title: A highly thermostable antimicrobial peptide from Aspergillus clavatus ES1: biochemical and molecular characterization.
abstract: Antimicrobial peptides (AMPs) are extremely attractive candidates as therapeutic agents due to their wide spectrum of antimicrobial activity and mechanism of action, which differs from that of small-molecule antibiotics. In this study, a 6.0-kDa antimicrobial peptide from Aspergillus clavatus ES1, designated as AcAMP, was isolated by a one-step heat treatment. AcAMP was sensitive to proteolytic enzymes, stable between pH 5.0 and 10.0, and heat resistant (15 min at 100 degrees C). The acamp gene encoding AcAMP peptide was isolated by reverse-transcriptase polymerase chain reaction (RT-PCR) and cloned in pCRII-TOPO vector. Sequence analysis of the complementary DNA (cDNA) acamp gene revealed an open reading frame of 282 bp encoding a peptide of 94 amino acid residues consisting of a 21-aa signal peptide, a 22-aa pro-peptide, and a 51-aa mature peptide. The deduced amino acid sequence showed high identity with other ascomycete antifungal peptides. AcAMP belongs to the group of small, cysteine-rich, basic proteins with antimicrobial activity. In addition to its antifungal activity, AcAMP is the first fungal peptide exhibiting antibacterial activity against several Gram-positive and Gram-negative bacteria. Based on all these features, AcAMP can be considered as a promising new member of the restraint family of ascomycete antimicrobial peptides that might be used in biological control of plant diseases and also for potential applications in food preservation.
authors.affiliation: Laboratoire de Génie Enzymatique et de Microbiologie, Ecole Nationale d'Ingénieurs de Sfax, 1173-3038 Sfax, Tunisia. hajjimed1989@yahoo.fr
authors.forename: Mohamed
authors.initials: M
authors.lastname: Hajji
authors.forename: Kemel
authors.initials: K
authors.lastname: Jellouli
authors.forename: Noomen
authors.initials: N
authors.lastname: Hmidet
authors.forename: Rafik
authors.initials: R
authors.lastname: Balti
authors.forename: Alya
authors.initials: A
authors.lastname: Sellami-Kamoun
authors.forename: Moncef
authors.initials: M
authors.lastname: Nasri
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D001230:Aspergillus / Q000737:chemistry*; D001419:Bacteria / Q000187:drug effects*; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000494:pharmacology*; D005658:Fungi / Q000187:drug effects*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016366:Open Reading Frames; D055550:Protein Stability; D020133:Reverse Transcriptase Polymerase Chain Reaction; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: D023181:Antimicrobial Cationic Peptides; D004269:DNA, Bacterial; D018076:DNA, Complementary; D005656:Fungal Proteins