Corinne Lasmézas

Corinne Lasmézas, Ph.D.


Business Phone: (561) 228-3456
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About Corinne Lasmézas

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Additional Positions:
Professor, Immunology and Microbial Science (IMS)
2015 – 2022 · Scripps Research
Joint Professor, Neuroscience
2015 – 2022 · Scripps Research
Professor, Infectious Diseases
2012 – 2015 · Scripps Research
Professor, Infectology
2005 – 2012 · Scripps Research

Research Profile

Neurodegenerative diseases

Our laboratory focuses on the study of neurodegenerative diseases, especially those linked to protein misfolding (protein misfolding neurodegenerative diseases, or PMNDs). These diseases comprise Alzheimer’s, Parkinson’s, Huntington’s, prion diseases, fronto-temporal dementia, and amyotrophic lateral sclerosis. None of them are curable. They are all due to host proteins loosing their natural, functional conformation and adopting a new shape that renders them neurotoxic and prone to aggregation.

Prion diseases constitute the prototypic PMND. These rapidly fatal neurodegenerative diseases affect humans and animals and are caused by infectious aggregates of the prion protein PrP, called prions. In humans, prions cause Creutzfeldt-Jakob disease. In animals, the recent epidemic of bovine spongiform encephalopathy in the United Kingdom has caused major turmoil throughout Europe, and later, in other countries such as Japan, Canada and the United States, because the bovine prion disease is transmissible to humans causing variant Creutzfeldt-Jakob disease. The transmissibility of the latter by blood transfusion created a novel public health issue.

Alzheimer’s and Parkinson’s diseases affect 5.8 and 1 Million people in the USA, respectively. Their incidence has steadily increased with an aging population, having a major impact on public health, society and the economy. Alzheimer’s disease is the 6th leading cause of death in developed countries. Amyotrophic lateral sclerosis (ALS or Lou Gehrig’s disease) is an orphan disease causing a progressive muscle weakness and paralysis, affecting an estimated 30,000 people in the USA.

In recent years, it has been discovered that aggregates of amyloidogenic proteins such as Ab, tau, a-synuclein or SOD-1 involved in Alzheimer’s, Parkinson diseases and amyotrophic lateral sclerosis, respectively, spread from cell to cell in culture and in the living organism similarly to PrP aggregates, showing “prion-like” behavior. There are other features common to these toxic proteins and the way they injure neurons (e.g. toxicity of low molecular weight aggregates, impairment of protein degradation mechanisms such as autophagy, mitochondrial distress).

Our aim is the development of novel, disease-modifying therapeutic approaches for protein misfolding neurodegenerative diseases. We think that this aim will be best achieved by intervention strategies based on targeting toxic protein aggregates, and blocking the neurodegenerative process to achieve neuroprotection. We are pursuing these goals by studying the underlying biology, defining therapeutic targets, identifying active molecules by high-throughput screening and developing lead compounds. The latter two tasks are performed in collaboration with our lead identification and chemist colleagues on campus.

Open Researcher and Contributor ID (ORCID)



Pα-syn* mitotoxicity is linked to MAPK activation and involves tau phosphorylation and aggregation at the mitochondria.
Neurobiology of disease. 124:248-262 [DOI] 10.1016/j.nbd.2018.11.015. [PMID] 30472299.
Identification of a highly neurotoxic α-synuclein species inducing mitochondrial damage and mitophagy in Parkinson’s disease.
Proceedings of the National Academy of Sciences of the United States of America. 115(11):E2634-E2643 [DOI] 10.1073/pnas.1713849115. [PMID] 29487216.
Identifying therapeutic targets and treatments in model systems.
Handbook of clinical neurology. 153:409-418 [DOI] 10.1016/B978-0-444-63945-5.00022-2. [PMID] 29887148.
Modeling Variant Creutzfeldt-Jakob Disease and Its Pathogenesis in Non-human Primates.
Food safety (Tokyo, Japan). 5(1):14-23 [DOI] 10.14252/foodsafetyfscj.2016034. [PMID] 32231924.
Neuronal death induced by misfolded prion protein is due to NAD+ depletion and can be relieved in vitro and in vivo by NAD+ replenishment.
Brain : a journal of neurology. 138(Pt 4):992-1008 [DOI] 10.1093/brain/awv002. [PMID] 25678560.
Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.
The EMBO journal. 34(1):4-19 [DOI] 10.15252/embj.201488896. [PMID] 25361606.
Unique drug screening approach for prion diseases identifies tacrolimus and astemizole as antiprion agents.
Proceedings of the National Academy of Sciences of the United States of America. 110(17):7044-9 [DOI] 10.1073/pnas.1303510110. [PMID] 23576755.
Highly neurotoxic monomeric α-helical prion protein.
Proceedings of the National Academy of Sciences of the United States of America. 109(8):3113-8 [DOI] 10.1073/pnas.1118090109. [PMID] 22323583.
Strain-specific role of RNAs in prion replication.
Journal of virology. 86(19):10494-504 [DOI] 10.1128/JVI.01286-12. [PMID] 22811520.
Early dysfunction of central 5-HT system in a murine model of bovine spongiform encephalopathy.
Neuroscience. 160(4):731-43 [DOI] 10.1016/j.neuroscience.2009.02.072. [PMID] 19285121.
Prion strain discrimination based on rapid in vivo amplification and analysis by the cell panel assay.
PloS one. 4(5) [DOI] 10.1371/journal.pone.0005730. [PMID] 19478942.
Atypical BSE (BASE) transmitted from asymptomatic aging cattle to a primate.
PloS one. 3(8) [DOI] 10.1371/journal.pone.0003017. [PMID] 18714385.
In vitro and in vivo neurotoxicity of prion protein oligomers.
PLoS pathogens. 3(8) [PMID] 17784787.
Toxic effects of intracerebral PrP antibody administration during the course of BSE infection in mice.
Prion. 1(3):198-206 [PMID] 19164902.
Of mice and men … and vCJD.
The Lancet. Neurology. 5(5):374-5 [PMID] 16632300.
Preclinical metabolic changes in mouse prion diseases detected by 1H-nuclear magnetic resonance spectroscopy.
Neuroreport. 17(1):89-93 [PMID] 16361957.
PrPTSE distribution in a primate model of variant, sporadic, and iatrogenic Creutzfeldt-Jakob disease.
Journal of virology. 79(22):14339-45 [PMID] 16254368.
Risk of oral infection with bovine spongiform encephalopathy agent in primates.
Lancet (London, England). 365(9461):781-3 [PMID] 15733719.
Knock-down of the 37-kDa/67-kDa laminin receptor in mouse brain by transgenic expression of specific antisense LRP RNA.
Transgenic research. 13(1):81-5 [PMID] 15070079.
Novel methods for disinfection of prion-contaminated medical devices.
Lancet (London, England). 364(9433):521-6 [PMID] 15302195.
Tissue distribution of bovine spongiform encephalopathy agent in primates after intravenous or oral infection.
Lancet (London, England). 363(9407):422-8 [PMID] 14962521.
A novel generation of heparan sulfate mimetics for the treatment of prion diseases.
The Journal of general virology. 84(Pt 9):2595-2603 [DOI] 10.1099/vir.0.19073-0. [PMID] 12917481.
Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP.
Biological chemistry. 384(2):243-6 [PMID] 12675517.
Evaluation of quinacrine treatment for prion diseases.
Journal of virology. 77(15):8462-9 [PMID] 12857915.
Putative functions of PrP(C).
British medical bulletin. 66:61-70 [PMID] 14522849.
The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells.
EMBO reports. 4(3):290-5 [PMID] 12634848.
Adaptation of the bovine spongiform encephalopathy agent to primates and comparison with Creutzfeldt– Jakob disease: implications for human health.
Proceedings of the National Academy of Sciences of the United States of America. 98(7):4142-7 [PMID] 11259641.
Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor.
The EMBO journal. 20(21):5876-86 [PMID] 11689428.
The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein.
The EMBO journal. 20(21):5863-75 [PMID] 11689427.
Neurotoxicity of the putative transmembrane domain of the prion protein.
Neurobiology of disease. 7(6 Pt B):644-56 [PMID] 11114262.
Role of spleen macrophages in the clearance of scrapie agent early in pathogenesis.
The Journal of pathology. 190(4):495-502 [PMID] 10700001.
Microglial cells respond to amyloidogenic PrP peptide by the production of inflammatory cytokines.
Neuroreport. 10(4):723-9 [PMID] 10208538.
New insight into abnormal prion protein using monoclonal antibodies.
Biochemical and biophysical research communications. 265(3):652-7 [PMID] 10600476.
Role of the 37 kDa laminin receptor precursor in the life cycle of prions.
Transfusion clinique et biologique : journal de la Societe francaise de transfusion sanguine. 6(1):7-16 [PMID] 10188208.
Ultrastructural localization of cellular prion protein (PrPc) at the neuromuscular junction.
Journal of neuroscience research. 55(2):261-7 [PMID] 9972829.
Distribution and submicroscopic immunogold localization of cellular prion protein (PrPc) in extracerebral tissues.
Cell and tissue research. 292(1):77-84 [PMID] 9506914.
Gene expression in scrapie. Cloning of a new scrapie-responsive gene and the identification of increased levels of seven other mRNA transcripts.
The Journal of biological chemistry. 273(13):7691-7 [PMID] 9516475.
Recombinant human growth hormone and insulin-like growth factor I induce PrP gene expression in PC12 cells.
Biochemical and biophysical research communications. 196(3):1163-9 [PMID] 7902706.


Ph.D. in Neurosciences
1995 · Pierre and Marie Curie University
Doctor of Veterinary Medicine
1993 · University of Toulouse, Toulouse National Veterinary School
Master's of Science in Neurosciences
1992 · Pierre and Marie Curie University
Diploma in Aeronautic and Space Medicine
1990 · University of Toulouse, University of Medicine

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(561) 228-3456
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Location B213