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 JJ 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.

 

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 JJ 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 JCell 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.

 

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 JCurr 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.

 

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. 

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 JBiochemistry. 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 JSci 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 JBiochim Biophys Acta. 2016 Feb;1862(2):213-22