Personale docente

Personal information:
Date of birth: February 23, 1969
Birthplace: Parma, Italy

Education:
April 2002: EMBO Course “Crystallization of Macromolecular Complexes”- Grenoble, France
March 2001: PhD in Molecular Biotechnology- Catholic University “Sacro Cuore”, Milan, Italy
March 1994: Doctor degree in Biological Sciences – Dissertation in Biochemistry, graduated cum laude –University of Parma, Italy

Research activity:
January 1995-December 1997: Research Fellowship from the Italian Association for Cancer Research - Institute of Biochemical Science, University of Parma. Research Topic: Molecular Interaction between retinoids and retinoic acid nuclear receptors.
January 1998-November 2000: PhD student in Molecular Biotechnology- Institute of Biochemical Sciences, University of Parma. PhD thesis: “Identification, overexpression, functional and structural characterization of novel intracellular retinol-binding proteins”.
December 2000-October 2003: Post-doctoral research fellow in Biochemistry – Deparment of Biochemistyry and Molecular Biology, University of Parma. Research topic: Isolation and characterization of toxins with antibacterial and insecticidal activity.
November 2003-October 2005: Post-doctoral research fellow – Department of Biochemistry and Molecular Biology, University of Parma. Research topic: Identification and functional-structural characterization of new cellular retinol-binding proteins (CRBP) and cellular retinoic acid-binding proteins (CRABP).
November 2005-present: Research Associate in Biochemistry –University of Parma.

The research activity was carried out mainly at the Department of Biochemistry and Molecular Biology of the University of Parma and was initially focused on the functional/structural characterization of proteins involved in retinoid transport and metabolism. Two novel cellular retinol binding proteins were also identified by means of bioinformatic tools and produced as recombinant proteins. Moreover, investigations have been conducted on the amyloidogenic protein transthyretin and on its mutant forms responsible for the inherited disorder known as Familial Amyloid Polyneuropathy to identify the conformational changes responsible for the destabilization of the protein structure and for the increase in the amyloidogenic potential of the protein.
More recently, the enzymatic activity of a mammalian protein initially named “transthyretin related protein”, due to its homology with transthyretin, has been discovered. Based on bioinformatic analyses, it has been proposed a role for this protein in the uric acid degradation pathway as HIUase, an activity that was confirmed experimentally. Moreover, similar studies permitted us to complete this biochemical pathway by identifying the OHCU decarboxylase enzyme. Additional studies have also been carried out to study other enzymes involved in uric acid degradation in bacteria and plants. A bi-functional enzyme from Arabidopsis involved in the synthesis of allantoin and the gene coding for a new bacterial allantoinase have been identified.
A subsequent study has focused on the role played by different proteins in the regulation of pheromone dependent plasmid conjiugation in enterococci isolated from food. In particular, the regulatory role played by two proteins called TraA and TraC has been clarified. The data collected in vitro allowed to propose a regulation model for the plasmid transfer that was further confirmed by in vivo studies.
Finally, further studies in the field of food biochemistry were aimed at the determination of the three-dimensional structure of the plant panallergen “lipid transfer protein“ from peach. The elucidation of the conformational properties of this protein is the starting point forward the identification of the structural epitopes recognized by IgE on protein surface during the allergenic response. Subsequently, different isoforms of LTP from pear have been biochemically and immunologically characterized.