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The transferrin binding protein genes (tbpA andtbpB ) from two strains ofMoraxella catarrhalis have been cloned and sequenced. The genomic organization of theM. catarrhalis transferrin binding protein genes is unique among known bacteria in thattbpA precedestbpB and there is a third gene located between them. The deduced sequences of theM. catarrhalis TbpA proteins from two strains were 98% identical, while those of the TbpB proteins from the same strains were 63% identical and 70% similar. The third gene, tentatively calledorf3 , encodes a protein of approximately 58 kDa that is 98% identical between the two strains. ThetbpB genes from four additional strains ofM. catarrhalis were cloned and sequenced, and two potential families of TbpB proteins were identified based on sequence similarities. Recombinant TbpA (rTbpA), rTbpB, and rORF3 proteins were expressed inEscherichia coli and purified. rTbpB was shown to retain its ability to bind human transferrin after transfer to a membrane, but neither rTbpA nor rORF3 did. Monospecific anti-rTbpA and anti-rTbpB antibodies were generated and used for immunoblot analysis, which demonstrated that epitopes ofM. catarrhalis TbpA and TbpB were antigenically conserved and that there was constitutive expression of thetbp genes. In the absence of an appropriate animal model, anti-rTbpA and anti-rTbpB antibodies were tested for their bactericidal activities. The anti-rTbpA antiserum was not bactericidal, but anti-rTbpB antisera were found to kill heterologous strains within the same family. Thus, if bactericidal ability is clinically relevant, a vaccine comprising multiple rTbpB antigens may protect againstM. catarrhalis disease.

The Transferrin Binding Protein B of Moraxella catarrhalis Elicits Bactericidal Antibodies and Is a Potential Vaccine Antigen