Fucose metabolism, alpha-L-fucosidases and fucosyltransferases: enzymatic characterization, mechanism of catalysis and physiological role

• Grant number: 14/15732-0
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• Start date: March 01, 2015
• End date: April 30, 2018
• Field of knowledge: Biological Sciences - Biochemistry - Enzymology
• Principal Investigator: Adriana Rios Lopes
• Grantee: Natalia Nappi Perrella
• Host Institution: Instituto Butantan. Secretaria da Saúde (São Paulo - Estado). São Paulo , SP, Brazil
• Associated scholarship(s): 15/11354-3 - Expression and site-directed mutagenesis of Arachnida alpha-L-fucosidases, BE.EP.DD

Abstract

Carbohydrates are diverse and complex molecules and are 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 is 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 been characterized in several species of snails. Recently, we described the presence of these enzymes in the digestive system of some species of arthropods as the tick Amblyomma cajennense, the spider Nephilengys cruentata and the gastropod Biomphalaria glabrata. This project will allow a detailed study of the metabolism of fucose in Arthropoda by quantifying the expression of fucosyltransferases and fucosidases in different tissues of animals by qPCR. The capacity of the digestive tissue to fucosilate carbohydrates and proteins will be accessed by the activity of transglycosylation of fucosidases from these animals, and the evaluation of fucosylation activity by detecting the presence /activity of fucosyltransferases. Furthermore, the study of the catalytic mechanism and specificity of fucosidases through specific mutagenesis will be held. (AU)

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. (14/15732-0, 15/23745-7, 15/11354-3)