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Expression and site-directed mutagenesis of Arachnida alpha-L-fucosidases

Grant number: 15/11354-3
Support type:Scholarships abroad - Research Internship - Doctorate (Direct)
Effective date (Start): March 14, 2016
Effective date (End): September 13, 2016
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal researcher:Adriana Rios Lopes
Grantee:Natalia Nappi Perrella
Supervisor abroad: Stephen George Withers
Home Institution: Instituto Butantan. Secretaria da Saúde (São Paulo - Estado). São Paulo , SP, Brazil
Research place: University of British Columbia (UBC), Canada  
Associated to the scholarship:14/15732-0 - Fucose metabolism, alpha-L-fucosidases and fucosyltransferases: enzymatic characterization, mechanism of catalysis and physiological role, BP.DD

Abstract

Carbohydrates are diverse and complex molecules involved in many biological functions in living organisms. L-Fucose is a constituent of many glycoconjugates synthesized by microorganisms, plants and animals. Glycoconjugates present on mammalian cell surface are related to a number of physiological and pathological processes including: cell-cell adhesion, cell differentiation, immune response, fertilization, viral and bacterial infection and, progression of tumors. The Alpha-L-fucosidases are glycoside hydrolases which catalyze the hydrolysis of glycosidic bonds between a residue of fucose and other molecules. The absence of this enzyme is associated with a number of shortcomings and pathological conditions, including: fucosidosis, cystic fibrosis, cancer and inflammation. Some digestive fucosidases has been characterized in several species of snails. Recently, we described the presence of fucosidase in the digestive system of the gastropod Biomphalaria glabrata and from some species of arthropods such as the tick Amblyomma cajennense and the spider Nephilengys cruentata. Some results indicate that fucosidases may have a defensive role against pathogen infection (MORETI et al., 2013). Transcriptomic and proteomic analysis of the arthropods we are studying allowed alignment analysis with human and bacterial ±-L-fucosidases. These alignments showed that the nucleophile is conserved along all fucosidases and suggest that Arthropoda fucosidases have an acid/base catalytic residue identical to the human fucosidase. However, Shaikh and colleagues (2013) have pointed out that bacterial fucosidases don´t have a conserved acid/base catalytic residue. Some of our results indicate that ticks and spiders present fucosidases with distinct specificities and expression patterns possibly due to very distinct diets. This project will allow a detailed study of the catalytic mechanism and specificity of Arthropoda fucosidases through site-specific mutagenesis and kinetic analysis of the resultant mutant proteins. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
PERRELLA, NATALIA N.; WITHERS, STEPHEN G.; LOPES, ADRIANA R. Identity and role of the non-conserved acid/base catalytic residue in the GH29 fucosidase from the spider Nephilingis cruentata. GLYCOBIOLOGY, v. 28, n. 12, p. 925-932, DEC 2018. Web of Science Citations: 1.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.