Y. Iijima et al., CHARACTERIZATION OF CHLAMYDIA-PNEUMONIAE SPECIES-SPECIFIC PROTEINS IMMUNODOMINANT IN HUMANS, Journal of clinical microbiology, 32(3), 1994, pp. 583-588
Proteins of Chlamydia pneumoniae immunodominant in humans were charact
erized with the sera of 13 patients who were not likely to have been e
xposed to C. trachomatis or C. psittaci. The serological responses amo
ng these patients were similar on a qualitative basis, but some differ
ences were found quantitatively. However, the serological responses of
the patients who were infected with C. pneumoniae differed markedly f
rom those of two patients who were infected with C. trachomatis and tw
o who were infected with C. psittaci and those of mice that were trans
tracheally infected with C. pneumoniae. Among proteins immunodominant
in the patients who were infected with C. pneumoniae, a 40-kDa major o
uter membrane protein was genus specific and 53-, 46-, and 43-kDa prot
eins were species specific in their reactions with the majority of the
human sera used. A few sera reacted Strongly with a 73-kDa protein ge
nus specifically. Some proteins with weak immunogenicity exhibited spe
cies specificity. An antigenic analysis with human sera and murine mon
oclonal antibodies against the 53-kDa protein showed that the antigeni
cities were strictly conserved among the seven strains of C. pneumonia
e tested. The genus-specific 73-kDa protein was solubilized with octyl
glucoside. All of the species-specific immunodominant proteins were so
lubilized with sodium dodecyl sulfate, but the genus-specific major ou
ter membrane protein was not. These results suggest that a serological
diagnosis of C. pneumoniae infection could be achieved species specif
ically by comparison of the serum responses to sodium dodecyl sulfate-
and octylglucoside-soluble fractions.