The genome of the obligate intracellular bacterium Chlamydia pneumoniae CWL
029 encodes a family of 21 proteins with predicted outer membrane localizat
ion. These polymorphic membrane proteins (Pmps) are heterogeneous in both a
mino acid sequence and predicted size but are unified by the conserved amin
o acid motifs GGAI and FXXN repeated in the N-terminal half of each protein
. Reverse transcriptase PCR analysis showed that all pmp genes are transcri
bed. To determine whether all proteins are expressed, specific antisera wer
e generated by immunization with mutually exclusive synthetic peptides repr
esenting each of the 21 predicted Pmps. Each antiserum reacted with, and wa
s typically immunospecific for, the corresponding peptide immunogen by enzy
me-linked immunosorbent assay. Western blot analyses of purified elementary
bodies showed that 11 of the 21 Pmps were detectable. Attempts to demonstr
ate by Sarykosyl fractionation that the Pmps were localized to the outer me
mbrane revealed that several of the Pmps were unstable and readily degraded
. Analyses of additional C. pneumoniae strains showed that although some Pm
ps are conserved, others vary between strains, in both molecular weight and
level of expression.