Isaac Scientific Publishing

Advances in Food Science and Engineering

Effect of Loop Structure of Bovine Lactoferricin on Escherichia Coli

Download PDF (447.2 KB) PP. 110 - 114 Pub. Date: December 1, 2018

DOI: 10.22606/afse.2018.24002

Author(s)

  • Rui Xu*
    College of Food Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, 066004, China
  • Xi-yan Zhao
    College of Food Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, 066004, China
  • Shuo Guo
    College of Food Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, 066004, China
  • Qi Yang
    College of Food Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, 066004, China

Abstract

As a glycoprotein, lactoferrin has many biological actions, among which the antibacterial activity is one of the most important effects studied. Bovine lactoferricin (Lfcin B) is a cationic peptide that possesses potent in vitro and in vivo antibacterial activity, and might affect the expression of DNA Adenine Methyltransferase (DAM). In the present study, the artificially synthesized Lfcin B and Lfcin B derived peptide (Cys 19 residue in Lfcin B was replaced by Ala) were added in Escherichia coli, and we determined the messenger ribonucleic acid and protein expression of DAM in Escherichia coli after incubated with Lfcin B by real-time quantitative reverse transcription PCR and Western blot analysis. The results of real–time quantitative reverse transcription PCR showed that DAM expression was reduced after treatment with Lfcin B. The results of western blot analysis showed that the expression of DAM protein was down-modulated by Lfcin B.

Keywords

Lactoferrin, DNA Adenine Methyltransferase, western blot, Escherichia coli

References

[1] F. F. Han, Y. H. Gao, C. Luan. “Comparing bacterial membrane interactions and antimicrobial activity of porcine lactoferricin-derived peptides,” Journal of Dairy Science, Vol. 96, no. 6, pp. 3471-3487, 2013.

[2] W. Bellamy, M. Takase, H. Wakabayashi, K. Kawase and M. Tomita. “Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin,” Journal of Applied Bacteriology, Vol. 73, no. 1, pp. 472-479, 1992.

[3] Y. Omata, M. Satake, R. Maeda, A. Saito, K. Shimazaki, K. Yamauchi, Y. Uzuka, S. Tanabe, T. Sarashina, T. Mikami. “Reduction of the infectivity of Toxoplasma gondii and Eimeria stiedai sporozoites by treatment with bovine lactoferricin,” Journal of Veterinary Medical Science, Vol. 63, no. 2, pp. 187–190, 2001.

[4] J. H. Andersen, H. Jenssen, T. J. Gutteberg. “Lactoferrin and lactoferricin inhibit herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir,” Antiviral Research, Vol. 58, no. 4, pp. 209–215, 2003.

[5] A. Shestakov, H. Jenssen, I. Nordstr?m. “Lactoferricin but not lactoferrin inhibit herpes simplex virus type 2 infection in mice,” Antiviral Research, Vol. 93, no. 3, pp. 340-345, 2012.

[6] H. Jenssen, J. H. Andersen, L. Uhlin-Hansen, T. J. Gutteberg, ?. Rekdal. “Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparansulfate,” Antiviral Research, Vol. 61, pp. 101–109, 2004.

[7] M. Balouiri, M. Sadiki, S. K. Ibnsouda. “Methods for in vitro evaluating antimicrobial activity,” Journal of Pharmaceutical Analysis, Vol. 6, no. 2, pp. 71-79, 2016.

[8] S. Poojariab, O. J. Alabi. “Green-based real-time quantitative reverse-transcription PCR for detection and discrimination of grapevine viruses,” Journal of Virological Methods, Vol. 235, no. 2, pp. 112-118, 2016.

[9] J. L. Kenneth and D. S. Thomas. “Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the TΔΔC2? Method,” Methods, Vol. 25, no. 1, pp. 402-408, 2001.

[10] N. Bruni, M. T. Capucchio, E. Biasibetti. “Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine,” Molecules, Vol. 21, no. 6, pp. 752-755, 2016.

[11] E. Yazidi-Belkoura, D. Legrand, J. Nuijens. “The binding of lactoferrin to glycosaminoglycans on enterocyte-like HT29-18-C1 cells is mediated through basic residues located in the N-terminus,” Biochimica et Biophysica Acta, Vol. 1568, no. 3, pp. 197-204, 2001.

[12] J. S. Mader, A. Richardson, J. Salsman, D. Top, R. Antueno, R. Duncan and D. W. Hoskin. “Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria,” Experimental Cell Research, Vol. 313, no. 1, pp. 2634-2650, 2007.

[13] S. Furlong, N. Ridgway, D. W. Hoskin. “Modulation of ceramide metabolism in T-leukemia cell lines potentiates apoptosis induced by the cationic antimicrobial peptide bovine lactoferricin,” International Journal of Oncology, Vol. 32, no. 1, pp. 537-544, 2008.