scholarly journals Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)

2019 ◽  
Vol 9 ◽  
Author(s):  
Aiping Zhao ◽  
Yin Li ◽  
Chunmeng Leng ◽  
Ping Wang ◽  
Yiping Li
Keyword(s):  
Protease Inhibitors ◽  
Plutella Xylostella ◽  
Inhibitory Effect ◽  
Larval Midgut

scholarly journals Tissue-Specific Transcriptome Profiling of Plutella Xylostella Third Instar Larval Midgut

2012 ◽  
Vol 8 (8) ◽  
pp. 1142-1155 ◽  
Author(s):  
Wen Xie ◽  
Yanyuan Lei ◽  
Wei Fu ◽  
Zhongxia Yang ◽  
Xun Zhu ◽  
...  
Keyword(s):  
Plutella Xylostella ◽  
Transcriptome Profiling ◽  
Tissue Specific ◽  
Larval Midgut

scholarly journals Trypsin is associated with the rotavirus capsid and is activated by solubilization of outer capsid proteins

2005 ◽  
Vol 86 (11) ◽  
pp. 3143-3151 ◽  
Author(s):  
Yann Benureau ◽  
Jean Claude Huet ◽  
Annie Charpilienne ◽  
Didier Poncet ◽  
Jean Cohen
Keyword(s):  
Protease Inhibitors ◽  
Outer Layer ◽  
Inhibitory Effect ◽  
High Titre ◽  
Capsid Proteins ◽  
Viral Particles ◽  
Outer Capsid ◽  
Viral Capsid Proteins

The rotavirus capsid is made up of three concentric protein layers. The outer layer, consisting of VP7 and VP4, is lost during virus entry into the host cell. Rotavirus field isolates can be adapted to high-titre growth in tissue culture by treatment with trypsin and by supplementing the culture medium with trypsin, which cleaves VP4 into two fragments, VP8* and VP5*. It is known that protease inhibitors reduce the replication of rotavirus in vitro and in vivo and also diminish disease symptoms in a mouse model. To clarify the molecular basis of these observations, a series of assays were conducted on purified rotavirus particles grown in the presence of trypsin. Results of HPLC and mass spectrometry followed by N-terminal sequencing showed that viral particles contain molecules of trypsin. When associated with triple-layer particles (TLPs), trypsin is inactive and not accessible to protease inhibitors, such as aprotinin. When the outer layer is solubilized by calcium-chelating agents, VP5*, VP8* and VP7 are released and the associated trypsin is activated, allowing cleavage of the viral capsid proteins, as well as other exogenous proteins. It is shown that addition of trypsin inhibitors significantly reduces synthesis of viral mRNA and viral proteins in cells and has a major inhibitory effect if present when virus enters the cell. These data indicate that incorporation of trypsin into rotavirus particles may enhance its infectivity.

scholarly journals Inhibitory Activity of Human Immunodeficiency Virus Aspartyl Protease Inhibitors against Encephalitozoon intestinalis Evaluated by Cell Culture-Quantitative PCR Assay

2005 ◽  
Vol 49 (6) ◽  
pp. 2362-2366 ◽  
Author(s):  
Jean Menotti ◽  
Maud Santillana-Hayat ◽  
Bruno Cassinat ◽  
Claudine Sarfati ◽  
Francis Derouin ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Quantitative Pcr ◽  
Inhibitory Effect ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Aspartyl Protease ◽  
Pcr Assay ◽  
Real Time Quantitative Pcr ◽  
Quantitative Pcr Assay ◽  
Aspartyl Protease Inhibitors

ABSTRACT Immune reconstitution might not be the only factor contributing to the low prevalence of microsporidiosis in human immunodeficiency virus (HIV)-infected patients treated with protease inhibitors, as these drugs may exert a direct inhibitory effect against fungi and protozoa. In this study, we developed a cell culture-quantitative PCR assay to quantify Encephalitozoon intestinalis growth in U-373-MG human glioblastoma cells and used this assay to evaluate the activities of six HIV aspartyl protease inhibitors against E. intestinalis. A real-time quantitative PCR assay targeted the E. intestinalis small-subunit rRNA gene. HIV aspartyl protease inhibitors were tested over serial concentrations ranging from 0.2 to 10 mg/liter, with albendazole used as a control. Ritonavir, lopinavir, and saquinavir were able to inhibit E. intestinalis growth, with 50% inhibitory concentrations of 1.5, 2.2, and 4.6 mg/liter, respectively, whereas amprenavir, indinavir, and nelfinavir had no inhibitory effect. Pepstatin A, a reference aspartyl protease inhibitor, could also inhibit E. intestinalis growth, suggesting that HIV protease inhibitors may act through the inhibition of an E. intestinalis-encoded aspartyl protease. These results showed that some HIV protease inhibitors can inhibit E. intestinalis growth at concentrations that are achievable in vivo and that the real-time quantitative PCR assay that we used is a valuable tool for the in vitro assessment of the activities of drugs against E. intestinalis.

scholarly journals Protease Inhibitors Purified from the Canola Meal Extracts of Two Genetically Diverse Genotypes Exhibit Antidiabetic and Antihypertension Properties

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 2078
Author(s):  
Saira Hussain ◽  
Ata-ur Rehman ◽  
David J. Luckett ◽  
S.M. Saqlan Naqvi ◽  
Christopher L. Blanchard
Keyword(s):  
Protease Inhibitors ◽  
Serine Proteases ◽  
Plant Pathogens ◽  
Gel Filtration ◽  
Ace Inhibition ◽  
Inhibitory Effect ◽  
Canola Meal ◽  
Native Page ◽  
Dpp Iv ◽  
Sds Page

Valorization of vegetable oil waste residues is gaining importance due to their high protein and polyphenol contents. Protease inhibitors (PIs), proteins from these abundantly available waste residues, have recently gained importance in treating chronic diseases. This research aimed to use canola meal of genetically diverse Brassica napus genotypes, BLN-3347 and Rivette, to identify PIs with diverse functionalities in therapeutic and pharmacological applications. The canola meal PI purification steps involved: native PAGE and trypsin inhibition activity, followed by ammonium sulfate fractionation, anion exchange, gel filtration, and reverse-phase chromatography. The purified PI preparations were characterized using SDS-PAGE, isoelectric focusing (IEF), and N terminal sequencing. SDS-PAGE analysis of PI preparations under native reducing and nonreducing conditions revealed three polymorphic PIs in each genotype. The corresponding IEF of the genotype BLN-3347, exhibited three acidic isoforms with isoelectric points (pI) of 4.6, 4.0, and 3.9, while Rivette possessed three isoforms, exhibiting two basic forms of pI 8.65 and 9.9, and one acidic of pI 6.55. Purified PI preparations from both the genotypes displayed dipeptidyl peptidase-IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibition activities; the BLN-3347 PI preparation exhibited a strong inhibitory effect with lower IC50 values (DPP-IV 37.42 µg/mL; ACE 129 µg/mL) than that from Rivette (DPP-IV 67.97 µg/mL; ACE 376.2 µg/mL). In addition to potential human therapy, these highly polymorphic PIs, which can inhibit damaging serine proteases secreted by canola plant pathogens, have the potential to be used by canola plant breeders to seek qualitative trait locus (QTLs) linked to genes conferring resistance to canola diseases.

Inhibitory effect of a series of protease inhibitors on influenza virus replication in vitro

1995 ◽  
Vol 26 (3) ◽  
pp. A348
Author(s):  
M. Hosoya ◽  
H. Kawamural ◽  
T. Ishii ◽  
H. Suzuki ◽  
J. Watanabe ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Protease Inhibitors ◽  
Virus Replication ◽  
Inhibitory Effect ◽  
Influenza Virus Replication

Inhibition of Influenza Virus A/WSN Replication by Serine Protease Inhibitors and anti-Protease Antibodies

1994 ◽  
Vol 5 (3) ◽  
pp. 187-190 ◽  
Author(s):  
A. Someya ◽  
N. Tanaka ◽  
A. Okuyama
Keyword(s):  
Serine Protease ◽  
Protease Inhibitors ◽  
Cathepsin B ◽  
Mdck Cells ◽  
Membrane Surface ◽  
Plaque Assay ◽  
Inhibitory Effect ◽  
Factor X ◽  
Serine Protease Inhibitors ◽  
Igg Antibody

The serine protease inhibitors, aprotinin and 6-amidino-2-naphthyl-p-guanidinobenzoate (Futhan), showed striking antiviral activity in the plaque assay of the canine kidney (MDCK) cell-WSN strain system. Anti-cathepsin B IgG antibody/showed the greatest inhibitory effect on plaque formation, followed by anti-factor X antibody and then anti-plasminogen antibody. Anti-cathepsin B antibody inhibited the proteolytic cleavage of haemagglutinin (HA). These results suggest that a serine protease-like enzyme and the other protein that binds to anti-cathepsin B antibody may be involved in the process of WSN HA cleavage on the membrane surface of MDCK cells.

scholarly journals Partial Characterization of Protease Inhibitors of Ulva ohnoi and Their Effect on Digestive Proteases of Marine Fish

Marine Drugs ◽  
2020 ◽  
Vol 18 (6) ◽  
pp. 319
Author(s):  
Antonio Jesús Vizcaíno ◽  
Alba Galafat ◽  
María Isabel Sáez ◽  
Tomás Francisco Martínez ◽  
Francisco Javier Alarcón
Keyword(s):  
Protease Inhibitors ◽  
Marine Fish ◽  
Inhibitory Effect ◽  
Inhibition Mechanism ◽  
Digestive Proteases ◽  
Reference Protein ◽  
Ulva Ohnoi ◽  
Hydrolysis Of

This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species, as well as their capacity to hamper the hydrolysis of a reference protein by those fish proteases, were assessed. In addition, thermal stability and the mode of inhibition on trypsin and chymotrypsin were also studied. Dose-response inhibition curves and in vitro protein hydrolysis assays revealed a noticeable inhibition of fish enzymes when Ulva concentration increased in the assay. The thermal treatment of Ulva reduced markedly the inhibitory effect on fish digestive protease. Finally, Lineweaver–Burk plots indicated that trypsin and chymotrypsin inhibition consisted of a mixed-type inhibition mechanism in which the inhibitory effect depends on Ulva concentration. Overall, the results confirmed the presence of protease inhibitors in Ulva, though heat treatment was enough for inactivating these compounds.

The effect of host plant on the development and larval midgut protease activity of Plutella xylostella (Lepidoptera: Plutellidae)

2019 ◽  
Vol 47 (4) ◽  
pp. 475-483 ◽  
Author(s):  
Aiping Zhao ◽  
Xiangqun Yuan ◽  
Di Hu ◽  
Chunmeng Leng ◽  
Yin Li ◽  
...  
Keyword(s):  
Host Plant ◽  
Plutella Xylostella ◽  
Protease Activity ◽  
Larval Midgut
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