Identification of a new lactoferrin-derived peptide isolated from camel milk with potential antimicrobial activity
Subject Areas : microbiology
Elnaz
Khajeh
1
(Graduate of Master of Microbiology, Faculty of Basic Sciences, Department of Biology,
Sabzevar Branch, Islamic Azad University, Sabzevar, Iran)
Majid
Jamshidian Mojaver
2
(Assistant Professor,Mashhad Branch, Razi Vaccine and Serum Research Institute, Agricultural
Research, Education and Extension Organization (AREEO), Mashhad, Iran)
Mohsen
Naeemipour
3
(Assistant Professor,Cellular and Molecular Research Center, Sabzevar University of Medical Sciences, Sabzevar,
Iran.)
Hamidreza
Farzin
4
(Assistant Professor, Mashhad Branch, Razi Vaccine and Serum Research Institute, Agricultural
Research, Education and Extension Organization (AREEO), Mashhad, Iran)
Keywords: lactoferrin, Camel milk, Trypsin, Antibacterial peptide,
Abstract :
Introduction: The increasing microbial resistance to existing antibiotics has increased the interest in novel antimicrobial compounds. Antimicrobial peptides (AMPs) represent an attractive alternative to classical antibiotics.Milk contains a lot of proteins, some of which have received a lot of attention, such as lactoferrin, which has antibacterial activity. The aim of this study was to investigate the antibacterial activity of a lactoferrin-derived peptide isolated from camel milk against Staphylococcus aureus, Streptococcus pyogenes, Pseudomonas aeruginosa and, Acinetobacter baumannii. Materials and methods: In the present study, antibacterial peptides in milk lactoferrin were identified using bioinformatics tools. Trypsin I peptide was synthesized. Then, the toxicity of the peptide on the cell line was investigated by the MTT method. The antibacterial properties of trypsin I was evaluated on four pathogenic bacteria, Staphylococcus aureus, Pseudomonas aeruginosa, Acinetobacter baumannii and, Streptococcus pyogenes. Results: The results showed that the peptides had no lethal effect on the cell line tested. The MIC results of trypsin peptide for Staphylococcus aureus, Pseudomonas aeruginosa, Acinetobacter baumannii and, Streptococcus pyogenes were 7.81, 15.62, 125 and 250, respectively. Conclusion: Antimicrobial peptides have received much attention in recent decades due to their appropriate properties and characteristics such as rapid lethality, a wide range of activity and, also the rare development of cases of drug resistance. According to the observed results of this study, the antibacterial properties of the compounds isolated from this study can be a good alternative to replacement with common antibiotics.
Playne MJ, Bennett LE, Smithers GW. Functional dairy foods and ingredients. Australian Journal of Dairy Technology. 2003; 58(3): 242-64.
Miller GD, Jarvis JK & McBean LD. Handbook of dairy foods and nutrition. CRC press; 2006: 15.
Legrand D & Mazurier J. A critical review of the roles of host lactoferrin in immunity. Biometals. 2010; 23(3): 365-76.
Feng X, Liu C, Guo J, Bi C, Cheng B, Li Z, Shan A & Li Z. Expression and purification of an antimicrobial peptide, bovine lactoferricin derivative LfcinB-W10 in Escherichia coli. Current microbiology. 2010; 60(3): 179-84.
Metz‐Boutigue MH, Jollés J, Mazurier J, Schoentgen F, Legrand D, Spik G, Montreuil J & Jollès P. Human lactotransferrin: Amino acid sequence and structural comparisons with other transferrins. European Journal of Biochemistry. 1984; 145(3): 659-76.
Baker EN. Structure and reactivity of transferrins. Advances in inorganic chemistry. 1994; 41: 389-464.
Yen CC, Shen CJ, Hsu WH, Chang YH, Lin HT, Chen HL & Chen CM. Lactoferrin: An iron-binding antimicrobial protein against Escherichia coli infection. Biometals. 2011; 24(4): 585-94.
Expósito IL & Recio I. Antibacterial activity of peptides and folding variants from milk proteins. International Dairy Journal. 2006; 16(11): 1294-305.
Arnold RR, Brewer M & Gauthier JJ. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infection and immunity. 1980; 28(3): 893-8.
Drago-Serrano ME, De La Garza-Amaya M, Luna JS & Campos-Rodríguez R. Lactoferrin-lipopolysaccharide (LPS) binding as key to antibacterial and antiendotoxic effects. International immunopharmacology. 2012; 12(1): 1-9.
Baker EN, Baker HM & Kidd RD. Lactoferrin and transferrin: functional variations on a common structural framework. Biochemistry and Cell Biology. 2002; 80(1): 27-34.
Kim WS, Shimazaki KI & Tamura T. Expression of bovine lactoferrin C-lobe in Rhodococcus erythropolis and its purification and characterization. Bioscience, biotechnology, and biochemistry. 2006; 70(11): 2641-5.
Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. Journal of immunological methods. 1983; 65 (1-2): 55-63.
Frija LM, Ntungwe E, Sitarek P, Andrade JM, Toma M, Śliwiński T, Cabral LS, Cristiano ML, Rijo P & Pombeiro AJ. In Vitro Assessment of Antimicrobial, Antioxidant, and Cytotoxic Properties of Saccharin-Tetrazolyl and-Thiadiazolyl Derivatives: The Simple Dependence of the pH Value on Antimicrobial Activity. Pharmaceuticals. 2019; 12(4): 167.
Kadoughani Sani S, Jamshidian-Mojaver M, Farzin H & Amiri M. Investigation of the effect of fungal and copper nanocomplexes on bacte-ria causing nosocomial infections. New Findings in Veterinary Microbiology. 2020; 3(1): 39-46.
Wallmann J, Böttner A, Goossens L, Hafez HM, Hartmann K, Kaspar H, Kehrenberg C, Kietzmann M, Klarmann D, Klein G & Krabisch P. Results of an interlaboratory test on antimicrobial susceptibility testing of bacteria from animals by broth microdilution. International journal of antimicrobial agents. 2006; 27(6): 482-90.
Balouiri M, Sadiki M & Ibnsouda SK. Methods for in vitro evaluating antimicrobial activity: A review. Journal of pharmaceutical analysis. 2016; 6(2): 71-9.
Ciccaglione AF, Di Giulio M, Di Lodovico S, Di Campli E, Cellini L & Marzio L. Bovine lactoferrin enhances the efficacy of levofloxacin-based triple therapy as first-line treatment of Helicobacter pylori infection: an in vitro and in vivo study. Journal of Antimicrobial Chemotherapy. 2019; 74(4): 1069-77.
Keil B. Proteolysis Data Bank: Specificity of alpha-chymotrypsin from computation of protein cleavages. Protein sequences & data analysis. 1987; 1(1): 13.
Gasteiger E, Hoogland C, Gattiker A, Wilkins MR, Appel RD & Bairoch A. Protein identification and analysis tools on the ExPASy server. In The proteomics protocols handbook. 2005; 74(4): 65-77.
De Gobba C, Espejo-Carpio FJ, Skibsted LH & Otte J. Antioxidant peptides from goat milk protein fractions hydrolysed by two commercial proteases. International Dairy Journal. 2014; 39(1): 28-40.
Sharbafi R, Moradian F, Rafiei AR. Evaluation of Antimicrobial Activity of Lactoferrin against P. Aeruginosa and E. Coli Growth. Journal of Babol University of Medical Sciences. 2016; 18(7): 19-23.
Taheri A, Farvin KS, Jacobsen C & Baron CP. Antioxidant activities and functional properties of protein and peptide fractions isolated from salted herring brine. Food chemistry. 2014; 142: 318-26.
Habibi Najafi MB, Tanhaeiyan A, Rahnama P & Azghandi M. Study on antibacterial activity and cytotoxicity of recombinant peptide, Lasioglossin ɪɪɪ, against foodborne pathogens. Agricultural Biotechnology Journal. 2018; 10(3): 31-44.
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Playne MJ, Bennett LE, Smithers GW. Functional dairy foods and ingredients. Australian Journal of Dairy Technology. 2003; 58(3): 242-64.
Miller GD, Jarvis JK & McBean LD. Handbook of dairy foods and nutrition. CRC press; 2006: 15.
Legrand D & Mazurier J. A critical review of the roles of host lactoferrin in immunity. Biometals. 2010; 23(3): 365-76.
Feng X, Liu C, Guo J, Bi C, Cheng B, Li Z, Shan A & Li Z. Expression and purification of an antimicrobial peptide, bovine lactoferricin derivative LfcinB-W10 in Escherichia coli. Current microbiology. 2010; 60(3): 179-84.
Metz‐Boutigue MH, Jollés J, Mazurier J, Schoentgen F, Legrand D, Spik G, Montreuil J & Jollès P. Human lactotransferrin: Amino acid sequence and structural comparisons with other transferrins. European Journal of Biochemistry. 1984; 145(3): 659-76.
Baker EN. Structure and reactivity of transferrins. Advances in inorganic chemistry. 1994; 41: 389-464.
Yen CC, Shen CJ, Hsu WH, Chang YH, Lin HT, Chen HL & Chen CM. Lactoferrin: An iron-binding antimicrobial protein against Escherichia coli infection. Biometals. 2011; 24(4): 585-94.
Expósito IL & Recio I. Antibacterial activity of peptides and folding variants from milk proteins. International Dairy Journal. 2006; 16(11): 1294-305.
Arnold RR, Brewer M & Gauthier JJ. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infection and immunity. 1980; 28(3): 893-8.
Drago-Serrano ME, De La Garza-Amaya M, Luna JS & Campos-Rodríguez R. Lactoferrin-lipopolysaccharide (LPS) binding as key to antibacterial and antiendotoxic effects. International immunopharmacology. 2012; 12(1): 1-9.
Baker EN, Baker HM & Kidd RD. Lactoferrin and transferrin: functional variations on a common structural framework. Biochemistry and Cell Biology. 2002; 80(1): 27-34.
Kim WS, Shimazaki KI & Tamura T. Expression of bovine lactoferrin C-lobe in Rhodococcus erythropolis and its purification and characterization. Bioscience, biotechnology, and biochemistry. 2006; 70(11): 2641-5.
Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. Journal of immunological methods. 1983; 65 (1-2): 55-63.
Frija LM, Ntungwe E, Sitarek P, Andrade JM, Toma M, Śliwiński T, Cabral LS, Cristiano ML, Rijo P & Pombeiro AJ. In Vitro Assessment of Antimicrobial, Antioxidant, and Cytotoxic Properties of Saccharin-Tetrazolyl and-Thiadiazolyl Derivatives: The Simple Dependence of the pH Value on Antimicrobial Activity. Pharmaceuticals. 2019; 12(4): 167.
Kadoughani Sani S, Jamshidian-Mojaver M, Farzin H & Amiri M. Investigation of the effect of fungal and copper nanocomplexes on bacte-ria causing nosocomial infections. New Findings in Veterinary Microbiology. 2020; 3(1): 39-46.
Wallmann J, Böttner A, Goossens L, Hafez HM, Hartmann K, Kaspar H, Kehrenberg C, Kietzmann M, Klarmann D, Klein G & Krabisch P. Results of an interlaboratory test on antimicrobial susceptibility testing of bacteria from animals by broth microdilution. International journal of antimicrobial agents. 2006; 27(6): 482-90.
Balouiri M, Sadiki M & Ibnsouda SK. Methods for in vitro evaluating antimicrobial activity: A review. Journal of pharmaceutical analysis. 2016; 6(2): 71-9.
Ciccaglione AF, Di Giulio M, Di Lodovico S, Di Campli E, Cellini L & Marzio L. Bovine lactoferrin enhances the efficacy of levofloxacin-based triple therapy as first-line treatment of Helicobacter pylori infection: an in vitro and in vivo study. Journal of Antimicrobial Chemotherapy. 2019; 74(4): 1069-77.
Keil B. Proteolysis Data Bank: Specificity of alpha-chymotrypsin from computation of protein cleavages. Protein sequences & data analysis. 1987; 1(1): 13.
Gasteiger E, Hoogland C, Gattiker A, Wilkins MR, Appel RD & Bairoch A. Protein identification and analysis tools on the ExPASy server. In The proteomics protocols handbook. 2005; 74(4): 65-77.
De Gobba C, Espejo-Carpio FJ, Skibsted LH & Otte J. Antioxidant peptides from goat milk protein fractions hydrolysed by two commercial proteases. International Dairy Journal. 2014; 39(1): 28-40.
Sharbafi R, Moradian F, Rafiei AR. Evaluation of Antimicrobial Activity of Lactoferrin against P. Aeruginosa and E. Coli Growth. Journal of Babol University of Medical Sciences. 2016; 18(7): 19-23.
Taheri A, Farvin KS, Jacobsen C & Baron CP. Antioxidant activities and functional properties of protein and peptide fractions isolated from salted herring brine. Food chemistry. 2014; 142: 318-26.
Habibi Najafi MB, Tanhaeiyan A, Rahnama P & Azghandi M. Study on antibacterial activity and cytotoxicity of recombinant peptide, Lasioglossin ɪɪɪ, against foodborne pathogens. Agricultural Biotechnology Journal. 2018; 10(3): 31-44.