Abstract
Antimicrobial proteins (peptides) are known to play important roles in the innate host defense mechanisms of most living organisms, including plants, insects, amphibians and mammals. They are also known to possess potent antibiotic activity against bacteria, fungi, and even certain viruses. Recently, the rapid emergence of microbial pathogens that are resistant to currently available antibiotics has triggered considerable interest in the isolation and investigation of the mode of action of antimicrobial proteins (peptides). Plants produce a variety of proteins (peptides) that are involved in the defense against pathogens and invading organisms, including ribosome-inactivating proteins, lectins, protease inhibitors and antifungal peptides (proteins). Specially, the protease inhibitors can inhibit aspartic, serine and cysteine proteinases. Increased levels of trypsin and chymotrypsin inhibitors correlated with the plants resistance to the pathogen. Usually, the purification of antimicrobial proteins (peptides) with protease inhibitor activity was accomplished by salt-extraction, ultrafiltration and C18 reverse phase chromatography, successfully. We discuss the relation between antimicrobial and anti-protease activity in this review. Protease inhibitors from plants potently inhibited the growth of a variety of pathogenic bacterial and fungal strains and are therefore excellent candidates for use as the lead compounds for the development of novel antimicrobial agents.
Highlights
Antimicrobial peptides have been isolated from a wide variety of organisms, including animals, bacteria, insects and plants [1,2,3,4,5,6]
Protease inhibitors in plants are usually considered to work as storage proteins and as a defense mechanism [19]
Reduced PT-1 almost completely lost its activity against fungi and proteases, indicating that the disulfide bridge is essential for its protease inhibitor and antibacterial activity [62] (Figure 4)
Summary
Antimicrobial peptides have been isolated from a wide variety of organisms, including animals, bacteria, insects and plants [1,2,3,4,5,6]. Protease inhibitors in plants are usually considered to work as storage proteins (nitrogen source) and as a defense mechanism [19] They have recently received improved interest because of their ability to potently inhibit carcinogenesis in a wide variety of in vivo and in vitro systems [20]. The cell wall associated peptide snakin-1 produced by the potato was initially purified as a member of what appears to be a widely distributed peptide type, the Snakin/GASA family This peptide was found to developmentally accumulate in different tissues of potato plants and the expression of its corresponding gene was unaffected by a variety of abiotic or biotic challenges. It has been reported that carboxypeptidase inhibitor, which contains 39-amino acids and three disulfide bridges, is an antagonist of human epidermal growth factor [49] It was purified antimicrobial proteins (peptides) from potato, that shares homology with an acid phosphatase. This study was conducted to evaluate low molecularweight potato peptides with antimicrobial activity and identify the mechanism by which they exert their protective role
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