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23 results on '"Carboni, Filippo"'

1. QUIN 2.0 - new release of the QUaternary fault strain INdicators database from the Southern Apennines of Italy

Author

Lavecchia, Giusy, Bello, Simone, Andrenacci, Carlo, Cirillo, Daniele, Pietrolungo, Federico, Talone, Donato, Ferrarini, Federica, de Nardis, Rita, Galli, Paolo, Faure Walker, Joanna, Sgambato, Claudia, Menichetti, Marco, Monaco, Carmelo, Gambino, Salvatore, De Guidi, Giorgio, Barreca, Giovanni, Carnemolla, Francesco, Brighenti, Fabio, Giuffrida, Salvatore, Pirrotta, Claudia, Carboni, Filippo, Ferranti, Luigi, Valoroso, Luisa, Toscani, Giovanni, Barchi, Massimiliano R., Roberts, Gerald, and Brozzetti, Francesco

Published
2024
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2. Author Correction: Proof of concept for a single-dose Group B Streptococcus vaccine based on capsular polysaccharide conjugated to Qβ virus-like particles

Author

Carboni, Filippo, Cozzi, Roberta, Romagnoli, Giacomo, Tuscano, Giovanna, Balocchi, Cristiana, Buffi, Giada, Bodini, Margherita, Brettoni, Cecilia, Giusti, Fabiola, Marchi, Sara, Brogioni, Giulia, Brogioni, Barbara, Cinelli, Paolo, Cappelli, Luigia, Nocciolini, Chiara, Senesi, Silvia, Facciotti, Claudia, Frigimelica, Elisabetta, Fabbrini, Monica, Stranges, Daniela, Savino, Silvana, Maione, Domenico, Adamo, Roberto, Wizel, Benjamin, Margarit, Immaculada, and Romano, Maria Rosaria

Published
2024
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3. Proof of concept for a single-dose Group B Streptococcus vaccine based on capsular polysaccharide conjugated to Qβ virus-like particles

Author

Carboni, Filippo, Cozzi, Roberta, Romagnoli, Giacomo, Tuscano, Giovanna, Balocchi, Cristiana, Buffi, Giada, Bodini, Margherita, Brettoni, Cecilia, Giusti, Fabiola, Marchi, Sara, Brogioni, Giulia, Brogioni, Barbara, Cinelli, Paolo, Cappelli, Luigia, Nocciolini, Chiara, Senesi, Silvia, Facciotti, Claudia, Frigimelica, Elisabetta, Fabbrini, Monica, Stranges, Daniela, Savino, Silvana, Maione, Domenico, Adamo, Roberto, Wizel, Benjamin, Margarit, Immaculada, and Romano, Maria Rosaria

Published
2023
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8. A Multidisciplinary Structural Approach to the Identification of the Haemophilus influenzaeType b Capsular Polysaccharide Protective Epitope

Author

Nonne, Francesca, Iacono, Lucia Dello, Bertuzzi, Sara, Unione, Luca, Proietti, Daniela, Norais, Nathalie, Margarit, Immaculada, Adamo, Roberto, Jiménez-Barbero, Jesús, Carboni, Filippo, and Romano, Maria Rosaria

Abstract

Glycoconjugate vaccines so far licensed are generally composed of a native or size-reduced capsular polysaccharide conjugated to carrier proteins. Detailed information on the structural requirements necessary for CPS recognition is becoming the key to accelerating the development of next-generation improved glycoconjugate vaccines. Structural glycobiology studies using oligosaccharides (OS) complexed with functional monoclonal antibodies represent a powerful tool for gaining information on CPS immunological determinants at the atomic level. Herein, the minimal structural epitope of Haemophilus influenzaetype b (Hib) CPS recognized by a functional human monoclonal antibody (hmAb) is reported. Short and well-defined Hib oligosaccharides originating from the depolymerization of the native CPS have been used to elucidate saccharide–mAb interactions by using a multidisciplinary approach combining surface plasmon resonance (SPR), saturation transfer difference-nanomagnetic resonance (STD-NMR), and X-ray crystallography. Our study demonstrates that the minimal structural epitope of Hib is comprised within two repeating units (RUs) where ribose and ribitol are directly engaged in the hmAb interaction, and the binding pocket fully accommodates two RUs without any additional involvement of a third one. Understanding saccharide antigen structural characteristics can provide the basis for the design of innovative glycoconjugate vaccines based on alternative technologies, such as synthetic or enzymatic approaches.

Published
2024
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9. Implementing the European Space Agency's SentiNel Application Platform's Open-Source Python Module for Differential Synthetic Aperture Radar Interferometry Coseismic Ground Deformation from Sentinel-1 Data.

Author

Occhipinti, Martina, Carboni, Filippo, Amorini, Shaila, Paltriccia, Nicola, López-Martínez, Carlos, and Porreca, Massimiliano

Subjects
*RADAR interferometry, *PYTHON programming language, *SYNTHETIC apertures, *SYNTHETIC aperture radar, *INTERFEROMETRY, *REMOTE-sensing images
Abstract

Differential SAR Interferometry is a largely exploited technique to study ground deformations. A key application is the detection of the effects promoted by earthquakes, including detailed variations in ground deformations at different scales. In this work, an implemented Python script (Snap2DQuake) based on the "snappy" module by SNAP software 9.0.8 (ESA) for the processing of satellite imagery is proposed. Snap2DQuake is aimed at producing detailed coseismic deformation maps using Sentinel-1 C-band data by the DInSAR technique. With this alternative approach, the processing is simplified, and several issues that may occur using the software are solved. The proposed tool has been tested on two case studies: the Mw 6.4 Petrinja earthquake (Croatia, December 2020) and the Mw 5.7 to Mw 6.3 earthquakes, which occurred near Tyrnavós (Greece, March 2021). The earthquakes, which occurred in two different tectonic contexts, are used to test and verify the validity of Snap2DQuake. Snap2DQuake allows us to provide detailed deformation maps along the vertical and E-W directions in perfect agreement with observations reported in previous works. These maps offer new insights into the deformation pattern linked to earthquakes, demonstrating the reliability of Snap2DQuake as an alternative tool for users working on different applications, even with basic coding skills. [ABSTRACT FROM AUTHOR]

Published
2024
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10. A stabilized glycomimetic conjugate vaccine inducing protective antibodies against Neisseria meningitidis serogroup A

Author

Enotarpi, Jacopo, Tontini, Marta, Balocchi, Cristiana, van der Es, Daan, Auberger, Ludovic, Balducci, Evita, Carboni, Filippo, Proietti, Daniela, Casini, Daniele, Filippov, Dmitri V., Overkleeft, Hermen S., van der Marel, Gijsbert A., Colombo, Cinzia, Romano, Maria Rosaria, Berti, Francesco, Costantino, Paolo, Codeé, Jeroen D. C., Lay, Luigi, and Adamo, Roberto

Published
2020
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11. Publisher Correction: A stabilized glycomimetic conjugate vaccine inducing protective antibodies against Neisseria meningitidis serogroup A

Author

Enotarpi, Jacopo, Tontini, Marta, Balocchi, Cristiana, van der Es, Daan, Auberger, Ludovic, Balducci, Evita, Carboni, Filippo, Proietti, Daniela, Casini, Daniele, Filippov, Dmitri V., Overkleeft, Hermen S., van der Marel, Gijsbert A., Colombo, Cinzia, Romano, Maria Rosaria, Berti, Francesco, Costantino, Paolo, Codeé, Jeroen D. C., Lay, Luigi, and Adamo, Roberto

Published
2020
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13. Retaining the structural integrity of disulfide bonds in diphtheria toxoid carrier protein is crucial for the effectiveness of glycoconjugate vaccine candidates

Author

Carboni, Filippo, Kitowski, Annabel, Sorieul, Charlotte, Veggi, Daniele, Marques, Marta C, Oldrini, Davide, Balducci, Evita, Brogioni, Barbara, Del Bino, Linda, Corrado, Alessio, Angiolini, Francesca, Dello Iacono, Lucia, Margarit, Immaculada, Romano, Maria Rosaria, Bernardes, Gonçalo JL, Adamo, Roberto, Kitowski, Annabel [0000-0002-8001-5928], Sorieul, Charlotte [0000-0003-1999-6007], Bernardes, Gonçalo JL [0000-0001-6594-8917], Adamo, Roberto [0000-0001-5228-6088], and Apollo - University of Cambridge Repository

Subjects
34 Chemical Sciences, Prevention, 1.1 Normal biological development and functioning, 3 Good Health and Well Being, General Chemistry, FOS: Health sciences, Vaccine Related, Infectious Diseases, Emerging Infectious Diseases, 3.4 Vaccines, 1 Underpinning research, Immunization, Biotechnology, 3 Prevention of disease and conditions, and promotion of well-being
Abstract

The introduction of glycoconjugate vaccines marks an important point in the fight against various infectious diseases. The covalent conjugation of relevant polysaccharide antigens to immunogenic carrier proteins enables the induction of a long-lasting and robust IgG antibody response, which is not observed for pure polysaccharide vaccines. Although there has been remarkable progress in the development of glycoconjugate vaccines, many crucial parameters remain poorly understood. In particular, the influence of the conjugation site and strategy on the immunogenic properties of the final glycoconjugate vaccine is the focus of intense research. Here, we present a comparison of two cysteine selective conjugation strategies, elucidating the impact of both modifications on the structural integrity of the carrier protein, as well as on the immunogenic properties of the resulting glycoconjugate vaccine candidates. Our work suggests that conjugation chemistries impairing structurally relevant elements of the protein carrier, such as disulfide bonds, can have a dramatic effect on protein immunogenicity.

Published
2022

17. Molecular basis of the interactions between carbohydrate antigens and monoclonal antibodies

Author

Carboni, Filippo

Subjects
GBS, carbohydrates, epitope mapping, glycoconjugates, epitope mapping, Settore BIO/10 - Biochimica, carbohydrates, BIO/11 Biologia molecolare, Settore BIO/11 - Biologia Molecolare, GBS, glycoconjugates, BIO/10 Biochimica
Abstract

Carbohydrate-based vaccines induce an immune response against surface glycans found on pathogenic bacteria and are used to protect children from meningitis and other bacterial diseases. The definition of the epitope targeted by protective antibodies is a crucial information for the design, description and even registration of glycoconjugate vaccines. The aim of this project is the characterization at atomic level of the interaction between Group B Streptococcus (GBS) oligosaccharides with functional antibodies mediating bacterial phagocytic killing. The specificity of anti-GBS type III polysaccharide (GBS PSIII) antibodies has been ascribed to a conformational epitope with an extended helical structure which would be formed by multiple repeating units. Here fragments of GBS PSIII were obtained by chemical synthesis and by sizing of the native polysaccharide from bacterial source. The oligosaccharides (OSs) were purified by ion exchange chromatography and were characterized by mass spectrometry, HPLC and NMR analysis. First, the obtained OSs were used to characterize the interaction to protective anti PSIII rabbit monoclonal antibody (mAb) by competitive ELISA and surface plasmon resonance analysis. The dependence of binding affinity on oligosaccharide length was confirmed and the minimal structures showing comparable binding to full-length PS III were identified. Next, a combination of saturation transfer difference NMR (STD-NMR) and X-ray crystallography was used to map at atomic level the interactions in the rabbit mAb-OS complex. The challenging crystallization of the carbohydrate-protein complex was achieved and the molecular bases of the antigen-antibody interaction were unveiled. The obtained results were used to optimize a vaccine based on short GBS PSIII fragments.

Published
2017

19. Structure of a protective epitope of group BStreptococcustype III capsular polysaccharide

Author

Carboni, Filippo, primary, Adamo, Roberto, additional, Fabbrini, Monica, additional, De Ricco, Riccardo, additional, Cattaneo, Vittorio, additional, Brogioni, Barbara, additional, Veggi, Daniele, additional, Pinto, Vittoria, additional, Passalacqua, Irene, additional, Oldrini, Davide, additional, Rappuoli, Rino, additional, Malito, Enrico, additional, Margarit, Immaculada y Ros, additional, and Berti, Francesco, additional

Published
2017
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21. Evolution to carbapenem-hydrolyzing activity in noncarbapenemase class D β-lactamase OXA-10 by rational protein design.

Author

Luca, Filomena De, Benvenuti, Manuela, Carboni, Filippo, Pozzi, Cecilia, Rossolini, Gian Maria, Mangani, Stefano, and Docquier, Jean-Denis

Subjects
BETA lactamases, DRUG resistance, CARBAPANEMS, PROTEIN engineering, GRAM-negative bacteria
Abstract

Class D β-lactamases with carbapenemase activity are emerging as carbapenem-resistance determinants in Gram-negative bacterial pathogens, mostly Acinetobacter baumannii and Klebsiella pneumoniae. Carbapenemase activity is an unusual feature among class D β-lactamases, and the structural elements responsible for this activity remain unclear. Based on structural and molecular dynamics data, we previously hypothesized a potential role of the residues located in the short-loop connecting strands β5 and β6 (the β5-β6 loop) in conferring the carbapenemase activity of the OXA-48 enzyme. In this work, the narrow-spectrum OXA-10 class D β-lactamase, which is unable to hydrolyze carbapenems, was used as a model to investigate the possibility of evolving carbapenemase activity by replacement of the β5-β6 loop with those present in three different lineages of class D carbapenemases (OXA-23, OXA-24, and OXA-48). Biological assays and kinetic measurements showed that all three OXA-10-derived hybrids acquired significant carbapenemase activity. Structural analysis of the OXA-10loop24 and OXA-10loop48 hybrids revealed no significant changes in the molecular fold of the enzyme, except for the orientation of the substituted β5-β6 loops, which was reminiscent of that found in their parental enzymes. These results demonstrate the crucial role of the β5-β6 loop in the carbapenemase activity of class D β-lactamases, and provide previously unexplored insights into the mechanism by which these enzymes can evolve carbapenemase activity. [ABSTRACT FROM AUTHOR]

Published
2011
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