Characteristics of the Enterococcus Phage vB_EfS_SE, and the Properties of Its Chimeric Endolysins Harboring a PlySE-Carbohydrate-Binding Domain and a Synthetic Enzymatic Domain

• Main Authors: Rustam M. Buzikov (Author), Vladislav A. Kulyabin (Author), Olga N. Koposova (Author), Vyacheslav A. Arlyapov (Author), Andrey M. Shadrin (Author)
• Format: Book
• Published: MDPI AG, 2024-10-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Summary

<b>Background/Objectives:</b> The World Health Organization has selected enterococci as one of the priority multidrug-resistant microorganisms for the development of new antibacterial drugs. Bacteriophages are promising antibacterial agents, but the biology of bacteriophages requires deeper understanding. <b>Methods:</b> The vB_EfS_SE phage which is capable of infecting four species of the genus <i>Enterococci</i> was isolated from sewage plant. The complete genome of the vB_EfS_SE phage was sequenced using illumina technology. The endolysin gene was cloned into pBAD18 expression vector. Two chimeric endolysins were engineered using the vB_EfS_SE carbohydrate-binding domain (CBD) and replacing its enzymatically active domain (EAD). <b>Results:</b> The bacteriophage exhibits promising lytic properties and persists at temperatures of 40 °C and below, and under pH conditions ranging from 5 to 11. The genome sequence is 57,904 bp in length. The vB_EfS_SE endolysin PlySE and chimeric endolysins PlyIME-SE and PlySheep-SE were found to have the same range of specificity, but different thermostability properties and a different pH range for enzyme activity. <b>Conclusions:</b> Taking together the results obtained in this work and other published studies, we can highly appreciate the potential of <i>Saphexavirus</i> phages and their endolysins as novel antibacterial compounds.

Item Description

10.3390/pharmaceutics16101312
1999-4923