Novel cathepsin L-like protease from dermestid beetle Dermestes frischii maggot

Papisova, Anastasia Ivanovna; Javadov, Araz; Rudenskaya, Yulia A.; Balandina, G. N.; Zhantiev, R. D.; Korsunovskaia, Olga Sergeevna; Dunaevsky, Yakov E.; Rudenskaya, G. N.

doi:10.1016/j.biochi.2010.08.014

Cited by 6 publications

(3 citation statements)

References 30 publications

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“…Similar results were observed in other crustaceans, since the CatL mature peptide in Penaeus monodon (ABQ10739.1), Artemia franciscana (AAV63977.1) and A. salina (ABS17682.1) are 215, 214 and 214 amino acids, respectively. On the other hand, the mature cysteine protease of Dermestes frischii contains 219-amino acid residues (Papisova et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

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Molecular characterization of cathepsin L cDNA and its expression during oogenesis and embryogenesis in the oriental river prawn Macrobrachium nipponense (Palaemonidae)

Zhao¹,

Chen²,

Zhang³

et al. 2013

Genet. Mol. Res.

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ABSTRACT. We identified the cDNA sequence of cathepsin L (CatL) in Macrobrachium nipponense, designated as MnCatL, for the first time. The MnCatL cDNA, isolated from the ovary, was 1710 bp in length, containing a 31-bp 5'-untranslated region, a 650-bp 3'-untranslated region, and an open reading frame of 1029 bp, encoding a 342-amino acid polypeptide with a predicted molecular mass of 37.7 kDa. The polypeptide is composed of an 18-amino acid signal peptide, a 106-amino acid propeptide and a 218-amino acid mature peptide. MnCatL mRNA was detected in all tissues that we examined, including the thoracic ganglia, heart, muscle, intestine, hemocytes, ovary, testis, gills, and hepatopancreas. MnCatL expression reached a maximum value in both hepatopancreas and ovaries at the later stages of vitellogenesis, suggesting that MnCatL is involved in ovarian maturation of the oriental river prawn. During embryogenesis, MnCatL expression decreased as the embryo developed. The expression of MnCatL in the ovary and embryo suggest that MnCatL plays an important role in the uptake of vitellogenin and yolk protein, which are deposited in the oocyte for ovary maturation and embryo development, during oogenesis and embryogenesis of M. nipponense.

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Section: Discussionmentioning

confidence: 99%

“…The Gln and Asn residues play an important role in catalysis. Gln preceding the catalytic Cys is believed to help the formation of the oxyanion hole (Papisova et al, 2011). The Asn residue orients the imidazolium ring of the catalytic His.…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of cathepsin L cDNA and its expression during oogenesis and embryogenesis in the oriental river prawn Macrobrachium nipponense (Palaemonidae)

Zhao¹,

Chen²,

Zhang³

et al. 2013

Genet. Mol. Res.

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“…Coleoptera insects mainly use cysteine proteases as digestive enzymes [ 3 , 4 , 5 , 6 , 7 ], while Lepidoptera usually rely on serine proteases activities [ 8 , 9 ]. Accordingly, the digestive protease profile of S. levis has revealed that its major protease is Sl-CathL, a cysteine cathepsin L-like, followed by other proteases, e.g., trypsin-like enzymes [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and Functional Analysis of a Pseudo-Cysteine Protease from the Midgut Transcriptome of Sphenophorus levis

Shibao

Ferro

Paula

et al. 2021

IJMS

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The Sphenophorus levis (Coleoptera, Curculionidae) is one of the main pests of sugarcane in Brazil. Although its major digestive proteases are known, its complex digestive process still needs to be further understood. We constructed a transcriptome from the midgut of 30-day-old larvae and identified sequences similar to its major digestive protease (cysteine cathepsin Sl-CathL), however, they presented a different amino acid than cysteine in the active cleft. We identified, recombinantly produced, and characterized Sl-CathL-CS, a pseudo cysteine protease, and verified that higher gene expression levels of Sl-CathL-CS occur in the midgut of 30-day old larvae. We reverted the serine residue to cysteine and compared the activity of the mutant (Sl-CathL-mutSC) with Sl-CathL-CS. Sl-CathL-CS presented no protease activity, but Sl-CathL-mutSC hydrolyzed Z-Phe-Arg-AMC (Vmax = 1017.60 ± 135.55, Km = 10.77 mM) and was inhibited by a cysteine protease inhibitor E-64 (Ki = 38.52 ± 1.20 μM), but not by the serine protease inhibitor PMSF. Additionally, Sl-CathL-CS interacted with a sugarcane cystatin, while Sl-CathL-mutSC presented weaker interaction. Finally, protein ligand docking reinforced the differences in the catalytic sites of native and mutant proteins. These results indicate that Sl-CathL-CS is a pseudo-cysteine protease that assists protein digestion possibly by interacting with canecystatins, allowing the true proteases to work.

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Characterization of insect stains produced by Dermestes maculatus De Greer (Coleoptera: Dermestidae) resulting from interactions with human blood

Rivers,

Waters

2023

Int J Legal Med

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Novel cathepsin L-like protease from dermestid beetle Dermestes frischii maggot

Cited by 6 publications

References 30 publications

Molecular characterization of cathepsin L cDNA and its expression during oogenesis and embryogenesis in the oriental river prawn Macrobrachium nipponense (Palaemonidae)

Molecular characterization of cathepsin L cDNA and its expression during oogenesis and embryogenesis in the oriental river prawn Macrobrachium nipponense (Palaemonidae)

Identification and Functional Analysis of a Pseudo-Cysteine Protease from the Midgut Transcriptome of Sphenophorus levis

Characterization of insect stains produced by Dermestes maculatus De Greer (Coleoptera: Dermestidae) resulting from interactions with human blood

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