Protein folds in Infectious and neurodegenerative diseases
Aussois (French Alps), France, April 25-29, 2009
Deadline for application: February 28, 2009
Chairperson: Alasdair C. Steven
Laboratory of Structural Biology, NIAMS, Bldg 50, Room 1517, 50 South Drive MSC 8025,
N.I.H., Bethesda, MD 20892-8025, USA
Phone: +00 1 301 496 01 32 - Fax: +00 1 301 443 76 51
Mail: stevena@mail.nih.gov
Vice-Chairperson: Andrey V. Kajava
Centre de Recherches de Biochimie Macromoléculaire, UMR 5237 CNRS,
1919 Route de Mende, 34293 Montpellier, Cedex 5, France
Phone: +33 4 67 61 33 64 – Fax: +33 4 67 52 15 59
Mail: andrey.kajava@crbm.cnrs.fr
The past few years have seen an efflorescence of information on the 3D structures of virulence factors, toxins, and adhesins of pathogenic bacteria and viruses, as well as of prion and amyloid fibrils. The emergence of this structural information can be attributed to the improved protein expression and crystallization strategies as well as applications of emerging experimental techniques, including cryo-electron microscopy, scanning transmission electron microscopy, solid-state NMR spectroscopy, and electron paramagnetic resonance spectroscopy. It has also become apparent that many polypeptides are “natively” unfolded under physiological conditions, and this class includes precursors to many of the pathogenic proteins outlined above. In addition to the recent revolutionary progress on a conceptual level, this area of research has a vitally important medical dimension related to the fact that the structures of pathogenic folds are key to developing new therapeutics for neurodegenerative disease and infectious diseases of bacterial and viral origins.
This conference will focus on the structures, stability, functions and pathogenicity of these folds as well as strategies for developing therapeutics and vaccines. It will bring together a critical mass of internationally recognized experts who will lead discussions that are intended to distinguish the characteristic structural features of the pathogenic folds, chart their notable diversity, dissect their sequence-structure relationships, and explore novel pathways to drug and vaccine discovery.
In the context of today’s emerging infectious threats and an increasing proportion of the population of the world, which is affected by the age-related neurodegenerative diseases as life-expectancy increases, we anticipate, by organization of this Jacques Monod conference, to generate a large interest among scientific and medical community as well as pharmaceutical companies.
The conference will have four sessions, focussing respectively on:
- The structures of virulence- and infectivity-associated proteins of microbial pathogens and their commonality with amyloid and prion fibrils; structure-based strategies of drug and vaccine development.
- The process and end-products of amyloidogenesis; new approaches to obtain atomic-level structural details of amyloid fibrils; prediction of amyloidogenic regions in proteins; strategies for the development of inhibitors of fibrillogenesis.
- Viral surface proteins; their roles in membrane fusion and infection; survey of structural properties of pathogenic and toxic proteins in general.
- The properties of natively unfolded protein regions as precursors of disease-related folds.
Invited speakers
(provisional titles)
BUCHANAN Susan (Bethesda, USA)
Secretion of virulence factors by bacterial autotransporters
CLARK Patricia (Notre Dame, USA)
The autotransporter beta-helix: a powerful tool for bacterial pathogenesis
DESSEN Andrea (Grenoble, France)
Sortase-mediated pilus biogenesis in Streptococcus pneumoniae
JANIN Joel (Orsay, France)
Viral capsid assembly and evolution from a structural perspective
KAJAVA Andrey (Montpellier, France)
Folds of beta-solenoid proteins and amyloid fibrils
LANGEN Ralf (Los Angeles, USA)
Mechamisms of amyloid protein misfolding studied by site-directed spin labeling
LASHUEL Hilal (Lausanne, Switzerland)
Chemical and biophysical approaches to understanding the molecular mechanisms protein aggregation and toxicity.
LETELLIER Lucienne (Paris, France)
Bacteriophage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities
LONGHI Sonia (Marseille, France)
Structural disorder in the replicative complex of measles virus: implications for pathogenicity
MANDELKOW Eckhard (Hamburg, Germany)
Tau protein: conformation and aggregation in Alzheimer’s disease
MEIER Beat (Zürich, Switzerland)
Comparing the structure of infectious and non-infectious HET-s amyloids: an NMR study
MITRAKI Anna (Heraklion, Greece)
Beta-structured fibrous folds from viruses and connection to amyloid fibrils
MURZIN Alexey (Cambridge, UK)
Metamorphic proteins
NUSSINOV Ruth (Frederick, USA/TelAviv, Israel)
Modeling amyloid conformations and toxic ion channels
POUPON Anne (Nouzilly, France)
Disorder predictions can be used to predict genetic constructs with improved expression, solubility and stability
REDFORD Sheena (Leeds, UK)
Molecular insights into beta-2-microglobulin assembly into amyloid
REY Felix (Paris, France)
Several structural classes of viral membrane fusion proteins: comparative studies provide insights into their mechanism of action
REZAEI Human (Jouy-en-Josas, France)
Conformational Dynamics and oligomerization pathways of prion protein
ROSSMANN Michael (West Lafayette, USA)
Viruses with jelly roll folds in their major capsid protein
RUIGROK Rob (Grenoble, France)
Unfolded domains in the polymerase cofactor of rhabdoviruses
SAUPE Sven (Bordeaux, France)
Infectious and non-infectious amyloids of the HET-s prion protein of the fungus Podospora anserina and its homolog in Fusarium graminearum
SECKLER Robert (Potsdam, Germany)
Parallel beta-helices in bacteriophage adhesions
SERPELL Louise (Sussex, UK)
Structural basis of protein misfolding
STEVEN Alasdair (Bethesda, USA)
Electron microscopy of amyloid fibril polymorphisms
SUSSMAN Joel (Rehovot, Israel)
Intrinsically disordered proteins: Possible biological roles?
TOMPA Peter (Budapest, Hungary)
Role of structural disorder in the formation of amyloids
UVERSKY Vladimir(Indianapolis, USA)
Natively unfolded proteins in amyloidoses and related pathologies
VILLERET Vincent (Lille, France)
Beta-Solenoid motifs in bacterial virulence factors secreted by the Two-Partner secretion pathway
Deadline for application: February 28, 2009
Registration fee (including board and lodging)
385 € for PhD students
575 € for other participants
Application for registration
The total number of participants is limited to about 115 and all participants are expected to attend for the whole duration of the conference. Selection is made on the basis of the affinity of potential participants with the topics of the conference. Scientists and PhD Students interested in the meeting should send:
- their curriculum vitae
- the list of their main publications for the 3 last years
- the abstract of their presentation
to the Chairperson of the conference before the deadline. After it, the chairman will select the participants. Except in some particular cases approved by the Chairperson, it is recommended that all selected participants present their work during the conference, either in poster form or by a brief in- session talk. The organizers choose the form in which the presentations are made. No payment will be sent with application. Information on how and when to pay will be mailed in due time to those selected.