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Filamentous Hemagglutinin of Bordetella pertussis Does Not Interact with the β2 Integrin CD11b/CD18
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SYSNO ASEP 0562903 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Filamentous Hemagglutinin of Bordetella pertussis Does Not Interact with the β2 Integrin CD11b/CD18 Tvůrce(i) Golshani, Maryam (MBU-M)
Rahman, Waheed Ur (MBU-M) ORCID
Osičková, Adriana (MBU-M) RID, ORCID
Holubová, Jana (MBU-M) RID, ORCID
Lora, J. (US)
Balashova, N. (US)
Šebo, Peter (MBU-M) RID, ORCID
Osička, Radim (MBU-M) RID, ORCIDČíslo článku 12598 Zdroj.dok. International Journal of Molecular Sciences. - : MDPI
Roč. 23, č. 20 (2022)Poč.str. 24 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova adenylate cyclase toxin ; Bordetella pertussis ; CD11b/CD18 ; filamentous hemagglutinin ; heparin ; integrin Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP LM2018133 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LX22NPO5103 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 000873376600001 EID SCOPUS 85140819219 DOI 10.3390/ijms232012598 Anotace The pertussis agent Bordetella pertussis produces a number of virulence factors, of which the filamentous hemagglutinin (FhaB) plays a role in B. pertussis adhesion to epithelial and phagocytic cells. Moreover, FhaB was recently found to play a crucial role in nasal cavity infection and B. pertussis 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 β2 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 B. pertussis to cells does not involve an interaction between the bacterial surface-associated FhaB and/or mature FHA and the β2 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2023 Elektronická adresa https://www.mdpi.com/1422-0067/23/20/12598
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