Protease Inhibitors from Plants with Antimicrobial Activity

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.

Purification, characterization, and bioassay of putative protease inhibitors from Hevea brasiliensis latex

“…In accordance with the literature, serine and cysteine protease inhibitors are two types found in large quantities in the cells (Habib & Fazili, 2007;Mendoza-Blanco & Casaretto, 2012;Popovic et al, 2013). Both of these PI are part of cell homeostasis playing a role in plant defense against pathogens (Hartl et al, 2011, Kim et al, 2009.…”

“…The activity of protease inhibitor is related to their ability to form stable complex targeting proteases in order to inhibit, alter or prevent access to the active site of the enzyme so that the protein hydrolysis does not occur (Ryan, 1990;van der Hoorn, 2008;Farady & Craik, 2010). The protease inhibitor was structured by high content of cysteine residues forming disulfide bonds to withstand high temperature, extreme pH or proteolysis (Howe & Jander, 2008;Kim et al, 2009 (Habib & Fazili, 2007). Protease inhibitors are generally involved in defense mechanisms against biotic stress and developmental aspects (Chisholm et al, 2006;BoexFontvieille et al, 2015;Habib & Fazili, 2007;Shan et al, 2008;Steppuhn & Baldwin, 2007).…”

Purification and characterization of a newly serine protease inhibitor from Rhamnus frangula with potential for use as therapeutic drug

“…Based on their amino acid sequences, eight classes of plant serine protease inhibitors were reported (Mosolov and Valueva 2005). Among them, protease inhibitor 1, protease inhibitor 2, and soybean trypsin inhibitor families were well studied (Kim et al 2009;Meulenbroek et al 2012). Almost all the previously studied serine protease inhibitors are isolated from Solanaceae, Fabaceae, Euphorbiaceae, Poaceae, and Cucurbitaceae families.…”

Trypsin inhibitors from Capsicum baccatum var. pendulum leaves involved in Pepper yellow mosaic virus resistance

“…Trypsin inhibitors are serine proteinase inhibitors, and high concentrations of such inhibitors are associated with plant resistance to insects, fungi, bacteria, and viruses (Kim et al, 2009, Macedo et al, 2010, Oliva et al, 2011. A successful strategy employing defense proteins in plant breeding requires the investigation of in vitro and in vivo activity against pathogens, determining the partial or full amino acid sequence, and purifying and characterizing the protein of interest (Oliveira and Macedo, 2011).…”