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Enhanced biofilm prevention activity of a SPLUNC1-derived antimicrobial peptide against Staphylococcus aureus.
Yu, Zhongjie; Deslouches, Berthony; Walton, William G; Redinbo, Matthew R; Di, Y Peter.
Afiliação
  • Yu Z; Department of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA, United States of America.
  • Deslouches B; Center for Molecular Genetics, Institute for Translational Medicine, Qingdao University, Qingdao, China.
  • Walton WG; Department of Environmental and Occupational Health, University of Pittsburgh, Pittsburgh, PA, United States of America.
  • Redinbo MR; Department of Microbiology and Molecular Genetics, University of Pittsburgh, Pittsburgh, PA, United States of America.
  • Di YP; Departments of Chemistry, Biochemistry, and Microbiology, University of North Carolina, Chapel Hill, NC, United States of America.
PLoS One ; 13(9): e0203621, 2018.
Article em En | MEDLINE | ID: mdl-30216370
ABSTRACT
SPLUNC1 is a multifunctional protein of the airway with antimicrobial properties. We previously reported that it displayed antibiofilm activities against P. aeruginosa. The goal of this study was to determine whether (1) the antibiofilm property is broad (including S. aureus, another prevalent organism in cystic fibrosis); (2) the α4 region is responsible for such activity; and (3), if so, this motif could be structurally optimized as an antimicrobial peptide with enhanced activities. We used S. aureus biofilm-prevention assays to determine bacterial biomass in the presence of SPLUNC1 and SPLUNC1Δα4 recombinant proteins, or SPLUNC1-derived peptides (α4 and α4M1), using the well-established crystal-violet biofilm detection assay. The SPLUNC1Δα4 showed markedly reduced biofilm prevention compared to the parent protein. Surprisingly, the 30-residue long α4 motif alone demonstrated minimal biofilm prevention activities. However, structural optimization of the α4 motif resulted in a modified peptide (α4M1) with significantly enhanced antibiofilm properties against methicillin-sensitive (MSSA) and-resistant (MRSA) S. aureus, including six different clinical strains of MRSA and the well-known USA300. Hemolytic activity was undetectable at up to 100µM for the peptides. The data warrant further investigation of α4-derived AMPs to explore the potential application of antimicrobial peptides to combat bacterial biofilm-related infections.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Fosfoproteínas / Staphylococcus aureus / Glicoproteínas / Biofilmes / Anti-Infecciosos Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Fosfoproteínas / Staphylococcus aureus / Glicoproteínas / Biofilmes / Anti-Infecciosos Idioma: En Ano de publicação: 2018 Tipo de documento: Article