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X-WR-CALDESC:Events for BIFI -  - Institute for Biocomputation and Physics of Complex Systems
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DTSTART;TZID=Europe/Madrid:20260417T123000
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DTSTAMP:20261015T132903
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SUMMARY:BIFI-Talk: Marcelo Guerín del IBMB-CSIC\, Barcelona
DESCRIPTION:[vc_row][vc_column][vc_column_text css=”.vc_custom_1776147804327{margin-bottom: 0px !important;}”]BIFI-Talk: Marcelo Guerín del IBMB-CSIC\, Barcelona \nTítulo: Structural basis of glycan diversity in biological systems \nAbstract \nGlycosylation is one of the most prevalent posttranslational modifications of proteins and lipids. It markedly influences their structure and function\, and plays a central role in nearly every aspect of biology. A deeper understanding of glycosylation —and the ability to precisely and rationally modulate it— are essential for advancing our fundamental biological knowledge and for developing innovative therapeutics across a wide range of human diseases. \nIn this talk\, I will present our recent findings and advances in the following research areas: \n(i) Bacterial cell envelope biosynthesis and remodeling\, and its impact in host-pathogen interactions and vaccine development. Surface glycan polymers are crucial virulence factors of pathogenic bacteria. We identified enzymatic machineries assembling these polymers\, key for developing novel antimicrobials and enzyme-based vaccine synthesis protocols (Sci. Adv. 7:eabj4565\, 2021; Nat. Chem. Biol. 19:795-796\, 2023; Nat. Commun. 14:6694\, 2023; Nat. Commun. 15:5740\, 2024; Nat. Chem. Biol. 21:120-130\, 2025). \n(ii) Unveiling the role of gut microbiota glycan processing machinery in human health and disease. The gut symbiotic microbiota provides the complementary enzymatic machinery necessary to orchestrate the depolymerization of glycan structures into their sugar components that otherwise could not be processed by the host. We identified novel enzymatic activities and substrate specificities associated to N- and O-linked glycans breakdown\, including FucOB from Akkermansia muciniphila capable of converting universal O red blood cells and human kidney tissues into the rare Bombay phenotype. \n(iii) Glycoprotein folding and quality-control mechanisms in human diseases. The endoplasmic reticulum (ER) glycoprotein folding quality control protein machineries survey glycoprotein folding in the early secretory pathway. We unveiled the structural and mechanistic aspects of the ER folding sensor UDP-glucose glycoprotein glucosyltransferase (UGGT). This allows us to define the molecular basis of a novel congenital disorder of glycosylation (CDG) disease\, characterized by significant neurological dysfunction. \nIn our research\, we are using a truly multidisciplinary approach. To determine high-resolution structures\, we employ X-ray crystallography and single particle cryo-electron microscopy. To obtain mechanistic insight\, we combine structural studies with molecular biology\, protein/membrane biochemistry/biophysics and AI-driven computational methods. These approaches are frequently integrated with collaborative efforts in genomics\, transcriptomics\, proteomics\, cell biology\, synthetic organic chemistry and NMR spectroscopy. \n[/vc_column_text][/vc_column][/vc_row]
URL:https://bifi.es/schedule/bifi-talk-marcelo-guerin-del-ibmb-csic-barcelona/
LOCATION:Salon de actos del edificio I+D
CATEGORIES:Events
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DTSTART;TZID=Europe/Madrid:20261009T123000
DTEND;TZID=Europe/Madrid:20261009T140000
DTSTAMP:20261015T132903
CREATED:20261008T100105Z
LAST-MODIFIED:20261008T100105Z
UID:10865-1791549000-1791554400@bifi.es
SUMMARY:BIFI TALK: Andrea Ilari\, Istituto di Biologia e Patologia Molecolari\, IBPM of CNR  c/o Dip. Scienze Biochimiche Università Sapienza\,Roma
DESCRIPTION:[vc_row][vc_column][vc_column_text css=”.vc_custom_1791453588217{margin-bottom: 0px !important;}”]BIFI TALK: Andrea Ilari\, Istituto di Biologia e Patologia Molecolari\, IBPM of CNR  c/o Dip. Scienze Biochimiche Università Sapienza\, P.le Aldo Moro 5\, 00185 Roma \nTítulo: Exploiting a Druggable E2 Ubiquitin Conjugating Enzyme and an E3 Ligase for PROTAC-Mediated Degradation of Trypanothione Reductase in Leishmania \nAbstract \nLeishmaniasis is a neglected tropical disease affecting up to one million people annually according to the World Health Organization. Visceral leishmaniasis\, caused by Leishmania infantum\, is the most severe form of the disease and can be fatal if left untreated. Current therapies are limited by toxicity\, variable efficacy\, lengthy treatment regimens\, and the emergence of drug resistance [1]. \nThe parasite survives the oxidative burst generated by host macrophages through a unique trypanothione-based redox system\, whose central enzyme\, trypanothione reductase (TR)\, maintains trypanothione in its reduced state. Owing to its essential role in parasite survival\, absence in humans\, and favorable druggability profile\, TR has long been considered an attractive therapeutic target. However\, despite decades of research\, no TR inhibitors have advanced to clinical development\, mainly because of insufficient efficacy and safety concerns [2]. \nTargeted protein degradation has recently emerged as an alternative therapeutic strategy capable of eliminating\, rather than inhibiting\, disease-relevant proteins. PROteolysis TArgeting Chimeras (PROTACs) are bifunctional molecules that induce ubiquitination and subsequent proteasomal degradation of a target protein by recruiting components of the ubiquitin–proteasome system (UPS) [3]. As first step\, we developed TR-targeting PROTACs designed to recruit a putative Leishmania E3 ligase\, but their activity was modest and the recruited E3 remains poorly characterized. To overcome these limitations\, we propose an innovative E2-recruiting PROTAC strategy that bypasses the requirement for a defined E3 ligase. As a first step\, we structurally and functionally characterized a Leishmania major ubiquitin-conjugating enzyme (E2). Crystallographic fragment screening identified potential ligandable sites on the enzyme\, while DeepFrag-guided fragment expansion and AutoDock Vina docking were employed to generate and prioritize E2-binding chemotypes. Together\, these studies establish the molecular framework for the rational development of E2-recruiting PROTACs targeting TR and open new opportunities for exploiting the ubiquitin–proteasome system in antileishmanial drug discovery [4]. \nReferences \n[1] S. Pradhan\, R. A. Schwartz\, A. Patil\, S. Grabbe\, and M. Goldust\, Clin Exp Dermatol\, 2022\, 47\, 516.\n[2] T. Battista\, G. Colotti\, A. Ilari\, and A. Fiorillo\, Molecules\, 2020. 25\, 1924.\n[3] S. Gu\, D. Cui\, X. Chen\, X. Xiong\, and Y. Zhao\, BioEssays\, 2018\, 40\, e1700247.\n[4] C. Exertier\, L. Antonelli\, A. Liuzzi\, M. Ruffa\, V. Brufani\, G. Colotti\, A. Fiorillo\, A. Ilari; ACS Omega 2026; https://doi.org/10.1021/acsomega.6c05158[/vc_column_text][/vc_column][/vc_row]
URL:https://bifi.es/schedule/bifi-talk-andrea-ilari-istituto-di-biologia-e-patologia-molecolari-ibpm-of-cnr-c-o-dip-scienze-biochimiche-universita-sapienzaroma/
LOCATION:Edificio Institutos I+D\, Mariano Esquillor\, 50018 Zaragoza\, Zaragoza\, Zaragoza\, 50018\, España
CATEGORIES:Events
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