Details
Zusammenfassung: <jats:p>During infection with<jats:italic>Chlamydia trachomatis</jats:italic>, CD8<jats:sup>+</jats:sup>T cells are primed, even though the bacteria remain confined to a host cell vacuole throughout their developmental cycle. Because CD8<jats:sup>+</jats:sup>T cells recognize antigens processed from cytosolic proteins, the<jats:italic>Chlamydia</jats:italic>antigens recognized by these CD8<jats:sup>+</jats:sup>T cells very likely have access to the host cell cytoplasm during infection. The identity of these<jats:italic>C. trachomatis</jats:italic>proteins has remained elusive, even though their localization suggests they may play important roles in the biology of the organism. Here we use a retroviral expression system to identify Cap1, a 31-kDa protein from<jats:italic>C. trachomatis</jats:italic>recognized by protective CD8<jats:sup>+</jats:sup>T cells. Cap1 contains no strong homology to any known protein. Immunofluorescence microscopy by using Cap1-specific antibody demonstrates that this protein is localized to the vacuolar membrane. Cap1 is virtually identical among the human<jats:italic>C. trachomatis</jats:italic>serovars, suggesting that a vaccine incorporating Cap1 might enable the vaccine to protect against all<jats:italic>C. trachomatis</jats:italic>serovars. The identification of proteins such as Cap1 that associate with the inclusion membrane will be required to fully understand the interaction of<jats:italic>C. trachomatis</jats:italic>with its host cell.</jats:p>
Umfang: 1160-1165
ISSN: 1091-6490
0027-8424
DOI: 10.1073/pnas.98.3.1160