SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1)
<i>Staphylococcus aureus</i> is one of the major pathogens causing and spreading hospital acquired infections. Since it is highly resistant to new generation antibiotics, novel strategies have to be developed such as the construction of biofunctionalized non-adherent surfaces that will p...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-02-01
|
| Series: | Journal of Functional Biomaterials |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-4983/13/1/21 |
| _version_ | 1797470352989749248 |
|---|---|
| author | Stefanos Pendas Antonis Asiminas Alexandros Katranidis Costas Tsioptsias Maria Pitou Georgios Papadopoulos Theodora Choli-Papadopoulou |
| author_facet | Stefanos Pendas Antonis Asiminas Alexandros Katranidis Costas Tsioptsias Maria Pitou Georgios Papadopoulos Theodora Choli-Papadopoulou |
| author_sort | Stefanos Pendas |
| collection | DOAJ |
| description | <i>Staphylococcus aureus</i> is one of the major pathogens causing and spreading hospital acquired infections. Since it is highly resistant to new generation antibiotics, novel strategies have to be developed such as the construction of biofunctionalized non-adherent surfaces that will prevent its tethering and subsequent spread in the hospital environment. In this frame, the domain D of protein A (SpAD) of <i>S. aureus</i> has been immobilized onto cellulose acetate scaffolds by using the streptavidin/biotin interaction, in order to study its interaction with the A1 domain of von Willebrand factor (vWF A1), a protein essential for hemostasis, found in human plasma. Subsequently, the biofunctionalized cellulose acetate scaffolds were incubated with <i>S. aureus</i> in the presence and absence of vWF A1 at different time periods and their potential to inhibit <i>S. aureus</i> growth was studied with scanning electron microscopy (SEM). The SpAD biofunctionalized scaffolds perceptibly ameliorated the non-adherent properties of the material, and in particular, the interaction between SpAD and vWF A1 effectively inhibited the growth of <i>S. aureus</i>. Thus, the exhibition of significant non-adherent properties of scaffolds addresses their potential use for covering medical equipment, implants, and stents. |
| first_indexed | 2024-03-09T19:36:22Z |
| format | Article |
| id | doaj.art-3035faec21484c6fb7442f5a529cb0fd |
| institution | Directory Open Access Journal |
| issn | 2079-4983 |
| language | English |
| last_indexed | 2024-03-09T19:36:22Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Functional Biomaterials |
| spelling | doaj.art-3035faec21484c6fb7442f5a529cb0fd2023-11-24T01:53:38ZengMDPI AGJournal of Functional Biomaterials2079-49832022-02-011312110.3390/jfb13010021SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1)Stefanos Pendas0Antonis Asiminas1Alexandros Katranidis2Costas Tsioptsias3Maria Pitou4Georgios Papadopoulos5Theodora Choli-Papadopoulou6Laboratory of Biochemistry, Department of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceDivision of Glial Disease and Therapeutics, Center for Translational Neuromedicine, University of Copenhagen, Nørre Alle 14, 24.3.9, 2200 Copenhagen N, DenmarkInstitute of Biological Information Processing IBI-6, Forschungszentrum Jülich (FZJ), 52425 Jülich, GermanyDepartment of Chemical Εngineering, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceLaboratory of Biochemistry, Department of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceDepartment of Biochemistry and Biotechnology, University of Thessaly, Biopolis, 41500 Larissa, GreeceLaboratory of Biochemistry, Department of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece<i>Staphylococcus aureus</i> is one of the major pathogens causing and spreading hospital acquired infections. Since it is highly resistant to new generation antibiotics, novel strategies have to be developed such as the construction of biofunctionalized non-adherent surfaces that will prevent its tethering and subsequent spread in the hospital environment. In this frame, the domain D of protein A (SpAD) of <i>S. aureus</i> has been immobilized onto cellulose acetate scaffolds by using the streptavidin/biotin interaction, in order to study its interaction with the A1 domain of von Willebrand factor (vWF A1), a protein essential for hemostasis, found in human plasma. Subsequently, the biofunctionalized cellulose acetate scaffolds were incubated with <i>S. aureus</i> in the presence and absence of vWF A1 at different time periods and their potential to inhibit <i>S. aureus</i> growth was studied with scanning electron microscopy (SEM). The SpAD biofunctionalized scaffolds perceptibly ameliorated the non-adherent properties of the material, and in particular, the interaction between SpAD and vWF A1 effectively inhibited the growth of <i>S. aureus</i>. Thus, the exhibition of significant non-adherent properties of scaffolds addresses their potential use for covering medical equipment, implants, and stents.https://www.mdpi.com/2079-4983/13/1/21cellulose acetate scaffolds<i>S. aureus</i> protein Avon Willebrand factor A1antibacterial properties |
| spellingShingle | Stefanos Pendas Antonis Asiminas Alexandros Katranidis Costas Tsioptsias Maria Pitou Georgios Papadopoulos Theodora Choli-Papadopoulou SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1) Journal of Functional Biomaterials cellulose acetate scaffolds <i>S. aureus</i> protein A von Willebrand factor A1 antibacterial properties |
| title | SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1) |
| title_full | SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1) |
| title_fullStr | SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1) |
| title_full_unstemmed | SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1) |
| title_short | SpAD Biofunctionalized Cellulose Acetate Scaffolds Inhibit <i>Staphylococcus aureus</i> Adherence in a Coordinating Function with the von Willebrand A1 Domain (vWF A1) |
| title_sort | spad biofunctionalized cellulose acetate scaffolds inhibit i staphylococcus aureus i adherence in a coordinating function with the von willebrand a1 domain vwf a1 |
| topic | cellulose acetate scaffolds <i>S. aureus</i> protein A von Willebrand factor A1 antibacterial properties |
| url | https://www.mdpi.com/2079-4983/13/1/21 |
| work_keys_str_mv | AT stefanospendas spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 AT antonisasiminas spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 AT alexandroskatranidis spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 AT costastsioptsias spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 AT mariapitou spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 AT georgiospapadopoulos spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 AT theodoracholipapadopoulou spadbiofunctionalizedcelluloseacetatescaffoldsinhibitistaphylococcusaureusiadherenceinacoordinatingfunctionwiththevonwillebranda1domainvwfa1 |