Chlamydia pneumoniae is a bacterial obligate intracellular parasite with a
developmental cycle common to all members of the genus Chlamydia, Like othe
r chlamydiae, the developmental cycle of C. pneumoniae occurs entirely with
in a membrane-bound intracellular vacuole, termed an inclusion, that is non
-fusogenic with endosomal or lysosomal compartments. To characterize the ve
sicular interactions of the C. pneumoniae inclusion, we used a fluorescent
analogue of ceramide, (N-[7-(4-nitrobenzo-2-oxa-1,3-diazole)]-6-aminocaproy
l-D-erythro-sphingosine (C-6-NBD-Cer), that has previously been used to cha
racterize the endogenous synthesis and transport of sphingolipids from the
Golgi apparatus to Chlamydia trachomatis and Chlamydia psittaci inclusions.
Sphingolipids are trafficked to C. pneumoniae inclusions in a time-, tempe
rature- and energy-dependent manner with properties very similar to the del
ivery of sphingomyelin to C. trachomatis inclusions. These results indicate
that interactions of the inclusion with a subset of sphingomyelin-containi
ng exocytic vesicles is a property common to all species of chlamydiae.