Generation of innovative scaffolds by manipulating hyperstable proteins
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Generation of innovative scaffolds by manipulating hyperstable proteins
Research areas: Biomolecules for biosensing applications, Macromolecules for biomedical and biotechnological applications, 

Keywords: Structural Biology, Protein Engineering, Biosensors, Protein Scaffolds

Contact person: Alessia Ruggiero, alessia.ruggierounina.it

Actors: Alessia Ruggiero, alessia.ruggierounina.it, Rita Berisio, rita.berisiounina.it, Luigi Vitagliano, luigi.vitaglianocnr.it,

Description:
We are currentlycharacterizing T. maritima ArginineBinding Protein (TmArgBP), which belong to the substrate binding proteinfamily, as a protein scaffold that can be exploited in different research areassuch as arginine sensing, protein stabilization, epitope presentation and forthe analysis of structure-stability relationships.  

In the last few years, wehave structurally characterized and manipulated TmArgBP that is endowed withseveral unusual features, which include an extraordinary thermal and pressurestability and a remarkable structural versatility [1-7]. In these investigations,the wild-type swapped dimer of  TmArgBPwas initially transformed in a monomeric form by deleting its C-terminal helix  [3]. This truncated form was further dissectedinto two domains (D1 and D2) that were exhaustively characterized using a repertoireof different experimental and computational techniques [4]. Interestingly, bothD1 and D2 retain the remarkable thermal/chemical stability of the wild-typeprotein [8]. The analysis of the structural and dynamic properties of TmArgBPand of the individual domains have also highlighted possible routes of domaincommunication. Very recently, we also report the development of twoTmArgBP-based different scaffolds for arginine sensing characterized bydifferent sizes and properties [9].

Giventhe remarkable stability of TmArgBP, we also used one of its variants as ascaffold for efficient epitope presentation by exploiting the proteinthermostability and the helix insertion motif, which we recently identified andcharacterized in this protein [10]. Interestingly, the variants bearingepitopes extracted from proteins of HCV or HIV viruses tightly bindsneutralizing antibodies targeting these pathogens. Our data indicate thatTmArgBP may be effectively engineered to generate protein variants that can beused for epitope presentation.

Figures:

Selected papers:

[1] RuggieroA, Dattelbaum JD, Staiano M, Berisio R, D'Auria S, Vitagliano L. PloS One . 2014 , 9 , e96560.

[2] Smaldone G,Vigorita M, Ruggiero A,Balasco N, Dattelbaum JD, D'Auria S, Del Vecchio P, Graziano G, Vitagliano L Biochim Biophys Acta . 2016 , 1864 , 814.

[3] Smaldone G, Berisio R, Balasco N, D'AuriaS, Vitagliano L, Ruggiero A. Biochim Biophys Acta . 2018 , 1866 ,952.

[4] Smaldone G, Balasco N, Vigorita M,Ruggiero A, Cozzolino S, Berisio R, Del Vecchio P, Graziano G, Vitagliano L. IntJ Biol Macromol . 2018 , 119 , 758.

[5] Balasco N, Smaldone G, Vigorita M, DelVecchio P, Graziano G, Ruggiero A, Vitagliano L. Sci Rep . 2019, 9 ,6617.

[6] Smaldone G, Ruggiero A, Balasco N,Abuhammad A, Autiero I, Caruso D, Esposito D, Ferraro G, Gelardi ELM, MoreiraM, Quareshy M, Romano M, Saaret A, Selvam I, Squeglia F, Troisi R,Kroon-Batenburg LMJ, Esposito L, Berisio R, Vitagliano L. Acta Cryst. F 2019 ,F 75 , 707.

[7] Jaworek MW, Ruggiero A, Graziano G,Winter R, Vitagliano L. Phys. Chem. Chem. Phys . 2020 , 22 ,11244.

[8] Cozzolino S, Balasco N, Vigorita M,Ruggiero A, Smaldone G, Del Vecchio P, Vitagliano L, Graziano G.  Int J Biol Macromol. 2020 , 163 ,375.

[9] Smaldone G, Ruggiero A, Balasco N,Vitagliano L. Int J Mol Sci. 2020 , 21 , 7503.

[10]Balasco N, Smaldone G, Ruggiero A, De Simone A, Vitagliano L. Int J BiolMacromol . 2018 , 118 , 1924 .
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Generation of innovative scaffolds by manipulating hyperstable proteins
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Last modified by Marco Comerci on Friday 04 December 2020, 17:37:17
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