PLANT-PIs: a database for plant protease inhibitors and their genes

Leo, Francesca De; Volpicella, Mariateresa; Licciulli, Flavio; Liuni, Sabino; Gallerani, Raffaele; Ceci, Luigi R.

doi:10.1093/nar/30.1.347

Cited by 141 publications

(73 citation statements)

References 9 publications

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“…Proteases inhibitors which are of common occurrence in plants are generally small proteins that have mainly found in storage tissues, such as seeds and tubers; however, they also occur in the aerial parts of plants (De Leo et al 2002). In plants, protease inhibitors are also induced in response to attack by pathogens and insects or injury (Ryan 1990).…”

Section: Resultsmentioning

confidence: 99%

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

et al. 2017

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Protease inhibitors from plants are well known to be potent inhibitors of the growth of bacteria, fungi, and even certain viruses which make them excellent candidates for use as the lead compounds for the development of novel antimicrobial agents for applications in medicine. In this study, Rhamnus frangula was selected as a protease inhibitor source. The maximum recovery of the protease inhibitor against trypsin was recorded in the crude extract made in 0.1 M phosphate buffer (pH 7.0) and isolated from the mature leaves. Then, the protease inhibitor designated as RfIP1 was purified to homogeneity by Sephadex G50 with an apparent molecular mass of 22.5 kDa and its N-terminal sequence exhibited a high degree of homology with known serine protease inhibitor sequences. The RfIP1 displayed maximal activity at pH 7 and 37°C. It maintained almost 80% of its maximal activity through a large pH range. The thermo-stability of RfIP1 was markedly enhanced by BSA, CaCl 2, and sorbitol, whereas the addition of Mg 2? , Zn 2? , NaTDC, SDS, DTT, and b-ME significantly promoted inhibitory activity. The protease inhibitor displayed high inhibitory activity toward some known proteases (cathepsin B, chymotrypsin, collagenase, thrombin, and trypsin) that have more importance in pharmaceutical industry and it acted as potent inhibitor of some commercially proteases from Aspergillus oryzae, Bacillus sp, and Bacillus licheniformis. The protease inhibitor also possessed an appreciable antibacterial effect against both Gram-positive and Gram-negative bacteria.

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Section: Resultsmentioning

confidence: 99%

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

et al. 2017

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“…They are classified into a number of families: serpins, Kunitz-STI, 3 Bowman-Birk, potato-type I and II, squash, and thaumatinlike inhibitors (2,4). For several decades, the Kunitz-STI superfamily has served as one of the model systems for the study of protein structure and protease-inhibitor recognition.…”

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confidence: 99%

The Plasticity of the β-Trefoil Fold Constitutes an Evolutionary Platform for Protease Inhibition

Azarkan

Martínez‐Rodríguez

Buts

et al. 2011

Journal of Biological Chemistry

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Background:The Kunitz-STI family is a paradigm of protease-inhibitor interaction in particular and protein-protein recognition in general. Results: PPI is a versatile protease inhibitor that targets several subfamilies of serine proteases. Conclusion: The ␤-trefoil fold constitutes an evolutionary platform for protease inhibition and molecular recognition. Significance: Fold plasticity influences protein evolution toward multiple function and binding promiscuity.

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“…PIs comprise at least 10 distinct protein families classified by their amino acid sequence and the mechanistic class of proteinases they inhibit (Laskowski and Kato, 1980;De Leo et al, 2002;Rawlings et al, 2004). Most plant PIs, such as the well-characterized Kunitz and Bowman-Birk PI families, inhibit Ser proteinases, in particular trypsin.…”

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confidence: 99%

Functional Analysis of the Kunitz Trypsin Inhibitor Family in Poplar Reveals Biochemical Diversity and Multiplicity in Defense against Herbivores

2007

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We investigated the functional and biochemical variability of Kunitz trypsin inhibitor (KTI) genes of Populus trichocarpa 3 Populus deltoides. Phylogenetic analysis, expressed sequence tag databases, and western-blot analysis confirmed that these genes belong to a large and diverse gene family with complex expression patterns. Five wound-and herbivore-induced genes representing the diversity of the KTI gene family were selected for functional analysis and shown to produce active KTI proteins in Escherichia coli. These recombinant KTI proteins were all biochemically distinct and showed clear differences in efficacy against trypsin-, chymotrypsin-, and elastase-type proteases, suggesting functional specialization of different members of this gene family. The in vitro stability of the KTIs in the presence of reducing agents and elevated temperature also varied widely, emphasizing the biochemical differences of these proteins. Significantly, the properties of the recombinant KTI proteins were not predictable from primary amino acid sequence data. Proteases in midgut extracts of Malacosoma disstria, a lepidopteran pest of Populus, were strongly inhibited by at least two of the KTI gene products. This study suggests that the large diversity in the poplar (Populus spp.) KTI family is important for biochemical and functional specialization, which may be important in the maintenance of pest resistance in long-lived plants such as poplar.

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PLANT-PIs: a database for plant protease inhibitors and their genes

Cited by 141 publications

References 9 publications

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

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

The Plasticity of the β-Trefoil Fold Constitutes an Evolutionary Platform for Protease Inhibition

Functional Analysis of the Kunitz Trypsin Inhibitor Family in Poplar Reveals Biochemical Diversity and Multiplicity in Defense against Herbivores

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