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Role of Phage Capsid in the Resistance to UV-C Radiations.
Plano, Laura Maria De; Franco, Domenico; Rizzo, Maria Giovanna; Zammuto, Vincenzo; Gugliandolo, Concetta; Silipigni, Letteria; Torrisi, Lorenzo; Guglielmino, Salvatore P P.
  • Plano LM; Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy.
  • Franco D; Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy.
  • Rizzo MG; Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy.
  • Zammuto V; Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy.
  • Gugliandolo C; Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy.
  • Silipigni L; Department of Mathematical and Computational Sciences, Physical Sciences and Earth Sciences, University of Messina, 98166 Messina, Italy.
  • Torrisi L; Department of Mathematical and Computational Sciences, Physical Sciences and Earth Sciences, University of Messina, 98166 Messina, Italy.
  • Guglielmino SPP; Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy.
Int J Mol Sci ; 22(7)2021 Mar 26.
Article in English | MEDLINE | ID: covidwho-1299434
ABSTRACT
The conformational variation of the viral capsid structure plays an essential role both for the environmental resistance and acid nuclear release during cellular infection. The aim of this study was to evaluate how capsid rearrangement in engineered phages of M13 protects viral DNA and peptide bonds from damage induced by UV-C radiation. From in silico 3D modelling analysis, two M13 engineered phage clones, namely P9b and 12III1, were chosen for (i) chemical features of amino acids sequences, (ii) rearrangements in the secondary structure of their pVIII proteins and (iii) in turn the interactions involved in phage capsid. Then, their resistance to UV-C radiation and hydrogen peroxide (H2O2) was compared to M13 wild-type vector (pC89) without peptide insert. Results showed that both the phage clones acquired an advantage against direct radiation damage, due to a reorganization of interactions in the capsid for an increase of H-bond and steric interactions. However, only P9b had an increase in resistance against H2O2. These results could help to understand the molecular mechanisms involved in the stability of new virus variants, also providing quick and necessary information to develop effective protocols in the virus inactivation for human activities, such as safety foods and animal-derived materials.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Radiation Tolerance / Ultraviolet Rays / Bacteriophage M13 / Capsid Proteins Type of study: Experimental Studies Topics: Variants Language: English Year: 2021 Document Type: Article Affiliation country: Ijms22073408

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Radiation Tolerance / Ultraviolet Rays / Bacteriophage M13 / Capsid Proteins Type of study: Experimental Studies Topics: Variants Language: English Year: 2021 Document Type: Article Affiliation country: Ijms22073408