Jerry Eichler

Prof. Jerry Eichler works in the Department of Life Sciences, Ben Gurion University of the Negev, Israel, where he started his career as lecturer in 1998, became a full professor in 2008, and Department Chair from 2013-2017. He trained in physiology at McGill University (Canada, 1985) and then at the Weizmann Institute of Science (Israel), where he earned his M.Sc. (1988) and Ph.D. (1994) in neurobiology, studying the physiology and biochemistry of acetylcholinesterase in the lab of Prof. Israel Silman. During his postdoctoral training with Prof. Bill Wickner at the Department of Biochemistry, Dartmouth Medical School (USA), he worked on SecA, the bacterial protein translocation motor. Upon establishing an independent research group in 1998, he addressed cell surface proteins and transport in Archaea, which lead him to his main research focus, protein glycosylation in Archaea. Over the last decade, Jerry Eichler has made major contributions to the molecular description of archaeal protein glycosylation pathways and their roles in archaeal physiology.

Key Publications

Guan Z., Naparstek, S., Kaminski, L., Konrad, Z. and Eichler, J. (2010) Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein. Mol. Microbiol., 78, 1294-1303.

Calo, D., Guan Z., Naparstek S., and Eichler, J. (2011) Different routes to the same ending: Comparing the N-glycosylation processes of Haloferax volcanii and Haloarcula marismortui, two halophilic archaea from the Dead Sea. Mol. Microbiol., 81, 1166-1177.

Kaminski, L., Guan, Z., Yurist-Doutsch, S. and Eichler, J. (2013) Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity. mBio, 4, e00716-13.

Elharar, Y., Podilapu, A.R., Guan, Z., Kulkarni, S.S. and Eichler, J. (2017) Assembling glycan-charged dolichol phosphates: Chemoenzymatic synthesis of a Haloferax volcanii N-glycosylation pathway intermediate. Bioconj. Chem., 28, 2461-2470.