Proteomic analysis revealed the biofilm-degradation abilities of the bacteriophage UPMK_1 and UPMK_2 against Methicillin-resistant Staphylococcus aureus
Objective The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant Staphylococcus aureus phages were examined using gel zymography. Methods The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage...
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Veröffentlicht in: | Biotechnology letters 2022-03, Vol.44 (3), p.513-522 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Objective
The degradation activity of two bacteriophages UPMK_1 and UPMK_2 against methicillin-resistant
Staphylococcus aureus
phages were examined using gel zymography.
Methods
The analysis was done using BLASTP to detect peptides catalytic domains. Many peptides that are related to several phage proteins were revealed.
Results
UPMK_1 and UPMK_2 custom sequence database were used for peptide identification. The biofilm-degrading proteins in the bacteriophage UPMK_2 revealed the same lytic activity towards polysaccharide intercellular adhesin-dependent and independent of Methicillin-resistant
Staphylococcus aureus
(MRSA) biofilm producers in comparison to UPMK_1, which had lytic activity restricted solely to its host.
Conclusion
Both bacteriophage enzymes were involved in MRSA biofilm degradation during phage infection and they have promising enzybiotics properties against MRSA biofilm formation. |
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ISSN: | 0141-5492 1573-6776 |
DOI: | 10.1007/s10529-022-03229-y |