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  • Alessandro Vitale

vitale2

Dirigente di Ricerca

Email: vitale * ibba.cnr.it | Phone: +39 02 23699 431 | Fax: +39 02 23699 411

 

Education and professional experience
1971-76. Degree (Laurea) in Biology, Università degli studi di Milano. Field: biochemistry 1978-82. CNR Fellowship, Istituto Biosintesi Vegetali - former denomination of IBBA - Field of activity: plant molecular and cell biology 1982-83. Visiting scientist in the laboratory of Maarten J. Chrispeels, UCSD, La Jolla, CA. Field of activity: plant cell biology.

Keywords
Plant and Animal Biodiversity, Biotic, Abiotic / Environmental Stress, Cell morphogenesis and organelle biogenesis / function, Plant reproduction, embryogenesis and development, Gene expression regulation, Protein biogenesis and degradation, Recombinant pharmaceuticals

Molecular biology, Cell Biology

Ongoing projects
We are studying the function and molecular organization of the endomembrane system and protein secretory pathway of plant cells, and in their biotechnological use for improving human nutrition and health. The endomembrane system is composed of the endoplasmic reticulum, the Golgi apparatus, vacuoles, the plasma membrane and endosomes. These compartments are functionally interconnected and host the secretory pathway, a metabolic pathway that takes care of the synthesis and correct distribution of proteins secreted into the apoplast or belonging to each endomembrane compartment, collectively termed secretory proteins. The plant secretory pathway namely feeds the world, by synthesizing enormous amounts of storage protein in the seeds of cereal and legume crops. More than this, proteins that defend plants from pathogen attacks, proteins that participate in constructing the cell wall, transporters of the tonoplast and the plasma membrane, and receptors that mediate hormone signaling, are all secretory proteins as well. Most secretory proteins are first inserted into the ER. The ones that are not destined to play their function in the ER itself then reach their final destination by membrane traffic, often passing through the Golgi apparatus (which is itself the final destination of many enzymes). The vacuoles and the apoplast are two major endpoints of the secretory pathway. For example, most storage proteins are vacuolar and cell wall proteins are obviously apoplastic. Because most secretory proteins start their life in the ER and not in their final compartment of action, they contain signals that allow their correct sorting by interactions with specific sorting mechanisms. Furthermore, a quality control system certainly operates on newly synthesized proteins when they are still in the ER, optimizing their folding and, when needed, assembly and also regulating their traffic from the ER to the next station of the secretory pathway or their disposal if they have structural defects. Which are the signals that lead each secretory protein to its destination? How do sorting mechanisms work and which are their constituents? How are defective proteins recognized by quality control and disposed? How is proteostasis of the endomembrane system regulated? These are major questions.

The advent of transgenic plant technology has opened further possibilities for the plant secretory system. Because many human proteins of great importance for our health are secretory proteins (antibodies and the other serum proteins, cell surface receptors and peptide hormones, to name a few) there is growing interest in producing them in transgenic plants, which are attractive bioreactors because of their easy transformation and low-cost cultivation. A detailed knowledge of the similarities and differences of the plant and mammalian secretory pathways are fundamental in this respect.

Alessandro Vitale is also: - member of the Società Italiana di Biologia Vegetale (awarded in 1998 the t"Assunta Baccarini-Melandri" Prize), the Società Italiana di Genetica Agraria and the American Society of Plant Biologists (awarded in 2008 the Corresponding Membership Award) - Editor of Planta and the Journal of Plant Biology, member of the Advisory Board of the Journal of Experimental Botany - Meber of tehe Scientific Council of the CNR Agrofood Department

Selected publications
SOLICITED PAPERS (2005 - present)

    • Vitale, A. and Hinz, G. (2005) Sorting of proteins to storage vacuoles: how many mechanisms? Trends Plant Sci. 10, 316-323.
    • Vitale A. and Pedrazzini E. (2005) Recombinant pharmaceuticals from plants: the plant endomembrane system as bioreactor. Mol. Interv. 5, 216-225. Vitale A. and Boston R.S. (2008) Endoplasmic reticulum quality control and the unfolded protein response: insights from plants. Traffic 9, 1581–1588.
    • Marusic C., Vitale A., Pedrazzini E., Donini M., Frigerio L., Bock R., Dix PJ., McCabe MS., Bellucci M. and Benvenuto E. (2009) Plant-based strategies aimed at expressing HIV antigens and neutralizing antibodies at high levels. Nef as a case study. Transgenic Res. 18, 499–512.
    • Vitale A. (2009) Calreticulins are not all the same. Proc. Natl. Acad. Sci. USA 106, 13151–13152.
    • Maîtrejean M, Vitale A (2011) How are tonoplast proteins degraded? Plant Signal. Behav. 6, 1809-1812.

RESEARCH PAPERS (2005-present)

  • Castelli, S. and Vitale, A. (2005) The phaseolin vacuolar sorting signal promotes transient, strong membrane association and aggregation of the bean storage protein in transgenic tobacco. J. Exp. Bot. 56, 1379-1387.

  • Pompa, A. and Vitale, A. (2006) Retention of a bean phaseolin/maize -zein fusion in the endoplasmic reticulum depends on disulfide bond formation. Plant Cell 18, 2608-2621.
  • Klein, E.M., Mascheroni L., Pompa, A., Ragni, L., Weimar, T., Lilley, K.S., Dupree, P. and Vitale, A. (2006) Plant endoplasmin supports the protein secretory pathway and has a role in proliferating tissues. Plant J. 48, 657-673.
  • Barbante, A., Irons, S., Hawes, C., Frigerio, L., Vitale, A. and Pedrazzini, E. (2008) Anchorage to the cytosolic face of the endoplasmic reticulum membrane: a new strategy to stabilize a cytosolic recombinant antigen in plants. Plant Biotechnol. J. 6, 560-675.
  • De Virgilio M., De Marchis F., Bellucci M., Mainieri D., Rossi M., Benvenuto E., Arcioni S. and Vitale A. (2008) The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin. J Exp Bot. 59, 2815-2829.
  • Foresti, O., De Marchis, F., de Virgilio M., Klein E.M., Arcioni S., Bellucci, M. and Vitale, A. (2008) Protein domains involved in assembly in the endoplasmic reticulum promote vacuolar delivery when fused to secretory GFP, indicating a protein quality control pathway for degradation in the plant vacuole. Mol. Plant 1, 1067-1076.
  • Lenzi, P., Scotti, N., Alagna, F., Tornesello, M.L., Pompa, A., Vitale, A., De Stradis, A., Monti, L., Grillo, S., Buonaguro, F.M., Maliga, P. and Cardi, T. (2008) Translational fusion of chloroplast-expressed human papillomavirus type 16 L1 capsid protein enhances antigen accumulation in transplastomic tobacco.Transgenic Res. 17, 1091-1102.
  • Scotti M., Alagna F., Ferraiolo E., Formisano G., Sannino L., Buonaguro L., De Stradis A., Vitale A., Monti L.,Grillo S., Buonaguro F.M. and Cardi T. (2009) High-level expression of the HIV-1 Pr55gag polyprotein in transgenic tobacco chloroplasts. Planta 229,1109–1122.
  • Rigano M., Manna C., Giulini A., Pedrazzini E., Capobianchi M., Castilletti C., Di Caro A., Ippolito G., Beggio P., De Giuli Morghen C., Monti L., Vitale A. and Cardi T. (2009) Transgenic chloroplasts are efficient sites for high-yield production of the vaccinia virus envelope protein A27L in plant cells. Plant Biotechnol. J. 7, 577-591.
  • Pompa, A., De Marchis, F., Vitale A., Arcioni S. and Bellucci M. (2010) An engineered C-terminal disulfide bond can partially replace the phaseolin vacuolar sorting signal. Plant J. 61, 782–791.
  • Avesani, L., Vitale, A., Pedrazzini, E., deVirgilio, M., Pompa, A., Barbante, A., Gecchele, E., Dominici, P., Morandini, F., Brozzetti, A., Falorni, A. and Pezzotti, M. (2010) Recombinant human GAD65 accumulates to high levels in transgenic tobacco plants when expressed as an enzymatically inactive mutant. Plant Biotechnol. J. 8, 1-11.
  • Maîtrejean M, Wudick MM, Voelker C, Prinsi B, Mueller-Roeber B, Czempinski K, Pedrazzini E, Vitale A (2011) Assembly and sorting of the tonoplast potassium channel AtTPK1 and its turnover by internalization into the vacuole. Plant Physiol. 156,1783-1796.
 
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