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The Moraxella catarrhalis outer membrane protein CD contains two distinct domains specifying adherence to human lung cells.

Most Moraxella catarrhalis isolates express a highly-conserved outer membrane protein of 453 residues designated OMPCD, which has been previously shown to mediate binding to A549 human lung cells. Here, it is reported that two distinct domains of the M. catarrhalis strain O35E OMPCD protein specify adherence. Truncated proteins were expressed in Escherichia coli to demonstrate that OMPCD residues 1-240 as well as 241-400 are important for attachment to A549 cells, and database searches indicated that amino acids 285-299 resemble an adhesive motif found in eukaryotic proteins termed thrombospondin-type 3 repeat (TT3R). Cellular enzyme-linked immunosorbent assay using His-tagged proteins demonstrated that residues 236-300 of OMPCD, containing the TT3R motif, specify adhesive properties. Furthermore, these assays revealed that a purified protein encompassing residues 16-236 binds to A549 cells. The two cell-binding domains of OMPCD were further defined to amino acids 16-150 and 261-300 by utilizing a surface-display system, which was constructed from the M. catarrhalis autotransporter protein McaP, to express foreign peptides on the surface of recombinant bacteria.