scholarly journals In silico identification and Bayesian phylogenetic analysis of multiple new mammalian kallikrein gene families

Genomics ◽  
2006 ◽  
Vol 88 (5) ◽  
pp. 591-599 ◽  
Author(s):  
Marc B. Elliott ◽  
David M. Irwin ◽  
Eleftherios P. Diamandis
PLoS ONE ◽  
2016 ◽  
Vol 11 (2) ◽  
pp. e0148390 ◽  
Author(s):  
Andrea Figueroa-Montiel ◽  
Marco A. Ramos ◽  
Rosa E. Mares ◽  
Salvador Dueñas ◽  
Genaro Pimienta ◽  
...  

2014 ◽  
Vol 13 (2) ◽  
pp. 211-225 ◽  
Author(s):  
Kumar Mohanta Tapan ◽  
Malnoy Mickael ◽  
Mohanta Nibedita ◽  
Nagamangala Kanchiswamy Chidananda

2020 ◽  
Vol 56 (5) ◽  
pp. 572-579
Author(s):  
E. A. Istomina ◽  
M. P. Slezina ◽  
A. S. Kovtun ◽  
T. I. Odintsova

2017 ◽  
Vol 39 (3) ◽  
pp. 320-332
Author(s):  
Chu Duc Ha ◽  
Kris A.G. Wyckhuys ◽  
Le Tien Dung

Plant lectins, a superfamily of glycan-binding proteins, play important roles in various biological processes, including plant defense and cell signaling. Until now, little or no research has been carried out on lectins in cassava (Manihot esculenta Crantz); a prime food, feed and bio-energy crop in the tropics to sub-tropics. In this study, we identified 5 homologous genes encoding class V chitinases (CRA) and 17 genes encoding hevein (Hvi) domains in total and annotated them in the cassava genome. The large size of MeCRA and MeHvi genes possibly resulted from tandem duplication events, directly linked to the expansion of CRA and hevein gene families. Phylogenetic analysis showed 3 distinct groups of hevein genes with their typical gene organization. The most common motif of gene structure of MeCRA family was recorded to be 2 exons/1 intron. Promoter analysis revealed that most of the members of lectin gene families are assumed to be responsive to light conditions and are expressed in specific for particular organs or plant tissues. The presence of hormonal- and/or stress-responsive elements in the promoter regions of all lectin genes indicated their involvement in the crop’s stress response and plant signaling. Since most members of CRA and hevein family were strongly expressed in various major tissues/organs, products of those lectin genes may play important roles in the development of cassava plants, especially in plant defense system.   Citation: Chu Duc Ha, Wyckhuys K. A. G., Le Tien Dung, 2017. In silico identification and characterlization of the lectin gene families in cassava (Manihot esculenta Crantz). Tap chi Sinh hoc, 39(3): 320-332. DOI: 10.15625/0866-7160/v39n3.9185 *Corresponding author: [email protected]; [email protected] Received 25 January 2017, accepted 20 August 2017 


2020 ◽  
Vol 17 (4) ◽  
pp. 342-351
Author(s):  
Sergio A. Durán-Pérez ◽  
José G. Rendón-Maldonado ◽  
Lucio de Jesús Hernandez-Diaz ◽  
Annete I. Apodaca-Medina ◽  
Maribel Jiménez-Edeza ◽  
...  

Background: The protozoan Giardia duodenalis, which causes giardiasis, is an intestinal parasite that commonly affects humans, mainly pre-school children. Although there are asymptomatic cases, the main clinical features are chronic and acute diarrhea, nausea, abdominal pain, and malabsorption syndrome. Little is currently known about the virulence of the parasite, but some cases of chronic gastrointestinal alterations post-infection have been reported even when the infection was asymptomatic, suggesting that the cathepsin L proteases of the parasite may be involved in the damage at the level of the gastrointestinal mucosa. Objective: The aim of this study was the in silico identification and characterization of extracellular cathepsin L proteases in the proteome of G. duodenalis. Methods: The NP_001903 sequence of cathepsin L protease from Homo sapienswas searched against the Giardia duodenalisproteome. The subcellular localization of Giardia duodenaliscathepsin L proteases was performed in the DeepLoc-1.0 server. The construction of a phylogenetic tree of the extracellular proteins was carried out using the Molecular Evolutionary Genetics Analysis software (MEGA X). The Robetta server was used for the construction of the three-dimensional models. The search for possible inhibitors of the extracellular cathepsin L proteases of Giardia duodenaliswas performed by entering the three-dimensional structures in the FINDSITEcomb drug discovery tool. Results: Based on the amino acid sequence of cathepsin L from Homo sapiens, 8 protein sequences were identified that have in their modular structure the Pept_C1A domain characteristic of cathepsins and two of these proteins (XP_001704423 and XP_001704424) are located extracellularly. Threedimensional models were designed for both extracellular proteins and several inhibitory ligands with a score greater than 0.9 were identified. In vitrostudies are required to corroborate if these two extracellular proteins play a role in the virulence of Giardia duodenalisand to discover ligands that may be useful as therapeutic targets that interfere in the mechanism of pathogenesis generated by the parasite. Conclusion: In silicoanalysis identified two proteins in the Giardia duodenalisprotein repertoire whose characteristics allowed them to be classified as cathepsin L proteases, which may be secreted into the extracellular medium to act as virulence factors. Three-dimensional models of both proteins allowed the identification of inhibitory ligands with a high score. The results suggest that administration of those compounds might be used to block the endopeptidase activity of the extracellular cathepsin L proteases, interfering with the mechanisms of pathogenesis of the protozoan parasite Giardia duodenalis.


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