Enhanced Expression and Functional Characterization of the Recombinant Putative Lysozyme-PMAP36 Fusion Protein |
Rao, Zhili
(Division of Biotechnology, College of Environmental & Bioresources Sciences, Chonbuk National University)
Kim, So Young (Division of Biotechnology, College of Environmental & Bioresources Sciences, Chonbuk National University) Akanda, Md Rashedunnabi (College of Veterinary Medicine and Bio-safety Research Institute, Chonbuk National University) Lee, Su Jin (Department of Immunology, Laboratory of Dendritic Cell Differentiation and Regulation, School of Medicine, Konkuk University) Jung, In Duk (Department of Immunology, Laboratory of Dendritic Cell Differentiation and Regulation, School of Medicine, Konkuk University) Park, Byung-Yong (College of Veterinary Medicine and Bio-safety Research Institute, Chonbuk National University) Kamala-Kannan, Seralathan (Division of Biotechnology, College of Environmental & Bioresources Sciences, Chonbuk National University) Hur, Jin (Veterinary Public Health, College of Veterinary Medicine, Chonbuk National University) Park, Jung Hee (Division of Biotechnology, College of Environmental & Bioresources Sciences, Chonbuk National University) |
1 | Takahashi, D., Shukla, S.K., Prakash, O., and Zhang, G. (2010). Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity. Biochimie 92, 1236-1241. DOI |
2 | Tang, Y.Q., Yuan, J., Osapay, G., Osapay, K., Tran, D., Miller, C.J., Ouellette, A.J., and Selsted, M.E. (1999). A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 286, 498-502. DOI |
3 | Teixeira, V., Feio, M.J., and Bastos, M. (2012). Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res. 51, 149-177. DOI |
4 | van Kan, E.J., Demel, R.A., van der Bent, A., and de Kruijff, B. (2003). The role of the abundant phenylalanines in the mode of action of the antimicrobial peptide clavanin. Biochim. Biophys. Acta 1615, 84-92. DOI |
5 | Wang, G., Li, X., and Wang, Z. (2016). APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res. 44, D1087-1093. DOI |
6 | Yeaman, M.R., and Yount, N.Y. (2003). Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55, 27-55. DOI |
7 | Yeung, A.T., Gellatly, S.L., and Hancock, R.E. (2011). Multifunctional cationic host defence peptides and their clinical applications. Cell Mol. Life Sci. 68, 2161-2176. DOI |
8 | Zasloff, M. (2002). Antimicrobial peptides of multicellular organisms. Nature 415, 389-395. DOI |
9 | Zheng, L., McQuaw, C.M., Ewing, A.G., and Winograd, N. (2007). Sphingomyelin/phosphatidylcholine and cholesterol interactions studied by imaging mass spectrometry. J. Am. Chem. Soc. 129, 15730-15731. DOI |
10 | Bahnsen, J.S., Franzyk, H., Sayers, E.J., Jones, A.T., and Nielsen, H.M. (2015). Cell-penetrating antimicrobial peptides-prospectives for targeting intracellular infections. Pharm. Res. 32, 1546-1556. DOI |
11 | Bulet, P., Dimarcq, J.L., Hetru, C., Lagueux, M., Charlet, M., Hegy, G., Van Dorsselaer, A., and Hoffmann, J.A. (1993). A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J. Biol. Chem. 268, 14893-14897. DOI |
12 | Ding, R., Lin, C., Wei, S., Zhang, N., Tang, L., Lin, Y., Chen, Z., Xie, T., Chen, X., Feng, Y., et al. (2017). Therapeutic benefits of mesenchymal stromal cells in a rat model of hemoglobin-induced hypertensive intracerebral hemorrhage. Mol. Cells 40, 133-142. DOI |
13 | Hancock, R.E., and Sahl, H.G. (2006). Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24, 1551-1557. DOI |
14 | Huang, Y., Huang, J., and Chen, Y. (2010). Alpha-helical cationic antimicrobial peptides: relationships of structure and function. Protein Cell 1, 143-152. DOI |
15 | Ingham, A.B., and Moore, R.J. (2007). Recombinant production of antimicrobial peptides in heterologous microbial systems. Biotechnol. Appl. Biochem. 47, 1-9. DOI |
16 | Jacoby, T.S., Kuchenbecker, R.S., Dos Santos, R.P., Magedanz, L., Guzatto, P., and Moreira, L.B. (2010). Impact of hospital-wide infection rate, invasive procedures use and antimicrobial consumption on bacterial resistance inside an intensive care unit. J. Hospital Infect. 75, 23-27. DOI |
17 | Li, Y., Xiang, Q., Zhang, Q., Huang, Y., and Su, Z. (2012). Overview on the recent study of antimicrobial peptides: origins, functions, relative mechanisms and application. Peptides 37, 207-215. DOI |
18 | Lv, Y., Wang, J., Gao, H., Wang, Z., Dong, N., Ma, Q., and Shan, A. (2014). Antimicrobial properties and membrane-active mechanism of a potential alpha-helical antimicrobial derived from cathelicidin PMAP-36. PLoS One 9, e86364. DOI |
19 | Lyu, Y., Yang, Y., Lyu, X., Dong, N., and Shan, A. (2016). Antimicrobial activity, improved cell selectivity and mode of action of short PMAP-36-derived peptides against bacteria and Candida. Scientific Reports 6, 27258. DOI |
20 | Mai, X.T., Huang, J., Tan, J., Huang, Y., and Chen, Y. (2015). Effects and mechanisms of the secondary structure on the antimicrobial activity and specificity of antimicrobial peptides. J. Pept. Sci. 21, 561-568. DOI |
21 | Miki, T., and Hardt, W.D. (2013). Outer membrane permeabilization is an essential step in the killing of gram-negative bacteria by the lectin RegIIIbeta. PLoS One 8, e69901. DOI |
22 | Pedulla, M.L., Ford, M.E., Karthikeyan, T., Houtz, J.M., Hendrix, R.W., Hatfull, G.F., Poteete, A.R., Gilcrease, E.B., Winn-Stapley, D.A., and Casjens, S.R. (2003). Corrected sequence of the bacteriophage p22 genome. J. Bacteriol. 185, 1475-1477. DOI |
23 | Rennell, D., and Poteete, A.R. (1989). Genetic analysis of bacteriophage P22 lysozyme structure. Genetics 123, 431-440. DOI |
24 | Scocchi, M., Zelezetsky, I., Benincasa, M., Gennaro, R., Mazzoli, A., and Tossi, A. (2005). Structural aspects and biological properties of the cathelicidin PMAP-36. FEBS J. 272, 4398-4406. DOI |
25 | Storici, P., Scocchi, M., Tossi, A., Gennaro, R., and Zanetti, M. (1994). Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA. FEBS Lett. 337, 303-307. DOI |
26 | Subbalakshmi, C., Bikshapathy, E., Sitaram, N., and Nagaraj, R. (2000). Antibacterial and hemolytic activities of single tryptophan analogs of indolicidin. Biochem. Biophys. Res. Commun. 274, 714-716. DOI |
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