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,...
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MDPI AG
2023-02-01
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| Series: | Journal of Personalized Medicine |
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| Online Access: | https://www.mdpi.com/2075-4426/13/2/302 |
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| author | Hongcheng Tang Daxiu Zhang Fenfen Jiang Lifeng Yu Hui Tang Jiafeng Zhu Shuyan Wu Hua Niu |
| author_facet | Hongcheng Tang Daxiu Zhang Fenfen Jiang Lifeng Yu Hui Tang Jiafeng Zhu Shuyan Wu Hua Niu |
| author_sort | Hongcheng Tang |
| collection | DOAJ |
| description | <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. |
| first_indexed | 2024-03-11T08:34:37Z |
| format | Article |
| id | doaj.art-780862ab1bfe44dab8cec0bfc47de3c3 |
| institution | Directory Open Access Journal |
| issn | 2075-4426 |
| language | English |
| last_indexed | 2024-03-11T08:34:37Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
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| series | Journal of Personalized Medicine |
| spelling | doaj.art-780862ab1bfe44dab8cec0bfc47de3c32023-11-16T21:33:32ZengMDPI AGJournal of Personalized Medicine2075-44262023-02-0113230210.3390/jpm13020302Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAPHongcheng Tang0Daxiu Zhang1Fenfen Jiang2Lifeng Yu3Hui Tang4Jiafeng Zhu5Shuyan Wu6Hua Niu7Department of Microbiology, School of Biology & Basic Medical Sciences, Soochow University, Suzhou 215123, ChinaClinical Laboratory Center, Affiliated Hospital of Guilin Medical University, Guilin 541001, ChinaLaboratory of Hepatobiliary and Pancreatic Surgery, Affiliated Hospital of Guilin Medical University, Guilin 541001, ChinaClinical Laboratory Center, Affiliated Hospital of Guilin Medical University, Guilin 541001, ChinaClinical Laboratory Center, Affiliated Hospital of Guilin Medical University, Guilin 541001, ChinaDepartment of Microbiology, School of Biology & Basic Medical Sciences, Soochow University, Suzhou 215123, ChinaDepartment of Microbiology, School of Biology & Basic Medical Sciences, Soochow University, Suzhou 215123, ChinaLaboratory of Hepatobiliary and Pancreatic Surgery, Affiliated Hospital of Guilin Medical University, Guilin 541001, China<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.https://www.mdpi.com/2075-4426/13/2/302<i>Anaplasma phagocytophilum</i>type IV secretion systemcell adhesionnucleolinactin filamentspodosomes |
| spellingShingle | Hongcheng Tang Daxiu Zhang Fenfen Jiang Lifeng Yu Hui Tang Jiafeng Zhu Shuyan Wu Hua Niu Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAP Journal of Personalized Medicine <i>Anaplasma phagocytophilum</i> type IV secretion system cell adhesion nucleolin actin filaments podosomes |
| title | Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAP |
| title_full | Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAP |
| title_fullStr | Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAP |
| title_full_unstemmed | Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAP |
| title_short | Enhancement of Cell Adhesion by <i>Anaplasma phagocytophilum</i> Nucleolin-Interacting Protein AFAP |
| title_sort | enhancement of cell adhesion by i anaplasma phagocytophilum i nucleolin interacting protein afap |
| topic | <i>Anaplasma phagocytophilum</i> type IV secretion system cell adhesion nucleolin actin filaments podosomes |
| url | https://www.mdpi.com/2075-4426/13/2/302 |
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