Landau - פקולטה לביולוגיה Biology Faculty

Education/ Resume:

2020-Present Visiting Group Leader, The European Molecular Biology Laboratory (EMBL), Hamburg, Germany.

2019-present Associate Professor, The Faculty of Biology at the Technion – Israel Institute of Technology.

Research Summary

Our lab pioneered the atomic-level analysis of structure-function relationships in bacterial amyloids and published the first structures of bacterial amyloid fibrils involved in cytotoxicity, antibacterial activity and biofilm structuring. In particular, the discovery of a novel class of cross-α amyloid fibrils of toxic peptides presented novel protein architectures, offered drug targets and leads, and opened a fresh perspective to study amyloid-related toxicity.

Awards:

2020      Daniel Shiran Memorial Prize
2020      Hestrin Prize of the Israel Society for Biochemistry and Molecular Biology
2019      Juludan Research Prize

Key Publications:

Landau, S.J. Fleishman and N. Ben-Tal. A Putative mechanism for down-regulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains. Structure 12: 2265-75, 2004.
Landau, I. Mayrose, Y. Rosenberg, F. Glaser, E. Martz, T. Pupko and N. Ben-Tal. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 33: W299-W302, 2005.
Landau and N. Zisapel. The low affinity binding of melatonin to calmodulin: use of computational methods to explain its physiological relevance. Melatonin: from molecules to therapy, S.R. Pandi-Perumal and D.P. Cardinali. Hauppauge, NY: Nova Science Publishers, Inc. 2006.

Landau, M.R. Sawaya, K.F. Faull, A. Laganowsky, L. Jiang, S.A. Sievers, J. Liu, J.R. Barrio and D. Eisenberg. Towards a Pharmacophore for Amyloid. PLoS Biology 9(6): e1001080; 2011.
Colletier*, A. Laganowsky*, M. Landau*, M. Zhao*, A.B. Soriaga*, L. Goldschmidt, D. Cascio, M.R. Sawaya, and D. Eisenberg. Molecular Basis for Amyloid-beta Polymorphism. PNAS 108(41):16938-43; 2011. *Authors contributed equally
Laganowsky, C. Lui, M.R. Sawaya, J.P. Whitelegge, J. Park, M. Zhao, A. Pensalfini, A.B. Soriaga, M. Landau, P.K. Teng, D. Cascio, C. Glabe, D. Eisenberg. Atomic View of a Toxic Amyloid Small Oligomer. Science 335(6073):1228-31; 2012.
Jiang, C. Liu, D. Leibly, M. Landau, M. Zhao, M. Hughes, and D.Eisenberg. Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta. eLife 2:e00857; 2013.
Tayeb-Fligelman*, O. Tabachnikov*, A. Moshe*, O. Goldshmidt-Tran, M.R. Sawaya, N. Coquelle, J-P. Colletier, and M. Landau. The Cytotoxic Staphylococcus aureus PSMα3 Reveals a Cross-α Amyloid-like Fibril. Science 355(6327): 831-833; 2017
Landau. Getting in charge of β-synuclein fibrillation. J Biol. Chem. 29;292(39):16380-16381; 2017
Malishev, E. Tayeb-Fligelman, S. David S, M. Meijler, M. Landau*, and R. Jelinek*. Reciprocal Interactions between Membrane Bilayers and S. aureus PSMalpha3 Cross-alpha Amyloid Fibrils Account for Species-Specific Cytotoxicity. J. Mol. Biol. 430(10):1431-1441; 2018. *Co-corresponding authors
Salinas, A. Moshe, J-P. Colletier, and M. Landau. Extreme Amyloid Polymorphism in Staphylococcus aureus Virulent PSMα Peptides. Nat. Commun. 9(1):3512; 2018.
Landau. Mimicking Cross-α Amyloids. Nat. Chem. Biol. 14(9):833-834; 2018
Perov*, O. Lidor*, N. Salinas*, N. Golan*, E. Tayeb-Fligelman, M. Deshmukh, D. Willbold, and M. Landau. Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspired Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents. PLoS Pathog 15(8): e1007978; 2019 *Authors contributed equally.
Tayeb-Fligelman, N. Salinas O. Tabachnikov, and M. Landau. Staphylococcus aureus PSMα3 Cross-α Fibril Polymorphism and Determinants of Cytotoxicity. Structure S0969-2126(19)30445-9; 2020
Engelberg, and M. Landau. The Human LL-37(17-29) Antimicrobial Peptide Reveals a Functional Supramolecular Nanostructure. Nat. Commun. 11, 3894; 2020
Salinas, TL. Povolotsky, M. Landau, I. and Kolodkin-Gal. Emerging Roles of Functional Bacterial Amyloids in Gene Regulation, Toxicity, and Immunomodulation. Microbiol Mol Biol Rev. 85(1):e00062-20; 2020
Salinas*, E. Tayeb-Fligelman*, M. Sammito, D. Bloch, R. Jelinek, D. Noy, I. Uson, and M. Landau. The Amphibian Antimicrobial Peptide Uperin 3.5 is a Cross-α/Cross-β Chameleon Functional Amyloid. *Authors contributed equally. PNAS in press.

Recent Publications:

- - - E. Tayeb-Fligelman*, O. Tabachnikov*, A. Moshe*, O. Goldshmidt-Tran, M.R. Sawaya, N. Coquelle, J-P. Colletier, and M. Landau. The Cytotoxic Staphylococcus aureus PSMα3 Reveals a Cross-α Amyloid-like Fibril. Science 355(6327): 831-833; 2017

Open Positions

Our lab is looking for highly motivated Master and Ph.D. candidates who are interested in research integrating biophysical, biochemical, biological and computational methods for applications in drug development, biomedicine and nanotechnology.

Meytal Landau