Enhancement of Cell Adhesion by <i<Anaplasma phagocytophilum</i< Nucleolin-Interacting Protein AFAP
<i<Anaplasma phagocytophilum</i<, the aetiologic agent of human granulocytic anaplasmosis (HGA), is an obligate intracellular Gram-negative bacterium. During infection, <i<A. phagocytophilum</i< enhances the adhesion of neutrophils to the infected endothelial cells. However, the bacterial factors contributing to this phenomenon remain unknown. In this study, we characterized a type IV secretion system substrate of <i<A. phagocytophilum</i<, AFAP (an actin filament-associated <i<Anaplasma phagocytophilum</i< protein) and found that it dynamically changed its pattern and subcellular location in cells and enhanced cell adhesion. Tandem affinity purification combined with mass spectrometry identified host nucleolin as an AFAP-interacting protein. Further study showed the disruption of nucleolin by RNA interference, and the treatment of a nucleolin-binding DNA aptamer AS1411 attenuated AFAP-mediated cell adhesion, indicating that AFAP enhanced cell adhesion in a nucleolin-dependent manner. The characterization of cell adhesion-enhancing AFAP and the identification of host nucleolin as its interaction partner may help understand the mechanism underlying <i<A. phagocytophilum</i<-promoting cell adhesion, facilitating the elucidation of HGA pathogenesis..
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:13 |
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| Enthalten in: |
Journal of Personalized Medicine - 13(2023), 2, p 302 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Hongcheng Tang [VerfasserIn] |
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| Links: |
doi.org [kostenfrei] |
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| Themen: |
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| doi: |
10.3390/jpm13020302 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
DOAJ080237444 |
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| 520 | |a <i<Anaplasma phagocytophilum</i<, the aetiologic agent of human granulocytic anaplasmosis (HGA), is an obligate intracellular Gram-negative bacterium. During infection, <i<A. phagocytophilum</i< enhances the adhesion of neutrophils to the infected endothelial cells. However, the bacterial factors contributing to this phenomenon remain unknown. In this study, we characterized a type IV secretion system substrate of <i<A. phagocytophilum</i<, AFAP (an actin filament-associated <i<Anaplasma phagocytophilum</i< protein) and found that it dynamically changed its pattern and subcellular location in cells and enhanced cell adhesion. Tandem affinity purification combined with mass spectrometry identified host nucleolin as an AFAP-interacting protein. Further study showed the disruption of nucleolin by RNA interference, and the treatment of a nucleolin-binding DNA aptamer AS1411 attenuated AFAP-mediated cell adhesion, indicating that AFAP enhanced cell adhesion in a nucleolin-dependent manner. The characterization of cell adhesion-enhancing AFAP and the identification of host nucleolin as its interaction partner may help understand the mechanism underlying <i<A. phagocytophilum</i<-promoting cell adhesion, facilitating the elucidation of HGA pathogenesis. | ||
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