Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces
Staphylococcal-associated device-related infections (DRIs) represent a significant clinical challenge causing major medical and economic sequelae. Bacterial colonization, proliferation, and biofilm formation after adherence to surfaces of the indwelling device are probably the primary cause of DRIs....
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| Format: | Article |
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MDPI AG
2021-11-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/22/12544 |
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| author | Wan Yang Vijay Singh Gondil Dehua Luo Jin He Hongping Wei Hang Yang |
| author_facet | Wan Yang Vijay Singh Gondil Dehua Luo Jin He Hongping Wei Hang Yang |
| author_sort | Wan Yang |
| collection | DOAJ |
| description | Staphylococcal-associated device-related infections (DRIs) represent a significant clinical challenge causing major medical and economic sequelae. Bacterial colonization, proliferation, and biofilm formation after adherence to surfaces of the indwelling device are probably the primary cause of DRIs. To address this issue, we incorporated constructs of silica-binding peptide (SiBP) with ClyF, an anti-staphylococcal lysin, into functionalized coatings to impart bactericidal activity against planktonic and sessile <i>Staphylococcus aureus</i>. An optimized construct, SiBP1-ClyF, exhibited improved thermostability and staphylolytic activity compared to its parental lysin ClyF. SiBP1-ClyF-functionalized coatings were efficient in killing MRSA strain N315 (>99.999% within 1 h) and preventing the growth of static and dynamic <i>S. aureus</i> biofilms on various surfaces, including siliconized glass, silicone-coated latex catheter, and silicone catheter. Additionally, SiBP1-ClyF-immobilized surfaces supported normal attachment and growth of mammalian cells. Although the recycling potential and long-term stability of lysin-immobilized surfaces are still affected by the fragility of biological protein molecules, the present study provides a generic strategy for efficient delivery of bactericidal lysin to solid surfaces, which serves as a new approach to prevent the growth of antibiotic-resistant microorganisms on surfaces in hospital settings and could be adapted for other target pathogens as well. |
| first_indexed | 2024-03-10T05:26:06Z |
| format | Article |
| id | doaj.art-e2e40985d0c243509b0097a50e781d41 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T05:26:06Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-e2e40985d0c243509b0097a50e781d412023-11-22T23:44:00ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-11-0122221254410.3390/ijms222212544Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device SurfacesWan Yang0Vijay Singh Gondil1Dehua Luo2Jin He3Hongping Wei4Hang Yang5State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCAS Key Laboratory of Special Pathogens and Biosafety, Center for Biosafety Mega-Science, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, ChinaState Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaState Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinaCAS Key Laboratory of Special Pathogens and Biosafety, Center for Biosafety Mega-Science, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, ChinaCAS Key Laboratory of Special Pathogens and Biosafety, Center for Biosafety Mega-Science, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, ChinaStaphylococcal-associated device-related infections (DRIs) represent a significant clinical challenge causing major medical and economic sequelae. Bacterial colonization, proliferation, and biofilm formation after adherence to surfaces of the indwelling device are probably the primary cause of DRIs. To address this issue, we incorporated constructs of silica-binding peptide (SiBP) with ClyF, an anti-staphylococcal lysin, into functionalized coatings to impart bactericidal activity against planktonic and sessile <i>Staphylococcus aureus</i>. An optimized construct, SiBP1-ClyF, exhibited improved thermostability and staphylolytic activity compared to its parental lysin ClyF. SiBP1-ClyF-functionalized coatings were efficient in killing MRSA strain N315 (>99.999% within 1 h) and preventing the growth of static and dynamic <i>S. aureus</i> biofilms on various surfaces, including siliconized glass, silicone-coated latex catheter, and silicone catheter. Additionally, SiBP1-ClyF-immobilized surfaces supported normal attachment and growth of mammalian cells. Although the recycling potential and long-term stability of lysin-immobilized surfaces are still affected by the fragility of biological protein molecules, the present study provides a generic strategy for efficient delivery of bactericidal lysin to solid surfaces, which serves as a new approach to prevent the growth of antibiotic-resistant microorganisms on surfaces in hospital settings and could be adapted for other target pathogens as well.https://www.mdpi.com/1422-0067/22/22/12544lysin<i>Staphylococcus aureus</i>silica-binding peptideantimicrobial agents immobilizationsurface functionalizationantimicrobial agents |
| spellingShingle | Wan Yang Vijay Singh Gondil Dehua Luo Jin He Hongping Wei Hang Yang Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces International Journal of Molecular Sciences lysin <i>Staphylococcus aureus</i> silica-binding peptide antimicrobial agents immobilization surface functionalization antimicrobial agents |
| title | Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces |
| title_full | Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces |
| title_fullStr | Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces |
| title_full_unstemmed | Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces |
| title_short | Optimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces |
| title_sort | optimized silica binding peptide mediated delivery of bactericidal lysin efficiently prevents i staphylococcus aureus i from adhering to device surfaces |
| topic | lysin <i>Staphylococcus aureus</i> silica-binding peptide antimicrobial agents immobilization surface functionalization antimicrobial agents |
| url | https://www.mdpi.com/1422-0067/22/22/12544 |
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