| Description | Chlamydia is a genus of bacteria, which causes the most common bacterial sexually transmitted diseases. They are obligate intracellular bacterial pathogens. Members of this genus lack a peptidoglycan layer, but as a substitute, it has been proposed that they have several cysteine rich membrane proteins. This includes the major outer membrane protein (MOMP). These form disulphide bonds to provide rigidity to the cell wall. The alignment of the amino acid sequences of the MOMP from various serovars of Chlamydia show that they have between seven and ten cysteine residues; seven of which are highly conserved [ ]. The MOMP has been the focus of efforts to produce a vaccine for Chlamydia trachomatis [].The 15kDa cysteine-rich protein in this entry is a multi-pass outer membrane protein. They are associated with the differentiation of reticulate bodies (RBs) into elementary bodies (EBs) [ ]. They immunolocalise to the inclusion membrane, which is the membrane that surrounds the intracellular parasite. These proteins are recognised by CD8+ T cells in both human and mouse infections, suggesting they gain access to the host cytoplasm. | Name | Chlamydia 15kDa cysteine-rich outer membrane |
| Short Name | CRPA | Type | Family |
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