scholarly journals The complex world of plant protease inhibitors: Insights into a Kunitz-type cysteine protease inhibitor of Arabidopsis thaliana

2017 ◽  
Vol 11 (1) ◽  
pp. e1368599 ◽  
Author(s):  
Sachin Rustgi ◽  
Edouard Boex-Fontvieille ◽  
Christiane Reinbothe ◽  
Diter von Wettstein ◽  
Steffen Reinbothe
Keyword(s):  
Arabidopsis Thaliana ◽  
Protease Inhibitor ◽  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitor ◽  
Complex World ◽  
Plant Protease ◽  
Kunitz Type

scholarly journals A Phytophthora palmivora Extracellular Cystatin-Like Protease Inhibitor Targets Papain to Contribute to Virulence on Papaya

2018 ◽  
Vol 31 (3) ◽  
pp. 363-373 ◽  
Author(s):  
Rebecca Gumtow ◽  
Dongliang Wu ◽  
Janice Uchida ◽  
Miaoying Tian
Keyword(s):  
Protease Inhibitor ◽  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Gene Editing ◽  
Sequence Data ◽  
Cysteine Protease Inhibitor ◽  
Phytophthora Palmivora ◽  
Cysteine Protease Inhibitors ◽  
Successful Infection

Papaya fruits, stems, and leaves are rich in papain, a cysteine protease that has been shown to mediate plant defense against pathogens and insects. Yet the oomycete Phytophthora palmivora is a destructive pathogen that infects all parts of papaya plants, suggesting that it has evolved cysteine protease inhibitors to inhibit papain to enable successful infection. Out of five putative extracellular cystatin-like cysteine protease inhibitors (PpalEPICs) from P. palmivora transcriptomic sequence data, PpalEPIC8 appeared to be unique to P. palmivora and was highly induced during infection of papaya. Purified recombinant PpalEPIC8 strongly inhibited papain enzyme activity, suggesting that it is a functional cysteine protease inhibitor. Homozygous PpalEPIC8 mutants were generated using CRISPR/Cas9-mediated gene editing via Agrobacterium-mediated transformation (AMT). Increased papain sensitivity of in-vitro growth and reduced pathogenicity during infection of papaya fruits were observed for the mutants compared with the wild-type strain, suggesting that PpalEPIC8, indeed, plays a role in P. palmivora virulence by inhibiting papain. This study provided genetic evidence demonstrating that plant-pathogenic oomycetes secrete cystatins as important weapons to invade plants. It also established an effective gene-editing system for P. palmivora by the combined use of CRISPR/Cas9 and AMT, which is expected to be applicable to other oomycetes.

A Kunitz-type cysteine protease inhibitor from cauliflower and Arabidopsis

Plant Science ◽  
2006 ◽  
Vol 170 (6) ◽  
pp. 1102-1110 ◽  
Author(s):  
Coralie E. Halls ◽  
Sally W. Rogers ◽  
Mohammed Oufattole ◽  
Ole Østergard ◽  
Birte Svensson ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitor ◽  
Kunitz Type

Cysteine protease inhibitors alter Golgi complex ultrastructure and function in Trypanosoma cruzi

1998 ◽  
Vol 111 (5) ◽  
pp. 597-606 ◽  
Author(s):  
J.C. Engel ◽  
P.S. Doyle ◽  
J. Palmer ◽  
I. Hsieh ◽  
D.F. Bainton ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Protease Inhibitor ◽  
Protease Inhibitors ◽  
Golgi Complex ◽  
Cysteine Protease ◽  
Intracellular Localization ◽  
Fluorescent Microscopy ◽  
Brefeldin A ◽  
Cysteine Protease Inhibitor ◽  
Cysteine Protease Inhibitors

Cruzain, the major cysteine protease of the protozoan parasite Trypanosoma cruzi, is a target of rational drug design for chemotherapy of Chagas' disease. The precise biological role of cruzain in the parasite life cycle and the mechanism involved in the trypanocidal effect of cysteine protease inhibitors are still unclear. Here we report biological and ultrastructural alterations caused by cysteine protease inhibitors in T. cruzi epimastigotes. Cruzain, a glycoprotein that transits the Golgi-endosomal pathway, localized to pre-lysosomes/lysosomes in the posterior end of untreated epimastigotes by fluorescent microscopy utilizing either a biotinylated cysteine protease inhibitor to tag the active site, or a specific anti-cruzain antibody. Radiolabeled or biotinylated cysteine protease inhibitors bound exclusively to cruzain in intact epimastigotes confirming that cruzain is accessible to, and is targeted by the inhibitors. Treatment of T. cruzi epimastigotes with specific cysteine protease inhibitors arrested growth, altered the intracellular localization of cruzain, and induced major alterations in the Golgi complex. Following treatment, cruzain accumulated in peripheral dilations of Golgi cisternae. There was a concomitant 70% reduction in gold-labeled cruzain transported to lysosomes. Cisternae abnormalities in the Golgi compartment were followed by distention of ER and nuclear membranes. Brefeldin A increased the number and size of cisternae in epimastigotes. Pre-treatment of epimastigotes with cysteine protease inhibitors followed by exposure to brefeldin A induced a more rapid appearance of the cysteine protease inhibitor-induced Golgi alterations. Our results suggest that cysteine protease inhibitors prevent the normal autocatalytic processing and trafficking of cruzain within the Golgi apparatus. Accumulation of cruzain may decrease mobility of Golgi membranes and result in peripheral distention of cisternae. These major alterations of the Golgi complex parallel the death of T. cruzi epimastigotes.

scholarly journals A Novel Cysteine Protease Inhibitor of Naegleria fowleri That Is Specifically Expressed during Encystation and at Mature Cysts

Pathogens ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 388
Author(s):  
Hương Giang Lê ◽  
A-Jeong Ham ◽  
Jung-Mi Kang ◽  
Tuấn Cường Võ ◽  
Haung Naw ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Expression Profiles ◽  
Critical Role ◽  
Cyst Formation ◽  
Cysteine Proteases ◽  
Cysteine Protease Inhibitor ◽  
Naegleria Fowleri ◽  
Nægleria Fowleri ◽  
Cystatin Family

Naegleria fowleri is a free-living amoeba that is ubiquitous in diverse natural environments. It causes a fatal brain infection in humans known as primary amoebic meningoencephalitis. Despite the medical importance of the parasitic disease, there is a great lack of knowledge about the biology and pathogenicity of N. fowleri. In this study, we identified and characterized a novel cysteine protease inhibitor of N. fowleri (NfCPI). NfCPI is a typical cysteine protease inhibitor belonging to the cystatin family with a Gln-Val-Val-Ala-Gly (QVVAG) motif, a characteristic motif conserved in the cystatin family of proteins. Bacterially expressed recombinant NfCPI has a dimeric structure and exhibits inhibitory activity against several cysteine proteases including cathespin Bs of N. fowleri at a broad range of pH values. Expression profiles of nfcpi revealed that the gene was highly expressed during encystation and cyst of the amoeba. Western blot and immunofluorescence assays also support its high level of expression in cysts. These findings collectively suggest that NfCPI may play a critical role in encystation or cyst formation of N. fowleri by regulating cysteine proteases that may mediate encystation or mature cyst formation of the amoeba. More comprehensive studies to investigate the roles of NfCPI in encystation and its target proteases are necessary to elucidate the regulatory mechanism and the biological significance of NfCPI.

Characterization of serine/cysteine protease inhibitor α1-antitripsin from meconium-instilled rabbit lungs

2005 ◽  
Vol 96 (1) ◽  
pp. 137-144 ◽  
Author(s):  
A.M. Zagariya ◽  
R. Bhat ◽  
E. Zhabotynsky ◽  
G. Chari ◽  
S. Navale ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Cysteine Protease ◽  
Cysteine Protease Inhibitor
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