Publications de Maria Josefina Marcaida Lopez

Exploring New Nanopore Sensors from the Aerolysin Family

Matteo Dal Peraro, Maria Josefina Marcaida Lopez, Juan Francisco Bada Juarez

Aerolysin‐like proteins are a family of pore‐forming toxins with potential biotechnological applications as nanopore sensors for biomolecular detection and sequencing. Despite their conserved structural fold, the low sequence identity complicates sequence ...

Wiley2025

Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment

Matteo Dal Peraro, Luciano Andres Abriata, Maria Josefina Marcaida Lopez, Juan Francisco Bada Juarez, Jana Susanne Anton

Aerolysin is a beta-pore-forming toxin produced by most Aeromonas bacteria, which has attracted large attention in the field of nanopore sensing due to its narrow and charged pore lumen. Structurally similar proteins, belonging to the aerolysin-like family ...

AMER CHEMICAL SOC2025

The HP1 box of KAP1 organizes HP1α for silencing of endogenous retroviral elements in embryonic stem cells

Matteo Dal Peraro, Rudolf Hovius, Beat Fierz, Maria Josefina Marcaida Lopez

Repression of endogenous retroviral elements (ERVs) is facilitated by KAP1 (KRAB-associated protein 1)-containing complexes, however the underlying mechanism remains unclear. Here, we show that binding of KAP1 to the major component of the heterochromatin ...

Springer Science and Business Media LLC2025

Missense variants in CMS22 patients reveal that PREPL has both enzymatic and nonenzymatic functions

Matteo Dal Peraro, Maria Josefina Marcaida Lopez, Aleksandar Antanasijevic, Anastasia Theodoropoulou, Edoardo Cavani

Congenital myasthenic syndrome-22 (CMS22, OMIM 616224) is a rare genetic disorder caused by deleterious genetic variation in the prolyl endopeptidase-like (PREPL) gene. Previous reports have described patients with deletions and nonsense variants in PREPL, ...

American Society for Clinical Investigation2024

Structural characterization of Prolyl endopeptidase-like, a mitochondrial protein involved in congenital myasthenic syndrome-22

Matteo Dal Peraro, Maria Josefina Marcaida Lopez, Anastasia Theodoropoulou, Edoardo Cavani

SPRINGER2023

Using integrative structural biology for the identification of novel aerolysin-like pore forming toxins for nanopore sensing

Matteo Dal Peraro, Maria Josefina Marcaida Lopez, Fernando Augusto Teixeira Pinto Meireles, Juan Francisco Bada Juarez, Jana Susanne Anton

SPRINGER2023

Structure and dynamics of Toll immunoreceptor activation in the mosquito Aedes aegypti

Maria Josefina Marcaida Lopez

Aedes aegypti can act as a vector for viral pathogens but the mechanism of viral resistance and evolving host-pathogen tolerance are poorly understood. Here the authors structurally characterise a duplicated pair of interacting Toll immunoreceptors and the ...

Nature Research2022

Prolyl endopeptidase-like is a (thio)esterase involved in mitochondrial respiratory chain function

Matteo Dal Peraro, Maria Josefina Marcaida Lopez

Deficiency of the serine hydrolase prolyl endopeptidase-like (PREPL) causes a recessive metabolic disorder characterized by neonatal hypotonia, feeding difficulties, and growth hormone deficiency. The pathophysiology of PREPL deficiency and the physiologic ...

CELL PRESS2021

Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains

Françoise Gisou van der Goot Grunberg, Matteo Dal Peraro, Laurence Gouzi Abrami, Florence Pojer, Maria Josefina Marcaida Lopez, Sylvia Ho, Francisco De Magalhães Sarmento R De Mesquita, Muhammad Umair Anwar, Patrick Alain Sandoz, Martina Audagnotto

Acyl protein thioesterase APT2 interacts with membranes via its charged beta-tongue, becomes palmitoylated by ZDHHC3/7 and deforms the bilayer to extract substrate acyl chains. APT2 deacylation leads to its membrane release and degradation. ...

NATURE RESEARCH2021

The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain

Matteo Dal Peraro, Giorgio Elikem Tamo, Maria Josefina Marcaida Lopez, Ruedi Aebersold

The polyQ expansion in huntingtin protein (HTT) is the prime cause of Huntington's disease (HD). The recent cryoelectron microscopy (cryo-EM) structure of HTT-HAP40 complex provided the structural information on its HEAT-repeat domains. Here, we present an ...

CELL PRESS2020