular Biology, 270, 39–85. doi:10.1016/S1937-6448(08)01402-0
   PubMed Web of Science ®Google Scholar
• Thissen, J. B., McLoughlin, K., Gardner, S., Gu, P., Mabery, S., Slezak, T., & Jaing, C. (2014). Analysis of sensitivity and rapid hybridization of a multiplexed microbial detection microarray. Journal of Virological Methods, 201, 73–78. doi:10.1016/j.jviromet.2014.01.024
   PubMed Web of Science ®Google Scholar
• Walker, R. I. (2005). Considerations for development of whole cell bacterial vaccines to prevent diarrheal diseases in children in developing countries. Vaccine, 23(26), 3369–3385. doi:10.1016/j.vaccine.2004.12.029
   PubMed Web of Science ®Google Scholar
• Walker, R. I., Steele, D., & Aguado, T. (2007). Analysis of strategies to successfully vaccinate infants in developing countries against enterotoxigenic E. coli (ETEC) disease. Vaccine, 25(14), 2545–2566. doi:10.1016/j.vaccine.2006.12.028
   PubMed Web of Science ®Google Scholar
• Wang, W., Feng, M., Kong, D., Liu, L., Song, S., & Xu, C. (2015). Development of an immunochromatographic strip for the rapid detection of Pseudomonas syringae pv. maculicola in broccoli and radish seeds. Food and Agricultural Immunology, 26(5), 738–745. doi:10.1080/09540105.2015.1023266
   Web of Science ®Google Scholar
• Wang, J., Song, J. J., Seong, I. S., Franklin, M. C., Kamtekar, S., Eom, S. H., & Chung, C. H. (2001). Nucleotide-dependent conformational changes in a protease-associated ATPase HslU. Structure, 9(11), 1107–1116. doi:10.1016/S0969-2126(01)00670-0
   PubMed Web of Science ®Google Scholar
• Weber-Sparenberg, C., Pöplau, P., Brookman, H., Rochón, M., Möckel, C., Nietschke, M., & Jung, H. (2006). Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli. Archives of Microbiology, 186(4), 307–316. doi:10.1007/s00203-006-0146-0
   PubMed Web of Science ®Google Scholar
• Ye, H., Liu, Z., Guo, A., Liang, J., Guo, N., Zeng, F., … Yu, L. (2011). Global transcriptional profiles of Mycobacterium tuberculosis treated with plumbagin. World Journal of Microbiology and Biotechnology, 27, 2261–2269. doi:10.1007/s11274-011-0689-3
   Web of Science ®Google Scholar
• Yu, L., Guo, N., Yang, Y., Wu, X., Meng, R., Fan, J., … Deng, X. (2010). Microarray analysis of p-anisaldehyde-induced transcriptome of Saccharomyces cerevisiae. Journal of Industrial Microbiology & Biotechnology, 37, 313–322. doi:10.1007/s10295-009-0676-y
   PubMed Web of Science ®Google Scholar
• Zmijewski, M. A., Macario, A. J. L., & Lipinska, B. (2004). Functional similarities and differences of an archaeal Hsp70(DnaK) stress protein compared with its homologue from the bacterium Escherichia coli. Journal of Molecular Biology, 336(2), 539–549. doi:10.1016/j.jmb.2003.12.053
   PubMed Web of Science ®Google Scholar