Main findings

 

Role of glycolipid receptors in HIV tropism and fusion mechanism (GalCer, Gb3, GM3)

Galactosyl ceramide (or a closely related molecule) is the receptor for human immunodeficiency virus type 1 on human colon epithelial HT29 cells. 

Yahi N, Baghdiguian S, Moreau H, Fantini J. J Virol. 1992 Aug;66(8):4848-54.

 

Infection of colonic epithelial cell lines by type 1 human immunodeficiency virus is associated with cell surface expression of galactosylceramide, a potential alternative gp120 receptor.

Fantini J, Cook DG, Nathanson N, Spitalnik SL, Gonzalez-Scarano F. Proc Natl Acad Sci U S A. 1993 Apr 1;90(7):2700-4.

 

Human erythrocyte glycosphingolipids as alternative cofactors for human immunodeficiency virus type 1 (HIV-1) entry: evidence for CD4-induced interactions between HIV-1 gp120 and reconstituted membrane microdomains of glycosphingolipids (Gb3 and GM3).

Hammache D, Yahi N, Maresca M, Piéroni G, Fantini J. J Virol. 1999 Jun;73(6):5244-8.

 

Consensus sphingolipid-binding domain (SBD) in proteins

Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins.

 Mahfoud R, Garmy N, Maresca M, Yahi N, Puigserver A, Fantini J. J Biol Chem. 2002 Mar 29;277(13):11292-6.

 

How sphingolipids bind and shape proteins: molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains.

 Fantini J. Cell Mol Life Sci. 2003 Jun;60(6):1027-32. 

 

Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells.

Fantini J, Garmy N, Yahi N. Biochemistry. 2006 Sep 12;45(36):10957-62.

 

The glycosphingolipid MacCer promotes synaptic bouton formation in Drosophila by interacting with Wnt.

 Huang Y, Huang S, Di Scala C, Wang Q, Wandall HH, Fantini J, Zhang YQ.  Elife. 2018 Oct 25;7. 

 

Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B. Flores A, Ramirez-Franco J, Desplantes R, Debreux K, Ferracci G, Wernert F, Blanchard MP, Maulet Y, Youssouf F, Sangiardi M, Iborra C, Popoff MR, Seagar M, Fantini J, Lévêque C, El Far O.   Proc Natl Acad Sci U S A. 2019 Sep 3;116(36):18098-18108. 

 

 

Molecular basis of lipid raft domains formation

Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases.

 Fantini J, Garmy N, Mahfoud R, Yahi N. Expert Rev Mol Med. 2002 Dec 20;4(27):1-22.

 

Interaction of proteins with lipid rafts through glycolipid-binding domains: biochemical background and potential therapeutic applications.

 Fantini J. Curr Med Chem. 2007;14(27):2911-7. 

 

Cholesterol binding domains in membrane proteins (CARC, tilted and mirror domains)

The fusogenic tilted peptide (67-78) of α-synuclein is a cholesterol binding domain.

Fantini J, Carlus D, Yahi N. Biochim Biophys Acta. 2011 Oct;1808(10):2343-51.

 

Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor.

Baier CJ, Fantini J, Barrantes FJ. Sci Rep. 2011;1:69.

 

How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains.

Fantini J, Barrantes FJ. Front Physiol. 2013 Feb 28;4:31. 

 

A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes.

Fantini J, Di Scala C, Evans LS, Williamson PT, Barrantes FJ. Sci Rep. 2016 Feb 26;6:21907. 

 

Molecular mechanisms of protein-cholesterol interactions in plasma membranes: Functional distinction between topological (tilted) and consensus (CARC/CRAC) domains. 

Fantini J, Di Scala C, Baier CJ, Barrantes FJ. Chem Phys Lipids. 2016 Sep;199:52-60.

 

Cholesterol-Recognition Motifs in Membrane Proteins. Fantini J, Epand RM, Barrantes FJ. Adv Exp Med Biol. 2019;1135:3-25. 

 

Cracking of the ganglioside recognition code of amyloid proteins

Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: key role of tyrosine 39 in membrane insertion.

Fantini J, Yahi N. J Mol Biol. 2011 May 13;408(4):654-69. 

 

Cholesterol accelerates the binding of Alzheimer's β-amyloid peptide to ganglioside GM1 through a universal hydrogen-bond-dependent sterol tuning of glycolipid conformation.

Fantini J, Yahi N, Garmy N. Front Physiol. 2013 Jun 10;4:120. 

 

Deciphering the glycolipid code of Alzheimer's and Parkinson's amyloid proteins allowed the creation of a universal ganglioside-binding peptide.

 Yahi N, Fantini J. PLoS One. 2014 Aug 20;9(8):e104751.

 

Elucidation of the universal mechanism of formation of oligomeric amyloid pores

The driving force of alpha-synuclein insertion and amyloid channel formation in the plasma membrane of neural cells: key role of ganglioside- and cholesterol-binding domains.

 Fantini J, Yahi N. Adv Exp Med Biol. 2013;991:15-26. 

 

Interaction of Alzheimer's β-amyloid peptides with cholesterol: mechanistic insights into amyloid pore formation.

Di Scala C, Chahinian H, Yahi N, Garmy N, Fantini J. Biochemistry. 2014 Jul 22;53(28):4489-502. 

 

Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein.

Di Scala C, Yahi N, Boutemeur S, Flores A, Rodriguez L, Chahinian H, Fantini J. Sci Rep. 2016 Jun 29;6:28781. 

 

Creation of 12-mer chimeric peptide able to block the formation of amyloid pores by Alzheimer’s and Parkinson’s amyloid proteins (international patent). 

Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides.

 Di Scala C, Yahi N, Flores A, Boutemeur S, Kourdougli N, Chahinian H, Fantini J. Biochim Biophys Acta. 2016 Feb;1862(2):213-22

 

Progress toward Alzheimer's disease treatment: Leveraging the Achilles' heel of Aβ oligomers?
Fantini J, Chahinian H, Yahi N.  Protein Sci. 2020 Aug;29(8):1748-1759.

 

 

 

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