Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus

2021 ◽  
Vol 77 (9) ◽  
pp. 1183-1196 ◽  
Author(s):  
Barbora Kascakova ◽  
Jan Kotal ◽  
Larissa Almeida Martins ◽  
Zuzana Berankova ◽  
Helena Langhansova ◽  
...  

Iripin-5 is the main Ixodes ricinus salivary serpin, which acts as a modulator of host defence mechanisms by impairing neutrophil migration, suppressing nitric oxide production by macrophages and altering complement functions. Iripin-5 influences host immunity and shows high expression in the salivary glands. Here, the crystal structure of Iripin-5 in the most thermodynamically stable state of serpins is described. In the reactive-centre loop, the main substrate-recognition site of Iripin-5 is likely to be represented by Arg342, which implies the targeting of trypsin-like proteases. Furthermore, a computational structural analysis of selected Iripin-5–protease complexes together with interface analysis revealed the most probable residues of Iripin-5 involved in complex formation.

Plant Science ◽  
2015 ◽  
Vol 241 ◽  
pp. 151-163 ◽  
Author(s):  
Yang Wang ◽  
Shoaib Azhar ◽  
Rosaria Gandini ◽  
Christina Divne ◽  
Ines Ezcurra ◽  
...  

2016 ◽  
Vol 430 ◽  
pp. 36-43 ◽  
Author(s):  
Chao Chen ◽  
Bin Liu ◽  
Yongchang Xu ◽  
Natalia Utkina ◽  
Dawei Zhou ◽  
...  

Endocrine ◽  
2010 ◽  
Vol 37 (3) ◽  
pp. 442-448 ◽  
Author(s):  
Vardan T. Karamyan ◽  
Jason Arsenault ◽  
Emanuel Escher ◽  
Robert C. Speth

2006 ◽  
Vol 99 (2) ◽  
pp. 616-627 ◽  
Author(s):  
Federica Bruzzone ◽  
Benoît Lectez ◽  
Hélène Tollemer ◽  
Jérôme Leprince ◽  
Cynthia Dujardin ◽  
...  

Endocrine ◽  
2010 ◽  
Vol 38 (2) ◽  
pp. 312-312
Author(s):  
Vardan T. Karamyan ◽  
Jason Arsenault ◽  
Emanuel Escher ◽  
Robert C. Speth

2012 ◽  
Vol 31 (4) ◽  
pp. 741-749 ◽  
Author(s):  
Vincent Deramecourt ◽  
Florence Lebert ◽  
Claude-Alain Maurage ◽  
Francisco-Jose Fernandez-Gomez ◽  
Simon Dujardin ◽  
...  

2011 ◽  
Vol 438 (2) ◽  
pp. 275-282 ◽  
Author(s):  
Marián Mazáň ◽  
Enrico Ragni ◽  
Laura Popolo ◽  
Vladimír Farkaš

BGTs [β-(1,3)-glucanosyltransglycosylases; EC 2.4.1.-] of the GH72 (family 72 of glycosylhydrolases) are GPI (glycosylphosphatidylinositol)-anchored proteins that play an important role in the biogenesis of fungal cell walls. They randomly cleave glycosidic linkages in β-(1,3)-glucan chains and ligate the polysaccharide portions containing newly formed reducing ends to C3(OH) at non-reducing ends of other β-(1,3)-glucan molecules. We have developed a sensitive fluorescence-based method for the assay of transglycosylating activity of GH72 enzymes. In the new assay, laminarin [β-(1,3)-glucan] is used as the glucanosyl donor and LamOS (laminarioligosaccharides) fluorescently labelled with SR (sulforhodamine) serve as the acceptors. The new fluorescent assay was employed for partial biochemical characterization of the heterologously expressed Gas family proteins from the yeast Saccharomyces cerevisiae. All the Gas enzymes specifically used laminarin as the glucanosyl donor and a SR–LamOS of DP (degree of polymerization) ≥5 as the acceptors. Gas proteins expressed in distinct stages of the yeast life cycle showed differences in their pH optima. Gas1p and Gas5p, which are expressed during vegetative growth, had the highest activity at pH 4.5 and 3.5 respectively, whereas the sporulation-specific Gas2p and Gas4p were most active between pH 5 and 6. The novel fluorescent assay provides a suitable tool for the screening of potential glucanosyltransferases or their inhibitors.


2013 ◽  
Vol 12 (8) ◽  
pp. 812-820 ◽  
Author(s):  
A. Blanco-Grau ◽  
I. Bonaventura-Ibars ◽  
J. Coll-Cantí ◽  
M. J. Melià ◽  
R. Martinez ◽  
...  

2004 ◽  
Vol 12 (18) ◽  
pp. 4803-4807 ◽  
Author(s):  
Jeffrey J. Hale ◽  
Lin Yan ◽  
William E. Neway ◽  
Richard Hajdu ◽  
James D. Bergstrom ◽  
...  

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