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
|
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.