Expression of recombinant Arabian camel lactoferricin-related peptide in Pichia pastoris and its antimicrobial identification

被引:19
作者
Chahardooli, Mahmood [1 ]
Niazi, Ali [2 ]
Aram, Farzaneh [1 ]
Sohrabi, Seyyed Mohsen [1 ]
机构
[1] Shiraz Univ, Inst Biotechnol, Shiraz, Iran
[2] Shiraz Univ, Coll Agr, Ctr Biotechnol, Shiraz, Iran
关键词
camel lactoferricin; antimicrobial activity; Pichia pastoris; thermal stability; N-TERMINAL REGION; BOVINE LACTOFERRIN; MECHANISM; ANTITUMOR; PROTEINS; INHIBIT;
D O I
10.1002/jsfa.7125
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
BACKGROUNDLactoferricin (LFcin) is a strong cationic peptide released from the N-terminus of lactoferrin by gastric pepsin digestion. LFcin has some important properties, including high antimicrobial activity. To date, lactoferricins have been isolated and characterised from various animal species, but not from camel. The aim of this study was to characterise and express recombinant camel lactoferricin (LFcinC) in Pichia pastoris and investigate its antimicrobial activity. RESULTSAfter methanol induction, LFcinC was expressed and secreted into a culture broth medium and the results determined by concentrated supernatant culture medium showed high antimicrobial activity against the following microorganisms: Escherichia coliPTCC 1330 (ATCC 8739), Staphylococcus aureusPTCC 1112 (ATCC 6538), Pseudomonas aeruginosaPTCC 1074 (ATCC 9027), Bacillus subtilisPTCC 1023 (ATCC 6633), and Candida albicansPTCC 5027 (ATCC 10231). Thermal stability was clarified with antibacterial activity against Escherichia coliPTCC 1330 (ATCC 8739). CONCLUSIONResults confirmed that camel lactoferricin had suitable antimicrobial activity and its production by Pichia pastoris can be used for recombinant production. (c) 2015 Society of Chemical Industry
引用
收藏
页码:569 / 575
页数:7
相关论文
共 39 条
  • [1] Al-Dughaym A. M., 2008, Scientific Journal of King Faisal University (Basic and Applied Sciences), V9, P119
  • [2] Al-Majali AM, 2007, INT J APPL RES VET M, V5, P120
  • [3] Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface
    Andersen, JH
    Jenssen, H
    Sandvik, K
    Gutteberg, TJ
    [J]. JOURNAL OF MEDICAL VIROLOGY, 2004, 74 (02) : 262 - 271
  • [4] Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts
    Andersen, JH
    Osbakk, SA
    Vorland, LH
    Traavik, T
    Gutteberg, TJ
    [J]. ANTIVIRAL RESEARCH, 2001, 51 (02) : 141 - 149
  • [5] BACTERICIDAL EFFECT FOR HUMAN LACTOFERRIN
    ARNOLD, RR
    COLE, MF
    MCGHEE, JR
    [J]. SCIENCE, 1977, 197 (4300) : 263 - 265
  • [6] Dealing with iron: Common structural principles in proteins that transport iron and heme
    Baker, HM
    Anderson, BF
    Baker, EN
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (07) : 3579 - 3583
  • [7] ANTIFUNGAL PROPERTIES OF LACTOFERRICIN-B, A PEPTIDE DERIVED FROM THE N-TERMINAL REGION OF BOVINE LACTOFERRIN
    BELLAMY, W
    YAMAUCHI, K
    WAKABAYASHI, H
    TAKASE, M
    TAKAKURA, N
    SHIMAMURA, S
    TOMITA, M
    [J]. LETTERS IN APPLIED MICROBIOLOGY, 1994, 18 (04) : 230 - 233
  • [8] ANTIBACTERIAL SPECTRUM OF LACTOFERRICIN-B, A POTENT BACTERICIDAL PEPTIDE DERIVED FROM THE N-TERMINAL REGION OF BOVINE LACTOFERRIN
    BELLAMY, W
    TAKASE, M
    WAKABAYASHI, H
    KAWASE, K
    TOMITA, M
    [J]. JOURNAL OF APPLIED BACTERIOLOGY, 1992, 73 (06): : 472 - 479
  • [9] IDENTIFICATION OF THE BACTERICIDAL DOMAIN OF LACTOFERRIN
    BELLAMY, W
    TAKASE, M
    YAMAUCHI, K
    WAKABAYASHI, H
    KAWASE, K
    TOMITA, M
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1121 (1-2) : 130 - 136
  • [10] Blondelle SE, 1996, METHOD MOL CELL BIOL, V6, P8