The sequence of the non-typable (NTHi) P5 outer-membrane protein from a range of clinical isolates is presented and represents the first analysis of the heterogeneity in P5 from NTHi isolates from diverse anatomical sites. the basis of the previously observed inter-strain variation in the electrophoretic mobility is attributed to heterogeneity in three hypervariable regions. Alignment of the P5 sequences identified regions which are highly conserved and align with the transmembrane region predicted for the homologous protein, OmpA. Variable regions correspond to surface-exposed loops, of which the first loop falls into subclasses. However, these subclasses fail to correlate with anatomical predisposition. Although P5 has been proposed as a fimbrial protein composed of coiled coils, both structural analysis by circular dichroism of purified P5 and computer analysis of the multiply aligned sequences predict a high proportion of β strand with no evidence of coiled coil structure. A detailed model of P5 is presented.


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