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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MDPI AG
2021
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oai:doaj.org-article:e2e40985d0c243509b0097a50e781d412021-11-25T17:57:39ZOptimized Silica-Binding Peptide-Mediated Delivery of Bactericidal Lysin Efficiently Prevents <i>Staphylococcus aureus</i> from Adhering to Device Surfaces10.3390/ijms2222125441422-00671661-6596https://doaj.org/article/e2e40985d0c243509b0097a50e781d412021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12544https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Staphylococcal-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.Wan YangVijay Singh GondilDehua LuoJin HeHongping WeiHang YangMDPI AGarticlelysin<i>Staphylococcus aureus</i>silica-binding peptideantimicrobial agents immobilizationsurface functionalizationantimicrobial agentsBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12544, p 12544 (2021) |
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lysin <i>Staphylococcus aureus</i> silica-binding peptide antimicrobial agents immobilization surface functionalization antimicrobial agents Biology (General) QH301-705.5 Chemistry QD1-999 |
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lysin <i>Staphylococcus aureus</i> silica-binding peptide antimicrobial agents immobilization surface functionalization antimicrobial agents Biology (General) QH301-705.5 Chemistry QD1-999 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 |
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. |
format |
article |
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 |
title |
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_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_sort |
optimized silica-binding peptide-mediated delivery of bactericidal lysin efficiently prevents <i>staphylococcus aureus</i> from adhering to device surfaces |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/e2e40985d0c243509b0097a50e781d41 |
work_keys_str_mv |
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