Biosensors for the Detection of Interaction between Legionella pneumophila Collagen-Like Protein and Glycosaminoglycans
The adhesin Legionella collagen-like (Lcl) protein can bind to extracellular matrix components and mediate the binding of Legionella pneumophila to host cells. In this study, electrochemical impedance spectroscopy (EIS) and surface plasmon resonance (SPR)-based biosensors were employed to characterize these interactions between glycosaminoglycans (GAGs) and the adhesin Lcl protein. Fucoidan displayed a high affinity (KD 18 nM) for Lcl protein. Chondroitin sulfate A and dermatan sulfate differ in the position of a carboxyl group replacing D-glucuronate with D-iduronate. Our results indicated that the presence of D-iduronate in dermatan sulfate strongly hindered its interaction with Lcl. These biophysical studies provided valuable information in our understanding of adhesin-ligand interactions related to Legionella pneumophila infections.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2018 |
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| Erschienen: |
2018 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:18 |
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| Enthalten in: |
Sensors (Basel, Switzerland) - 18(2018), 8 vom: 14. Aug. |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Su, Han [VerfasserIn] |
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| Links: |
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| Themen: |
9007-34-5 |
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| Anmerkungen: |
Date Completed 21.01.2019 Date Revised 21.01.2019 published: Electronic Citation Status MEDLINE |
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| doi: |
10.3390/s18082668 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM287497526 |
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| 520 | |a The adhesin Legionella collagen-like (Lcl) protein can bind to extracellular matrix components and mediate the binding of Legionella pneumophila to host cells. In this study, electrochemical impedance spectroscopy (EIS) and surface plasmon resonance (SPR)-based biosensors were employed to characterize these interactions between glycosaminoglycans (GAGs) and the adhesin Lcl protein. Fucoidan displayed a high affinity (KD 18 nM) for Lcl protein. Chondroitin sulfate A and dermatan sulfate differ in the position of a carboxyl group replacing D-glucuronate with D-iduronate. Our results indicated that the presence of D-iduronate in dermatan sulfate strongly hindered its interaction with Lcl. These biophysical studies provided valuable information in our understanding of adhesin-ligand interactions related to Legionella pneumophila infections | ||
| 650 | 4 | |a Journal Article | |
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| 650 | 4 | |a electrochemical impedance spectroscopy | |
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| 650 | 4 | |a surface plasmon resonance | |
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| 700 | 1 | |a Kerman, Kagan |e verfasserin |4 aut | |
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