Sciact
  • EN
  • RU

Characterization of a Thermostable Endolysin of the Aeribacillus Phage AeriP45 as a Potential Staphylococcus Biofilm-Removing Agent Full article

Journal Viruses
ISSN: 1999-4915
Output data Year: 2024, Volume: 16, Number: 1, Article number : 93, Pages count : DOI: 10.3390/v16010093
Tags thermostable endolysin; cell-binding domain CBD; phage;
Authors Golosova Natalia N. 1 , Khlusevich Yana A. 1 , Morozova Vera V. 1 , Matveev Andrey L. 1 , Kozlova Yulia N. 1 , Tikunov Artem Y. 1 , Panina Elizaveta A. 1 , Tikunova Nina V. 1
Affiliations
1 Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia

Funding (1)

1 МИНИСТЕРСТВО НАУКИ И ВЫСШЕГО ОБРАЗОВАНИЯ РОССИЙСКОЙ ФЕДЕРАЦИИ 2021-1930-ФП5-8365-8981

Abstract: Multidrug-resistant Gram-positive bacteria, including bacteria from the genus Staphylococcus, are currently a challenge for medicine. Therefore, the development of new antimicrobials is required. Promising candidates for new antistaphylococcal drugs are phage endolysins, including endolysins from thermophilic phages against other Gram-positive bacteria. In this study, the recombinant endolysin LysAP45 from the thermophilic Aeribacillus phage AP45 was obtained and characterized. The recombinant endolysin LysAP45 was produced in Escherichia coli M15 cells. It was shown that LysAP45 is able to hydrolyze staphylococcal peptidoglycans from five species and eleven strains. Thermostability tests showed that LysAP45 retained its hydrolytic activity after incubation at 80 ◦C for at least 30 min. The enzymatically active domain of the recombinant endolysin LysAP45 completely disrupted biofilms formed by multidrug-resistant S. aureus, S. haemolyticus, and S. epidermidis. The results suggested that LysAP45 is a novel thermostable antimicrobial agent capable of destroying biofilms formed by various species of multidrug-resistant Staphylococcus. An unusual putative cellbinding domain was found at the C-terminus of LysAP45. No domains with similar sequences were found among the described endolysins.
Cite: Golosova N.N. , Khlusevich Y.A. , Morozova V.V. , Matveev A.L. , Kozlova Y.N. , Tikunov A.Y. , Panina E.A. , Tikunova N.V.
Characterization of a Thermostable Endolysin of the Aeribacillus Phage AeriP45 as a Potential Staphylococcus Biofilm-Removing Agent
Viruses. 2024. V.16. N1. 93 . DOI: 10.3390/v16010093 WOS Scopus РИНЦ OpenAlex
Dates:
Published print: Jan 7, 2024
Identifiers:
Web of science: WOS:001152942100001
Scopus: 2-s2.0-85183246212
Elibrary: 64996197
OpenAlex: W4390662877
Citing:
DB Citing
OpenAlex 2
Web of science 2
Altmetrics: