I was born in Tel Aviv and was raised in Bat-Yam. Since Elementary school, Nature and science studies were my favourite fields of knowledge and I was fascinated by them. I chose to study Biology as my major in High school. I joined the IDF and recruited to the armour corps. I moved Up the rank and shift my expertise to intelligence and became an Intelligence officer. I retired from the army as a Major. I decided to pursue my passion for biology and joined the undergraduates program in the Faculty of Life Science at Tel-Aviv University where I first was introduced to the captivating world of structural biology. I joined the Lab of Prof. Joel Hirsch at the department of Biochemistry and molecular biology, Tel-Aviv University for the direct PhD program. In my doctoral research I focused on the structural elements and assembly of the COP9 signalosome (CSN),
a highly conserved nuclear protein complex involved in regulating protein degradation via the ubiquitin-proteasome pathway. My research goals were to determine the structural and functional elements of the PCI domain, a sequence motif found in the multi-subunit complexes; 19S Proteasome lid, CSN and translation Initiation factor 3 (eIF3). I determined the three dimensional structure of that domain to 1.5 ? resolution. Using structure based mutagenesis I was able to distinguish between different protein-protein interaction within the CSN complex. Furthermore, I was able to show a novel interaction through the disordered C-terminus of AtCSN7 with non-PCI subunit CSN6. Our work (Dessau et.al., Plant Cell 2008) was cited in many prestigious journals and was the ground for many other studies in the field.
In my postdoctoral work at Yale University I focused on the entry mechanism of Rift Valley fever virus (RVFV), a member of phlebovirus genus in the family Bunyaviridae. Enveloped viruses, like RVFV, rely on glycoproteins embedded to their membrane to facilitate virus entry and genome delivery into their hosts cell. I determined the first atomic structure of an envelope protein from a bunyavirus, the RVFV GC ectodomain in two conformations. A non-glycosylated GC crystallized in a novel conformation, yet to be seen in class II fusion proteins. The structure of RVFV sGC establishes a link between the fusion machineries of negative- and positive-sense RNA viruses, which is intriguing from the virus evolution point of view (Dessau et.al., PNAS 2013).
In my lab at the Faculty of Medicine in the Galilee, Bar Ilan University we pursue the structural basis for the entry of pathogens (mainly RNA viruses) that originate from poverty related parts of the world. Although these pathogens cause sever human, it is not reflected in funding and research agend of many pharmaceutical companies. Therefore we study these pathogens to eventually develop new strategies for countermeasures aginst them.
I live in the Galilee (Kamon) with my wife, Nurit and three children; Nevo, Maya and Stav.
In 2015, UN member states agreed to 17 global Sustainable Development Goals (SDGs) to end poverty, protect the planet and ensure prosperity for all. This person’s work contributes towards the following SDG(s):