Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18
The pertussis agent <i>Bordetella pertussis</i> produces a number of virulence factors, of which the filamentous hemagglutinin (FhaB) plays a role in <i>B. pertussis</i> adhesion to epithelial and phagocytic cells. Moreover, FhaB was recently found to play a crucial role in n...
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MDPI AG
2022-10-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/20/12598 |
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| author | Maryam Golshani Waheed Ur Rahman Adriana Osickova Jana Holubova Jinery Lora Nataliya Balashova Peter Sebo Radim Osicka |
| author_facet | Maryam Golshani Waheed Ur Rahman Adriana Osickova Jana Holubova Jinery Lora Nataliya Balashova Peter Sebo Radim Osicka |
| author_sort | Maryam Golshani |
| collection | DOAJ |
| description | The pertussis agent <i>Bordetella pertussis</i> produces a number of virulence factors, of which the filamentous hemagglutinin (FhaB) plays a role in <i>B. pertussis</i> adhesion to epithelial and phagocytic cells. Moreover, FhaB was recently found to play a crucial role in nasal cavity infection and <i>B. pertussis</i> transmission to new hosts. The 367 kDa FhaB protein translocates through an FhaC pore to the outer bacterial surface and is eventually processed to a ~220 kDa N-terminal FHA fragment by the SphB1 protease. A fraction of the mature FHA then remains associated with bacterial cell surface, while most of FHA is shed into the bacterial environment. Previously reported indirect evidence suggested that FHA, or its precursor FhaB, may bind the β<sub>2</sub> integrin CD11b/CD18 of human macrophages. Therefore, we assessed FHA binding to various cells producing or lacking the integrin and show that purified mature FHA does not bind CD11b/CD18. Further results then revealed that the adhesion of <i>B. pertussis</i> to cells does not involve an interaction between the bacterial surface-associated FhaB and/or mature FHA and the β<sub>2</sub> integrin CD11b/CD18. In contrast, FHA binding was strongly inhibited at micromolar concentrations of heparin, corroborating that the cell binding of FHA is ruled by the interaction of its heparin-binding domain with sulfated glycosaminoglycans on the cell surface. |
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| last_indexed | 2024-03-09T20:05:18Z |
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| spelling | doaj.art-e23a5aa7fd7d40388b6390cfea1720992023-11-24T00:34:00ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-10-0123201259810.3390/ijms232012598Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18Maryam Golshani0Waheed Ur Rahman1Adriana Osickova2Jana Holubova3Jinery Lora4Nataliya Balashova5Peter Sebo6Radim Osicka7Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech RepublicInstitute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech RepublicInstitute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech RepublicInstitute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech RepublicDepartment of Basic and Translational Sciences, School of Dental Medicine, University of Pennsylvania, 240 S. 40th St., Philadelphia, PA 19104, USADepartment of Basic and Translational Sciences, School of Dental Medicine, University of Pennsylvania, 240 S. 40th St., Philadelphia, PA 19104, USAInstitute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech RepublicInstitute of Microbiology of the Czech Academy of Sciences, Videnska 1083, 142 20 Prague, Czech RepublicThe pertussis agent <i>Bordetella pertussis</i> produces a number of virulence factors, of which the filamentous hemagglutinin (FhaB) plays a role in <i>B. pertussis</i> adhesion to epithelial and phagocytic cells. Moreover, FhaB was recently found to play a crucial role in nasal cavity infection and <i>B. pertussis</i> transmission to new hosts. The 367 kDa FhaB protein translocates through an FhaC pore to the outer bacterial surface and is eventually processed to a ~220 kDa N-terminal FHA fragment by the SphB1 protease. A fraction of the mature FHA then remains associated with bacterial cell surface, while most of FHA is shed into the bacterial environment. Previously reported indirect evidence suggested that FHA, or its precursor FhaB, may bind the β<sub>2</sub> integrin CD11b/CD18 of human macrophages. Therefore, we assessed FHA binding to various cells producing or lacking the integrin and show that purified mature FHA does not bind CD11b/CD18. Further results then revealed that the adhesion of <i>B. pertussis</i> to cells does not involve an interaction between the bacterial surface-associated FhaB and/or mature FHA and the β<sub>2</sub> integrin CD11b/CD18. In contrast, FHA binding was strongly inhibited at micromolar concentrations of heparin, corroborating that the cell binding of FHA is ruled by the interaction of its heparin-binding domain with sulfated glycosaminoglycans on the cell surface.https://www.mdpi.com/1422-0067/23/20/12598adenylate cyclase toxin<i>Bordetella pertussis</i>CD11b/CD18filamentous hemagglutininheparinintegrin |
| spellingShingle | Maryam Golshani Waheed Ur Rahman Adriana Osickova Jana Holubova Jinery Lora Nataliya Balashova Peter Sebo Radim Osicka Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18 International Journal of Molecular Sciences adenylate cyclase toxin <i>Bordetella pertussis</i> CD11b/CD18 filamentous hemagglutinin heparin integrin |
| title | Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18 |
| title_full | Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18 |
| title_fullStr | Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18 |
| title_full_unstemmed | Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18 |
| title_short | Filamentous Hemagglutinin of <i>Bordetella pertussis</i> Does Not Interact with the β<sub>2</sub> Integrin CD11b/CD18 |
| title_sort | filamentous hemagglutinin of i bordetella pertussis i does not interact with the β sub 2 sub integrin cd11b cd18 |
| topic | adenylate cyclase toxin <i>Bordetella pertussis</i> CD11b/CD18 filamentous hemagglutinin heparin integrin |
| url | https://www.mdpi.com/1422-0067/23/20/12598 |
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