Evolutionary analysis of the cystatin family in three Schistosoma species

Cuesta-Astroz, Yesid; Scholte, Larissa Lopes Silva; Pais, Fabiano Sviatopolk-Mirsky; Oliveira, Guilherme; Nahum, Laila Alves

doi:10.3389/fgene.2014.00206

Cited by 14 publications

(16 citation statements)

References 61 publications

(116 reference statements)

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“…nipponicum cysteine peptidase inhibitor (EnStef) displays the typical length of type I cystatins (98 amino acids) and shares most of its sequential and structural characteristics with other type I cystatins, which are also known under the name stefins (I25A subfamily) 6 . Similarly to other platyhelminth stefin orthologs identified by combined computational approach 35 , EnStef lacks a signal peptide and the PW motif, but include the QxVxG and LP domains.…”

Section: Discussionmentioning

confidence: 99%

A novel type I cystatin of parasite origin with atypical legumain-binding domain

Ilgová

Jedličková

Dvořáková

et al. 2017

Sci Rep

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Parasite inhibitors of cysteine peptidases are known to influence a vast range of processes linked to a degradation of either the parasites’ own proteins or proteins native to their hosts. We characterise a novel type I cystatin (stefin) found in a sanguinivorous fish parasite Eudiplozoon nipponicum (Platyhelminthes: Monogenea). We have identified a transcript of its coding gene in the transcriptome of adult worms. Its amino acid sequence is similar to other stefins except for containing a legumain-binding domain, which is in this type of cystatins rather unusual. As expected, the recombinant form of E. nipponicum stefin (rEnStef) produced in Escherichia coli inhibits clan CA peptidases – cathepsins L and B of the worm – via the standard papain-binding domain. It also blocks haemoglobinolysis by cysteine peptidases in the worm’s excretory-secretory products and soluble extracts. Furthermore, we had confirmed its ability to inhibit clan CD asparaginyl endopeptidase (legumain). The presence of a native EnStef in the excretory-secretory products of adult worms, detected by mass spectrometry, suggests that this protein has an important biological function at the host-parasite interface. We discuss the inhibitor’s possible role in the regulation of blood digestion, modulation of antigen presentation, and in the regeneration of host tissues.

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Section: Discussionmentioning

confidence: 99%

A novel type I cystatin of parasite origin with atypical legumain-binding domain

Ilgová

Jedličková

Dvořáková

et al. 2017

Sci Rep

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“…microstoma and T . solium [ 19 ]. In addition, excepting cestode cystatins, all predicted models of platyhelminth stefins and cystatins exhibited the similar conserved α-helix and β-pleat and the functional hydrophobic edge features that find in the human stefin [ 33 , 51 ] and chicken cystatin models [ 32 ], respectively (not shown).…”

Section: Resultsmentioning

confidence: 99%

“…Additionally, some studies have shown that nematode cystatins modulate host immune responses [ 13 – 16 ]. However, little is known about the cestode cystatin superfamily and trematode cystatin superfamily [ 17 – 19 ].…”

Section: Introductionmentioning

confidence: 99%

Comparative Analysis of Cystatin Superfamily in Platyhelminths

Guo

2015

PLoS ONE

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The cystatin superfamily is comprised of cysteine proteinase inhibitors and encompasses at least 3 subfamilies: stefins, cystatins and kininogens. In this study, the platyhelminth cystatin superfamily was identified and grouped into stefin and cystatin subfamilies. The conserved domain of stefins (G, QxVxG) was observed in all members of platyhelminth stefins. The three characteristics of cystatins, the cystatin-like domain (G, QxVxG, PW), a signal peptide, and one or two conserved disulfide bonds, were observed in platyhelminths, with the exception of cestodes, which lacked the conserved disulfide bond. However, it is noteworthy that cestode cystatins had two tandem repeated domains, although the second tandem repeated domain did not contain a cystatin-like domain, which has not been previously reported. Tertiary structure analysis of Taenia solium cystatin, one of the cestode cystatins, demonstrated that the N-terminus of T. solium cystatin formed a five turn α-helix, a five stranded β-pleated sheet and a hydrophobic edge, similar to the structure of chicken cystatin. Although no conserved disulfide bond was found in T. solium cystatin, the models of T. solium cystatin and chicken cystatin corresponded at the site of the first disulfide bridge of the chicken cystatin. However, the two models were not similar regarding the location of the second disulfide bridge of chicken cystatin. These results showed that T. solium cystatin and chicken cystatin had similarities and differences, suggesting that the biochemistry of T. solium cystatin could be similar to chicken cystatin in its inhibitory function and that it may have further functional roles. The same results were obtained for other cestode cystatins. Phylogenetic analysis showed that cestode cystatins constituted an independent clade and implied that cestode cystatins should be considered to have formed a new clade during evolution.

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“…The hairpin loop 1 containing the conserved QVVAG motif was a classic conformation of Cystatins. In TK-cystatin, the hairpin loop 2, formed by amino acid residues between two C-terminal β-sheet included conservative hydrophobic LP residues that was absence or replaced by PW in other cystatins (Cuesta-Astroz et al 2014).…”

Section: D Structure Of Tk-cystatin and Molecular Dockingmentioning

confidence: 99%

Bioinformatics analysis and characterization of a secretory cystatin from Thelohanellus kitauei

Zhang

Yang

Gao

et al. 2020

Preprint

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Thelohanellus kitauei , is a group of obligate parasitic Myxozoans, which causes intestinal giant-cystic disease of common carp ( Cyprinus carpio) and has resulted in significant economic losses in carp farms. Cystatin secreted by parasites can regulate the immune response of host to facilitate parasite’s survival. In this study, the secretory TK-cystatin gene, encoding a protein of 120 amino acid residues (13.65 kDa), was cloned from T. kitauei genome. Phylogenetic analysis showed that TK-cystatin gene is closely related to the cystatin-A from Hydra vulgaris . Multiple sequence alignment revealed that TK-cystatin had three conserved motifs: N-terminal G 19 G 20 , Q 73 VVAG 77 , and C-terminal L 102 P 103 . Molecular docking between TK-cystatin and three cysteine proteases showed a lower binding energy (-13 kal/mol) with cathepsin L whereas a higher binding energy (-8.6 kal/mol) with cathepsin B. TK-cystatin gene was expressed in Escherichia coli . Activity assays revealed that TK-cystatin has stronger inhibitory activity on endopeptidases (papain and cathepsin L) and weaker inhibitory activity on exopeptidase (cathepsin B). TK-cystatin was stable under the condition of acidity or alkalinity or below 57 °C. This study laid a foundation for the design and development of the anti-TK-cystatin vaccine in carp culture in the future.

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Evolutionary analysis of the cystatin family in three Schistosoma species

Cited by 14 publications

References 61 publications

A novel type I cystatin of parasite origin with atypical legumain-binding domain

A novel type I cystatin of parasite origin with atypical legumain-binding domain

Comparative Analysis of Cystatin Superfamily in Platyhelminths

Bioinformatics analysis and characterization of a secretory cystatin from Thelohanellus kitauei

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