Publications by Mircea Ioan Iacovache

Ultrasensitive Label-Free Detection of Protein–Membrane Interaction Exemplified by Toxin-Liposome Insertion

Mircea Ioan Iacovache, Matteo Dal Peraro, Sylvie Roke, Halil Ibrahim Okur, Chan Cao, Tereza Schönfeldová

Measuring the high-affinity binding of proteins to liposome membranes remains a challenge. Here, we show an ultrasensitive and direct detection of protein binding to liposome membranes using high throughput second harmonic scattering (SHS). Perfringolysin ...

2022

Cell-free reconstitution reveals centriole cartwheel assembly mechanisms

Henning Paul-Julius Stahlberg, Pierre Gönczy, Mircea Ioan Iacovache, Virginie Hamel, Isabelle Fluckiger, Paul Guichard, Veronika Nemcíková Villímová, Niccolo Banterle

How cellular organelles assemble is a fundamental question in biology. The centriole organelle organizes around a nine-foldsymmetrical cartwheel structure typically 100 nm high comprising a stack of rings that each accommodates nine homodimers of SAS-6 pro ...

Springer Nature2017

Revealing Assembly of a Pore-Forming Complex Using Single-Cell Kinetic Analysis and Modeling

Felix Naef, Daniel Boss, Mirko Bischofberger, Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache

Many biological processes depend on the sequential assembly of protein complexes. However, studying the kinetics of such processes by direct methods is often not feasible. As an important class of such protein complexes, pore-forming toxins start their jou ...

Elsevier2016

Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process

Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache, Matteo Dal Peraro, Nuria Cirauqui Diaz

Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-s ...

Nature Publishing Group2016

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism

Henning Paul-Julius Stahlberg, Matteo Thomas Degiacomi, Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache, Matteo Dal Peraro

Aerolysin is the founding member of a superfamily of (beta-pore-forming toxins whose pore structure is unknown. We have combined X-ray crystallography, cryo-EM, molecular dynamics and computational modeling to determine the structures of aerolysin mutants ...

Nature Publishing Group2013

The Molecular Assembly of the Aerolysin Pore Reveals a Unique Swirling Membrane-Insertion Mechanism

Matteo Thomas Degiacomi, Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache, Matteo Dal Peraro

Cell Press2013

Pathogenic Pore-Forming Proteins: Function and Host Response

Mirko Bischofberger, Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache

Organisms from all kingdoms produce pore-forming proteins, with the best-characterized being of bacterial origin. The last decade of research has revealed that the channels formed by these proteins can be very diverse, thus differentially affecting target ...

Cell Press2012

Monalysin, a novel ß-pore-forming toxin from the Drosophila pathogen Pseudomonas entomophila, contributes to host intestinal damage and lethality

Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache, Rodrigo Manuel Gonzalez, Bruno Lemaitre, Onya Opota

Pseudomonas entomophila is an entomopathogenic bacterium that infects and kills Drosophila. P. entomophila pathogenicity is linked to its ability to cause irreversible damages to the Drosophila gut, preventing epithelium renewal and repair. Here we report ...

2011

Extending the aerolysin family: from bacteria to vertebrates

Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache

A number of bacterial virulence factors have been observed to adopt structures similar to that of aerolysin, the principal toxin of Aeromonas species. However, a comprehensive description of architecture and structure of the aerolysin-like superfamily has ...

Public Library of Science2011

Dual Chaperone Role of the C-Terminal Propeptide in Folding and Oligomerization of the Pore-Forming Toxin Aerolysin

Matteo Thomas Degiacomi, Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache, Matteo Dal Peraro, Sylvia Ho

Throughout evolution, one of the most ancient forms of aggression between cells or organisms has been the production of proteins or peptides affecting the permeability of the target cell membrane. This class of virulence factors includes the largest family ...

2011

Folding and Structure of the Pore Forming Toxin Aerolysin

Mircea Ioan Iacovache

The first obstacle encountered by a bacterial pathogen once inside the host is the plasma membrane surrounding the target cells. Throughout evolution bacteria has acquired and maintained genes that upon stimulation express proteins capable of damaging the ...

EPFL2011

Pore formation: an ancient yet complex form of attack

Françoise Gisou van der Goot Grunberg, Mircea Ioan Iacovache

Bacteria, as well as higher organisms such as sea anemones or earthworms, have developed sophisticated virulence factors such as the pore-forming toxins (PFTs) to mount their attack against the host. One of the most fascinating aspects of PFTs is that they ...

2008