Filamentous Hemagglutinin of Bordetella pertussis Does Not Interact with the β2 Integrin CD11b/CD18

被引:2
作者
Golshani, Maryam [1 ]
Rahman, Waheed Ur [1 ]
Osickova, Adriana [1 ]
Holubova, Jana [1 ]
Lora, Jinery [2 ]
Balashova, Nataliya [2 ]
Sebo, Peter [1 ]
Osicka, Radim [1 ]
机构
[1] Czech Acad Sci, Inst Microbiol, Videnska 1083, Prague 14220, Czech Republic
[2] Univ Penn, Sch Dent Med, Dept Basic & Translat Sci, 240 S 40th St, Philadelphia, PA 19104 USA
关键词
adenylate cyclase toxin; Bordetella pertussis; CD11b/CD18; filamentous hemagglutinin; heparin; integrin; ADENYLATE-CYCLASE TOXIN; GLY-ASP SEQUENCE; BACTERIAL ADHESIN; EPITHELIAL-CELLS; RECOGNITION; INVASION; BINDING; DOMAIN; BRONCHISEPTICA; PATHOGENESIS;
D O I
10.3390/ijms232012598
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 similar to 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 beta(2) 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 beta(2) 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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页数:24
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