An antimicrobial peptide is produced by extracellular processing of a protein from Propionibacterium jensenii

被引:30
作者
Faye, T
Brede, DA
Langsrud, T
Nes, IF
Holo, H
机构
[1] Agr Univ Norway, Lab Microbial Gene Technol, Dept Chem & Biochem, N-1432 As, Norway
[2] Agr Univ Norway, Dept Food Sci, N-1432 As, Norway
[3] Norwegian Dairies Assoc, Oslo, Norway
关键词
D O I
10.1128/JB.184.13.3649-3656.2002
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A protease-activated antimicrobial peptide (PAMP) and its inactive precursor were purified from the culture supernatant of Propionibacterium jensenii LMG 3032 and characterized at the molecular level. PAMP is a 64-amino-acid cationic peptide of 6,383 Da with physicochemical features similar to those of bacteriocins from gram-positive bacteria. This peptide displayed bactericidal activity against several propionibacteria and lactobacilli. DNA sequencing indicated that the PAMP-encoding gene (pamA) is translated as a proprotein of 198 amino acids with an N-terminal signal peptide of 27 amino acids and that PAMP constitutes the C-terminal part of this precursor. The amino acid sequence of pro-PAMP showed no similarity to those of other known proteins. By using activity tests and mass spectrometry, we showed that PAMP was formed upon protease treatment of the precursor protein. The propionibacteria produced the PAMP precursor constitutively during growth up to a level of similar to4 mg/liter, but the producing bacteria were unable to activate the precursor. The requirement for an external protease represents a novel strategy for generating antimicrobial peptides.
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页码:3649 / 3656
页数:8
相关论文
共 35 条
[1]  
CAMMUE BPA, 1992, J BIOL CHEM, V267, P2228
[2]   Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder [J].
Cole, AM ;
Weis, P ;
Diamond, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (18) :12008-12013
[3]   EVIDENCE THAT THE AMYLOID FIBRIL PROTEIN IN SENILE SYSTEMIC AMYLOIDOSIS IS DERIVED FROM NORMAL PREALBUMIN [J].
CORNWELL, GG ;
SLETTEN, K ;
JOHANSSON, B ;
WESTERMARK, P .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 154 (02) :648-653
[4]  
Creighton TE, 1993, PROTEINS STRUCTURES
[5]  
Eijsink VGH, 1998, APPL ENVIRON MICROB, V64, P3275
[6]   Class IIa bacteriocins: biosynthesis, structure and activity [J].
Ennahar, S ;
Sashihara, T ;
Sonomoto, K ;
Ishizaki, A .
FEMS MICROBIOLOGY REVIEWS, 2000, 24 (01) :85-106
[7]   Biochemical and genetic characterization of propionicin T1, a new bacteriocin from Propionibacterium thoenii [J].
Faye, T ;
Langsrud, T ;
Nes, IF ;
Holo, H .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (10) :4230-4236
[8]  
GILMORE MS, 1991, GENETICS AND MOLECULAR BIOLOGY OF STREPTOCOCCI, LACTOCOCCI, AND ENTEROCOCCI, P206
[9]   JENSENIIN-G, A HEAT-STABLE BACTERIOCIN PRODUCED BY PROPIONIBACTERIUM-JENSENII P126 [J].
GRINSTEAD, DA ;
BAREFOOT, SF .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1992, 58 (01) :215-220
[10]   Molecular nature of a novel bacterial toxin:: the cytolysin of Enterococcus faecalis [J].
Haas, W ;
Gilmore, MS .
MEDICAL MICROBIOLOGY AND IMMUNOLOGY, 1999, 187 (04) :183-190