• Je něco špatně v tomto záznamu ?

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

J. Ilgová, L. Jedličková, H. Dvořáková, M. Benovics, L. Mikeš, L. Janda, J. Vorel, P. Roudnický, D. Potěšil, Z. Zdráhal, M. Gelnar, M. Kašný,

. 2017 ; 7 (1) : 17526. [pub] 20171213

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19035481

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.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc19035481
003      
CZ-PrNML
005      
20191008113033.0
007      
ta
008      
191007s2017 enk f 000 0|eng||
009      
AR
024    7_
$a 10.1038/s41598-017-17598-2 $2 doi
035    __
$a (PubMed)29235483
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a enk
100    1_
$a Ilgová, Jana $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Brno, 611 37, Czech Republic. jana.ilgova@gmail.com.
245    12
$a A novel type I cystatin of parasite origin with atypical legumain-binding domain / $c J. Ilgová, L. Jedličková, H. Dvořáková, M. Benovics, L. Mikeš, L. Janda, J. Vorel, P. Roudnický, D. Potěšil, Z. Zdráhal, M. Gelnar, M. Kašný,
520    9_
$a 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.
650    _2
$a zvířata $7 D000818
650    _2
$a kapři $x parazitologie $7 D002347
650    _2
$a klonování DNA $7 D003001
650    _2
$a počítačová simulace $7 D003198
650    _2
$a cystatiny $x metabolismus $7 D015891
650    _2
$a cysteinové endopeptidasy $x metabolismus $7 D003546
650    _2
$a Escherichia coli $7 D004926
650    _2
$a proteiny červů $x genetika $x metabolismus $7 D015801
650    _2
$a fylogeneze $7 D010802
650    _2
$a ploštěnci $x metabolismus $7 D010986
650    _2
$a vazba proteinů $7 D011485
650    _2
$a konformace proteinů $7 D011487
650    _2
$a proteinové domény $7 D000072417
650    _2
$a rekombinantní proteiny $x genetika $x metabolismus $7 D011994
650    _2
$a sekvenční seřazení $7 D016415
650    _2
$a sekvenční analýza proteinů $7 D020539
655    _2
$a srovnávací studie $7 D003160
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Jedličková, Lucie $u Department of Parasitology, Faculty of Science, Charles University, Prague, 128 44, Czech Republic.
700    1_
$a Dvořáková, Hana $u Department of Parasitology, Faculty of Science, Charles University, Prague, 128 44, Czech Republic.
700    1_
$a Benovics, Michal $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Brno, 611 37, Czech Republic.
700    1_
$a Mikeš, Libor $u Department of Parasitology, Faculty of Science, Charles University, Prague, 128 44, Czech Republic.
700    1_
$a Janda, Lubomír $u Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic.
700    1_
$a Vorel, Jiří $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Brno, 611 37, Czech Republic.
700    1_
$a Roudnický, Pavel $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Brno, 611 37, Czech Republic.
700    1_
$a Potěšil, David $u Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic.
700    1_
$a Zdráhal, Zbyněk $u Central European Institute of Technology, Masaryk University, Brno, 625 00, Czech Republic.
700    1_
$a Gelnar, Milan $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Brno, 611 37, Czech Republic.
700    1_
$a Kašný, Martin $u Department of Botany and Zoology, Faculty of Science, Masaryk University, Brno, 611 37, Czech Republic. Department of Parasitology, Faculty of Science, Charles University, Prague, 128 44, Czech Republic.
773    0_
$w MED00182195 $t Scientific reports $x 2045-2322 $g Roč. 7, č. 1 (2017), s. 17526
856    41
$u https://pubmed.ncbi.nlm.nih.gov/29235483 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20191007 $b ABA008
991    __
$a 20191008113449 $b ABA008
999    __
$a ok $b bmc $g 1452141 $s 1074031
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2017 $b 7 $c 1 $d 17526 $e 20171213 $i 2045-2322 $m Scientific reports $n Sci Rep $x MED00182195
LZP    __
$a Pubmed-20191007
Zpět

Najít záznam

Citační ukazatele

Možnosti archivace