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Structural and functional studies of the Golgi Re-Assembly and Stacking Protein (GRASP) from Cryptococcus neoformans

Grant number: 12/13309-7
Support type:Scholarships in Brazil - Doctorate (Direct)
Effective date (Start): September 01, 2012
Effective date (End): February 17, 2018
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal researcher:Antonio José da Costa Filho
Grantee:Luis Felipe Santos Mendes
Home Institution: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Associated scholarship(s):16/09676-5 - Nuclear magnetic resonance studies of the Golgi reassembly and stacking protein from C. neoformans, BE.EP.DD


The secretion of virulence factors is a critical mechanism for the establishment of criptococose, a disease that along with candidiasis represent opportunistic fungi infection in HIV patients. Criptococose is a disease caused by Cryptococcus neoformans, which appears to be the only pathogen species from the Cryptococcus genus. The virulence of this pathogen seems to be related to the external capsule formed by a variety of intracellular biomolecules that appear to reach the extracellular space by unconventional methods of secretion. Despite the lack of detailed information about these methods, it is known that they depend on a protein called Golgi Re-Assembly and Stacking Protein (GRASP). GRASPs have been implicated in a variety of functions, including unconventional mechanisms of secretion and assembling/organization of the Golgi apparatus. However, its exact role in each cases can still benefit from structural and functional results at a molecular level. This proposal is included in this context aiming at generating results that will enable a structural/function correlation in GRASP from C. neoformans (CnGRASP). For this purpose we will use a variety of experimental techniques in molecular biophysics ranging from GRASP structural determination by X-ray diffraction (until now only the GRASP domain from the human orthologue GRAPS55 was obtained) and studies covering GRASP interactions with natural ligands, such as GXM, and biological membrane models using spectroscopic techniques, such as Electron Magnetic Resonance (EMR). (AU)

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Scientific publications (5)
(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)
ALVAREZ, NATALIA; MENDES, LUIS F. S.; GABRIELA KRAMER, M.; TORRE, MARIA H.; COSTA-FILHO, ANTONIO J.; ELLENA, JAVIER; FACCHIN, GIANELLA. Development of copper(II)-diimine-iminodiacetate mixed ligand complexes as potential antitumor agents. Inorganica Chimica Acta, v. 483, p. 61-70, NOV 1 2018. Web of Science Citations: 11.
FONTANA, N. A.; FONSECA-MALDONADO, R.; MENDES, L. F. S.; MELEIRO, L. P.; COSTA-FILHO, A. J. The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior. SCIENTIFIC REPORTS, v. 8, OCT 24 2018. Web of Science Citations: 3.
MENDES, LUIS F. S.; BASSO, LUIS G. M.; KUMAGAI, PATRICIA S.; FONSECA-MALDONADO, RAQUEL; COSTA-FILHO, ANTONIO J. Disorder-to-order transitions in the molten globule-like Golgi Reassembly and Stacking Protein. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, v. 1862, n. 4, p. 855-865, APR 2018. Web of Science Citations: 4.
MICHELETTO, MARIANA C.; MENDES, LUIS F. S.; BASSO, LUIS G. M.; FONSECA-MALDONADO, RAQUEL G.; COSTA-FILHO, ANTONIO J. Lipid membranes and acyl-CoA esters promote opposing effects on acyl-CoA binding protein structure and stability. International Journal of Biological Macromolecules, v. 102, p. 284-293, SEP 2017. Web of Science Citations: 2.
MENDES, LUIS F. S.; GARCIA, ASSUERO F.; KUMAGAI, PATRICIA S.; DE MORAIS, FABIO R.; MELO, FERNANDO A.; KMETZSCH, LIVIA; VAINSTEIN, MARILENE H.; RODRIGUES, MARCIO L.; COSTA-FILHO, ANTONIO J. New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution. SCIENTIFIC REPORTS, v. 6, JUL 20 2016. Web of Science Citations: 6.

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