National Research Council of Italy

Institute of Biosciences and Bioresources

Rossana D’Avino

Role: Associated Staff
Section: Associate Members
Division: Naples
Tel: (39) 081-6132551-081-6132586
E-mail: rossana.davino@ibbr.cnr.it


Education
Degree in Biological Sciences cum laude at the University of Naples Federico II in 1976

Professional experience

2014 to now. Senior Researcher at the Institute of Biosciences and BioResources (IBBR), CNR, Naples

2002-2013. Senior Researcher at the Institute of Protein Biochemistry (IBP), CNR, Naples

1999-2002 Senior Researcher at Institute of Protein Biochemistry and Enzymology (IBPE), CNR, Naples

1988-1999 Researcher at Institute of Protein Biochemistry and Enzymology (IBPE), CNR, Naples

1983-1987 Researcher at the International Institute of Genetics and Biophysics (IIGB), CNR Naples

1979 Guest Scientist at the V.A. Wadsworth Medical Center and Center for Health Sciences of the University of California, Los Angeles.

1976-78 Guest Scientist at the International Institute of Genetics and Biophysics (IIGB), CNR, Naples.

1974-1976 Thesis Student at IIGB- CNR Naples

1974-83 Working positions at the Institute of Internal Medicine, II Faculty of Medicine and Surgery of Naples. Biological assistant after graduation.

Reasearch interests

Study of the structure/function relationship of proteins and enzymes. Studies of subunit communication mechanisms and protein-protein interaction.

Research tools

Protein purification and characterization, including elucidation of the primary structure and of post-translational modifications by amino acid sequencing and mass spectrometry. Functional characterization, including kinetic studies of enzymatic activity and inhibition. Studies of protein-protein interaction by biochemical tools and by model building. Studies of protein folding by circular dichroism and fluorescence spectroscopy. Bioinformatics and molecular modelling.

Current Scientific activity

  • Study of the proteinaceous inhibitors of the carbohydrate modifying enzymes pectin methylesterase (PME) and invertase (INV). In the course of our structure-function studies on PME and its inhibitor (PMEI), in silico analysis revealed the existence of a novel PMEI-like protein family comprising invertase inhibitors (INVI), PME proregions and proteins of unknown function. Despite the very high structural similarity, PMEI and INVI are specific for their target enzymes. The study of the enzyme-inhibitor system has a particular interest since the regulation of PME and INV activity is important both in the plant development and in the utilization of these enzymes in food industry. The aim of the research is to characterize the structural and functional behavior of the isolated interacting partners and of the specific enzyme-inhibitor complex and to study the effect of possible environmental changes (mainly pH and salt) on the complex formation and stability. Bioinformatics and molecular modelling approach is largely utilized in this study. Analysis of 3D structures and models building are used as a tool for the comprehension of the molecular mechanisms that regulate association and dissociation between enzyme and inhibitor.
  • Identification and structural characterization of plant proteins having allergenic properties. Study of the allergenic determinants by bioinformatics and molecular modelling approach.

Previous scientific activity

  • Identification and structural characterization of patological hemoglobins.
  • Studies of coagulation disorders.
  • Studies on histidine binding to haevy metals by mean of fluorimetry and atomic absorbtion spectrofotometry (at the V.A. Wadsworth Medical Center, Los Angeles).
  • Studies in the framework of the Research Project “Physiological, biochemical and molecular mechanisms of the adaptation at low temperatures”, National Program of Research in Antarctica, PNRA /CNR (1985-1999) Study of the structural and functional properties of antarctic and non antarctic fish hemoglobins to gain insight into the evolution of the oxygen binding function and the adaptation of the oxygen-transport system to physiological and environmental conditions. Study of Bohr and Root effects in fish hemoglobins by oxygen and ligands binding measurements and by molecular model building. In 1994, in the framework of the PNRA project, she introduced in the Institute the molecular modelling technique and in 1998 she took care of the activation and setting of the Silicon Graphics System for molecular modelling for the IBPE.
  • Investigation covering different clinical, biochemical and hematological aspects, in collaboration with the IGB- Napoli, aimed at the elucidation of the basis of the genetic heterogeneity of beta-thalassemia in individuals carrying mutations.
  • Investigation of the mechanism of stabilization in proteins from hyperthermophilic Archeobacteria in collaboration with IBP- Marco Moracci group. Building of native and mutant proteins by molecular modelling to identify the molecular determinants of thermal activity and thermostability.

Publication list

Ramirez F, Mears JG, Nudel U, Bank A, Luzzatto L, di Prisco G, D’Avino R, Pepe G, Camardella L, Gambino R, Cimino R, Quattrin N (1979) Defects in DNA and Globin Messenger RNA in Homozygotes for Hemoglobin Lepore. J Clin Invest 63:736-742

Rotoli B, D’Avino R, Chiurazzi F (1983) Combined Factor V and Factor VII Deficiency. Acta Haematol 69:117-122

Gagliardi C, D’Avino R, Stassano P, Musumeci A, Spampinato N (1983) Open Heart Surgery in Factor VII Deficiency. J Cardiovas Surg 24(2):172-174

D’Avino R, di Prisco G (1985) Structural studies on hemoglobins from Antarctic marine organisms. Ital J Biochem 34:457-460

D’Avino R, di Prisco G (1988) Antarctic fish hemoglobin: an outline of the molecular structure and oxygen binding properties. - 1. Molecular structure. In: G di Prisco, B Maresca, B Tota (eds) Comp Biochem Physiol 90B:579-584

di Prisco G, Giardina B, D’Avino R, Condò SG, Bellelli A, Brunori M (1988) Antarctic fish hemoglobin:an outline of the molecular structure and oxygen binding properties. - 2. Oxygen binding properties. In: G di Prisco, B Maresca, B Tota (eds) Comp Biochem Physiol 90B:585-591

D’Avino R, di Prisco G (1989) Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. - 1. Purification and characterisation. Eur J Biochem 179:699-705

D’Avino R, Caruso C, Romano M, Camardella L, Rutigliano B, di Prisco G (1989) Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. - 2. Amino acid sequence of the alpha-chain of Hb 1. Eur J Biochem 179:707-713

di Prisco G, D’Avino R (1989) Molecular adaptation of the blood of Antarctic teleosts to environmental conditions. Antarctic Science 1:119-124

D’Avino R, Caruso C, Schininà ME, Rutigliano B, Romano M, Camardella L, Bossa F, Barra D, di Prisco G (1989) The amino acid sequence of the a and ß-chains of the two hemoglobins of the Antarctic Fish Notothenia coriiceps neglecta. FEBS Letters 250:53-56

D’Avino R, Caruso C, Romano M, Camardella L, Rutigliano B, di PriscoG (1989) Hemoglobins in cold-adapted Antarctic teleosts. Italian Journal of Biochemistry 38:33A-35A

Camardella L, Caruso C, D’Avino R, di Prisco G, Romano M, Rutigliano B (1989) Life under extreme conditions: biochemistry of cold adaptation in Antarctic fishes. CHIMICAoggi 7:65-68.

di Prisco G, D’Avino R, Camardella L, Caruso C, Romano M, Rutigliano B (1990) Structure and function of hemoglobin in Antarctic fishes and evolutionary implications. Polar Biol 10:269-274

D’Avino R, Caruso C, Schininà ME, Rutigliano B, Romano M, Camardella L, Bossa F, Barra D,di Prisco G (1990) Hemoglobin from the Antarctic fish Notothenia coriiceps neglecta. Amino acid sequence of the beta chain. Comp Biochem Physiol 96B:367-373

D’Avino R, Camardella L, Carratore V, di Prisco G (1990) The aminoacid sequence of the a chain of Hb 2 completes the primary structure of the hemoglobins of the Antarctic fish Notothenia coriiceps neglecta. Comp Biochem Physiol 97B:803-807

Tamburrini M, D’Avino R, Caruso C, Camardella L, Carratore V, Rutigliano B, Romano M, di Prisco G (1990) Amino acid sequence of the hemoglobin of the Antarctic teleost Pagothenia bernacchii. J Prot Chem 9:354-355

D’Avino R, Caruso C, Camardella L, Schininà ME, Rutigliano B, Romano M, Carratore V, Barra D, di Prisco G (1991) An overview of the molecular structure and functional properties of the hemoglobins of a cold-adapted Antarctic teleost. In: G di Prisco (ed) Life under Extreme Conditions: Biochemical Adaptation, pp 15-33. Springer-Verlag, Berlin, Heidelberg, New York

di Prisco G, D’Avino R, Caruso C, Tamburrini M, Camardella L, Rutigliano B, Carratore V, Romano M (1991) The biochemistry of oxygen transport in red-blooded Antarctic fishes. In: G di Prisco, B Maresca, B Tota (eds) Biology of Antarctic Fish, pp 263-281. Springer-Verlag, Berlin, Heidelberg, New York

D’Avino R, Fago A, Kunzmann A, di Prisco G. (1992) The primary structure and oxygen-binding properties of the single haemoglobin of the high-Antarctic fish Aethotaxis mitopteryx DeWitt. Polar Biol 12:135-140

Kunzmann A, Fago A, D’Avino R, di Prisco G (1992) Haematological studies on Aethotaxis mitopteryx DeWitt, a high-Antarctic fish with a single haemoglobin. Polar Biol 12:141-145

Camardella L, Caruso C, D’Avino R, di Prisco G, Rutigliano B, Tamburrini M, Fermi G, Perutz MF (1992) Haemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. J Mol Biol 224:449-460

Scudiero R, De Prisco P, Capasso C, Camardella L, D’Avino R, di Prisco G, Parisi E (1992) Differential expression of metal-binding proteins in sea urchin. Comparison between Antarctic and temperate species. In: RJ Wegmann, MA Wegmann (eds) Recent Advances in Cellular and Molecular Biology, pp 351-355. Peeters Press, Leuven, Belgium

Scudiero R, De Prisco P, Camardella L, D’Avino R, di Prisco G, Parisi E (1992) Apparent deficiency of metallothionein in the liver of the Antarctic icefish Chionodraco hamatus. Identification and isolation of a zinc-containing protein unlike metallothionein. Comp Biochem Physiol 103B:201-207

Fago A, D’Avino R, di Prisco G (1992) The hemoglobins of Notothenia angustata, a temperate fish belonging to a family largely endemic to the Antarctic Ocean. Eur J Biochem 210:963-970

Fago A, Romano M, Tamburrini M, Coletta M, D’Avino R, di Prisco G (1993) A polymerising Root-effect fish hemoglobin with high subunit heterogeneity. Correlation with primary structure. Eur J Biochem 218:829-835

D’Avino R, Caruso C, Tamburrini M, Romano M, Rutigliano B, Polverino de Laureto P, Camardella L, Carratore V, di Prisco G (1994) Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi. J Biol Chem, 269:9675-9681

Tamburrini M, D’Avino R, Fago A, Carratore V, Kunzmann A, and di Prisco G (1996) The unique hemoglobin system of Pleuragramma antarcticum, an Antarctic migratory teleost. J Biol Chem, 271:23780-23785

Coletta M, Ascenzi P, D’Avino R, and di Prisco G (1996) Proton-linked subunit kinetic heterogeneity for carbon monoxide binding to hemoglobin from Chelidonichthys kumu. J Biol Chem, 271:29859-29864

D’Avino R and di Prisco G (1997) The hemoglobin system of Antarctic and non-Antarctic notothenioid fishes. Comp Biochem Physiol 118A(4):1045-1049

Stam W.T, Beintema J.J, D’Avino R, Tamburrini M, and di Prisco G (1997) Molecular evolution of hemoglobins of Antarctic fishes (Notothenioidei) J Mol Evol 45(4):437-445

Tamburrini M, D’Avino R, Carratore V, Kunzmann A, and di Prisco G (1997) The hemoglobin system of Pleuragramma antarcticum: correlation of hematological and biochemical adaptation with life style. Comp Biochem Physiol 118A(4):1037-1044

Capasso C, Scudiero R, Capasso A, D’Avino R, Camardella L, di Prisco G, and Parisi E (1997) Purification and characterization of atypical zinc-binding polipeptides from the Antarctic sea urchin Sterechinus neumayeri. In: Battaglia B, Valencia J, Walton DHW (eds) Antarctic Communities: species, structure and survival. pp 305-308. Cambridge University Press, Cambridge

di Prisco G, Tamburrini M, and D’Avino R (1998) Oxygen-transport systems in extreme environments: multiplicity and structure/function relationship in hemoglobins of Antarctic fish. In Pörtner HO, Playle R (eds) Cold Ocean Physiology. Soc Exptl Biol, Seminar Series 66:143-165. Cambridge University Press, Cambridge

Smulevich G, Possenti M, D’Avino R, di Prisco G, and Coletta M (1998) Spectroscopic studies of the heme active site of hemoglobin from Chelidonichthys kumu. J Raman Spectroscopy 29:57-65

R. D’Avino, M. Tamburrini, E. Cocca, W. Stam, J. Beintema, and G. di Prisco (1998) The evolution of hemoglobin in teleost of the suborder notothenioidei. Ital J Biochem 47(2):119-121

Witze T Stam, Jaap J Beintema, Rossana D’Avino, Maurizio Tamburrini, Ennio Cocca, and Guido di Prisco (1998) Evolutionary studies on teleost hemoglobin sequences. In di Prisco G. Pisano E, and Clarke A. (eds) Fishes of Antarctica. A biological overview. pp 355-359. Springer-Verlag Italia Milano

Mazzarella, L., D’Avino, R., di Prisco, G., Savino, C., Vitagliano, L., Moody, P.C.E. and Zagari, A (1999) Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question. J. Mol. Biol. 287:897-906

di Prisco, G., D’Avino, R. and Tamburrini, M. (1999) Structure and function of hemoglobins from antarctic organisms: the search for correlation with adaptive evolution. In Margesin R. and Schinner F. (eds) Cold-Adapted Organisms. Ecology, Physiology, Enzymology and Molecular Biology. pp 239-253. Springer-Verlag Berlin Heidelberg

D’Avino R and De Luca R.(2000) Molecular modelling of Trematomus newnesi Hb1: insights for a lowered oxygen affinity and lack of Root effect. Proteins 39:155-165

Giangiacomo L, D’AvinoR, di Prisco G, and Chiancone E. (2001). Hemoglobin of the antarctic fishes Trematomus bernacchii and Trematomus newnesi. Structural basis for the increased stability of the liganded tetramer relative to human hemoglobin. Biochemistry 40:3062-3068

Fago A, Giangiacomo L, D’Avino R, Carratore V, Romano M, Boffi A, Chiancone E. (2001). Hagfish hemoglobins, structure, function and oxygen-linked association. J Biol Chem. 276(29):27415-23

Cobucci-Ponzano B, Moracci M, Di Lauro B, Ciaramella M, D’Avino R and Rossi M. (2002) The ionic network at the C-terminus of the b-glycosidase from the hyperthermophilic Archeon Sulfolobus sulfataricus: functional role in the quaternary structure thermal stabilization. Proteins 48:98-106 (messo due volte in People-CNR)

D’Avino R, CamardellaL, ChristensenTMIE, GiovaneA and ServilloL. (2003) Tomato pectin methylesterase: modeling, fluorescence and inhibitor interaction studies. Comparison with the bacterial (Erwinia chrysanthemi) enzyme. Proteins 53:830-839

A. Giovane, L. Servillo, C. Balestrieri, A. Raiola, R. D’Avino, M. Tamburrini, M.A. Ciardiello, L. Camardella (2004) Pectin methylesterase inhibitor. Biochem Biophyis Acta, Special issue “Plant Protein Inhibitors of Glycosidase”, 1696:245-252

De Angioletti M, Lacerra G, Pagano L, Alessi M, D’Avino R, Manca L, Carestia C (2004) b Thalassaemia 87 C→G: relationship of the Hb F modulation and polymorphisms in compound heterozygous patients. J. British Haematol. 126, 743-749

Ausili A, Cobucci-Ponzano B, Di Lauro B, D’Avino R, Scire A, Rossi M,Tanfani F, Moracci M. (2006) Structural basis of the destabilization produced by an amino-terminal tag in the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus. Biochimie. 88(7):807-17.

Ausili A, Cobucci-Ponzano B, Di Lauro B, D’Avino R, Perugino G, Bertoli E, Scirè A, Rossi M, Tanfani F, Moracci M. (2007) A comparative infrared spectroscopic study of glycoside hydrolase from extremophilic archea revealed different molecular mechanisms of adaptation to high temperatures. Proteins 267(4):991-1001.

Ciardiello MA, D’Avino R., Amoresano A, Tuppo L, Carpentieri A, Carratore V, Tamburrini M, Giovane A, Pucci P, Camardella L. (2008) The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor. Proteins 71:195-206

Reca IB, Brutus A, D’Avino R, Villard C, Bellincampi D, Giardina T. (2008) Molecular cloning, expression and characterization of a novel apoplastic invertase inhibitor from tomato (Solanum lycopersicum) and its use to purify a vacuolar invertase. Biochimie 90:1611-23

D’Avino R, Bernardi ML, Wallner M, Palazzo P, Camardella L, Tuppo L, Alessandri C, Breiteneder H, Ferreira F, Ciardiello MA, Mari A (2011) Kiwifruit Act d 11 is the first member of the Ripening-related Protein family identified as an allergen. Allergy 66(7):870-7

Reca IB, Lionetti V, Camardella L, D’Avino R, Giardina T, Cervone F, Bellincampi D. (2012) A functional pectin methylesterase inhibitor protein (SolyPMEI) is expressed d... Plant Mol Biol. 79(4-5):429-42

 

Selected Publications
(full list available at CNR People)

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