Bordetella pertussis and Bordetella bronchiseptica filamentous hemagglutinins are processed at different sites

0494800 - MBÚ 2019 RIV US eng J - Článek v odborném periodiku
Jurnečka, David - Man, Petr - Šebo, Peter - Bumba, Ladislav
Bordetella pertussis and Bordetella bronchiseptica filamentous hemagglutinins are processed at different sites.
FEBS Open Bio. Roč. 8, č. 8 (2018), s. 1256-1266. ISSN 2211-5463. E-ISSN 2211-5463
Grant CEP: GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) LM2015043; GA MŠMT(CZ) LM2015064; GA MŠMT(CZ) LQ1604; GA ČR(CZ) GA18-20621S; GA ČR(CZ) GA15-11851S
Institucionální podpora: RVO:61388971
Klíčová slova: bacterial pathogenesis * Bordetella bronchiseptica * Bordetella pertussis
Obor OECD: Microbiology
Impakt faktor: 1.959, rok: 2018

Filamentous hemagglutinin (FHA) mediates adherence and plays an important role in lower respiratory tract infections by pathogenic Bordetellae. The mature FHA proteins of B. pertussis (Bp-FHA) and the B. bronchiseptica (Bb-FHA) are generated by processing of the respective FhaB precursors by the autotransporter subtilisin-type protease SphB1. We have used bottom-up proteomics with differential O-16/O-18 labeling and show that despite high-sequence conservation of the corresponding FhaB segments, the mature Bp-FHA (similar to 230 kDa) and Bb-FHA (similar to 243 kDa) proteins are processed at different sites of FhaB, after the Ala-2348 and Lys-2479 residues, respectively. Moreover, protease surface accessibility probing by oncolumn (on-line) digestion of the Bp-FHA and Bb-FHA proteins yielded different peptide patterns, revealing structural differences in the N-terminal and C-terminal domains of the Bp-FHA and Bb-FHA proteins. These data indicate specific structural variations between the highly homologous FHA proteins.
Trvalý link: http://hdl.handle.net/11104/0287868