Affiliations 

  • 1 Department of Biology, College of Science, Mustansiriyah University, Palestine Street, PO Box 14022, Baghdad, Iraq
  • 2 Department of Cell and Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
  • 3 Department of Biology, Faculty of Science and Mathematics, Universiti Pendidikan Sultan Idris, 35900, Tanjong Malim, Perak, Malaysia. Jr_alobaidi@yahoo.com
  • 4 Department of Medical Microbiology and Parasitology, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
  • 5 Department of Agriculture Technology, Faculty of Agriculture, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
  • 6 Malaysia Genome Institute (MGI), Jalan Bangi, 43000, Kajang, Selangor, Malaysia
  • 7 Membranology Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1, Tancha, Onna-son, Kunigami-kun, Okinawa, 904-0495, Japan
  • 8 Institute of Bioscience, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia
Biotechnol Lett, 2022 Feb 05.
PMID: 35122191 DOI: 10.1007/s10529-022-03229-y

Abstract

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.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.