Protease inhibitors from plants with antimicrobial activity.
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 C(18) 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.
Kim
Jin-Young
JY
Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Park
Seong-Cheol
SC
Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.
Hwang
Indeok
I
Department of Biotechnology and BK21 Research Team for Protein Activity Control, Chosun University, Gwangju 501-759, Korea.
Cheong
Hyeonsook
H
Department of Biotechnology and BK21 Research Team for Protein Activity Control, Chosun University, Gwangju 501-759, Korea.
Nah
Jae-Woon
JW
Department of Polymer Science and Engineering, Sunchon National University, 315 Maegok, Suncheon, Korea.
Hahm
Kyung-Soo
KS
Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.|Department of Cellular & Molecular Medicine, School of Medicine, Chosun University, Gwangju 501-759, Korea.
Park
Yoonkyung
Y
Research Center for Proteineous Materials, Chosun University, Gwangju 501-759, Korea.|Department of Biotechnology and BK21 Research Team for Protein Activity Control, Chosun University, Gwangju 501-759, Korea.
D000890:Anti-Infective Agents / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects; D002176:Candida albicans / Q000187:drug effects; D007887:Fabaceae / Q000378:metabolism; D010455:Peptides / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D010944:Plants / Q000378:metabolism*; D011480:Protease Inhibitors / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D011198:Solanum tuberosum / Q000378:metabolism
D000890:Anti-Infective Agents; D010455:Peptides; D011480:Protease Inhibitors