Strategy to create chimeric proteins derived from functional adhesin regions of Mycoplasma pneumoniae for vaccine development.

ABSTRACT: The cell wall-less bacterium Mycoplasma pneumoniae is one of the most common agents of respiratory tract diseases in humans. Adhesin-mediated binding of the bacteria to host cells is a crucial step in colonization and subsequent pathogenesis. For the first time, we expressed 16 recombinant proteins covering almost the whole major adhesin P1 and the adherence-associated protein P30 to characterize these proteins immunologically and functionally. We describe a new in vitro assay using several human cell lines in combination with fluorescence-activated cell sorting analysis to screen antisera raised against the recombinant proteins quantitatively for adherence inhibition activity. The protein derived from the nearly C-terminal part of the P1 adhesin (amino acids [aa] 1288 to 1518) and the pro

SUBMITTER: Schurwanz N 

PROVIDER: S-EPMC2772511 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature