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Departments of
*
Medical Microbiology and
Clinical Chemistry, Lund University, Malmö University Hospital, Malmö, Sweden
Moraxella catarrhalis ubiquitous surface protein A2 (UspA2) mediates resistance to the bactericidal activity of normal human serum. In this study, an interaction between the complement fluid phase regulator of the classical pathway, C4b binding protein (C4BP), and M. catarrhalis mutants lacking UspA1 and/or UspA2 was analyzed by flow cytometry and a RIA. Two clinical isolates of M. catarrhalis expressed UspA2 at a higher density than UspA1. The UspA1 mutants showed a decreased C4BP binding (37.6% reduction), whereas the UspA2-deficient Moraxella mutants displayed a strongly reduced (94.6%) C4BP binding compared with the wild type. In addition, experiments with recombinantly expressed UspA150–770 and UspA230–539 showed that C4BP (range, 1–1000 nM) bound to the two proteins in a dose-dependent manner. The equilibrium constants (KD) for the UspA150–770 and UspA230–539 interactions with a single subunit of C4BP were 13 µM and 1.1 µM, respectively. The main isoform of C4BP contains seven identical 
-chains and one 
-chain linked together with disulfide bridges, and the -chains contain eight complement control protein (CCP) modules. The UspA1 and A2 bound to the -chain of C4BP, and experiments with C4BP lacking CCP2, CCP5, or CCP7 showed that these three CCPs were important for the Usp binding. Importantly, C4BP bound to the surface of M. catarrhalis retained its cofactor activity as determined by analysis of C4b degradation. Taken together, M. catarrhalis interferes with the classical complement activation pathway by binding C4BP to UspA1 and UspA2.
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