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CD8+T cells recognize an inclusion membrane-associated protein from the vacuolar pathogenChlamydia trachomatis
- Source :
- Proceedings of the National Academy of Sciences. 98:1160-1165
- Publication Year :
- 2001
- Publisher :
- Proceedings of the National Academy of Sciences, 2001.
-
Abstract
- During infection withChlamydia trachomatis, CD8+T cells are primed, even though the bacteria remain confined to a host cell vacuole throughout their developmental cycle. Because CD8+T cells recognize antigens processed from cytosolic proteins, theChlamydiaantigens recognized by these CD8+T cells very likely have access to the host cell cytoplasm during infection. The identity of theseC. trachomatisproteins 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 fromC. trachomatisrecognized by protective CD8+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 humanC. trachomatisserovars, suggesting that a vaccine incorporating Cap1 might enable the vaccine to protect against allC. trachomatisserovars. The identification of proteins such as Cap1 that associate with the inclusion membrane will be required to fully understand the interaction ofC. trachomatiswith its host cell.
- Subjects :
- Molecular Sequence Data
Restriction Mapping
Chlamydia trachomatis
Vacuole
CD8-Positive T-Lymphocytes
medicine.disease_cause
Polymerase Chain Reaction
Cell Line
Mice
Bacterial Proteins
Antigen
medicine
Animals
Cytotoxic T cell
Cells, Cultured
Gene Library
Mice, Inbred BALB C
Multidisciplinary
Base Sequence
biology
Membrane Proteins
Biological Sciences
Immunohistochemistry
Virology
Oligodeoxyribonucleotides
Membrane protein
Vacuoles
Host cell cytoplasm
biology.protein
Female
Antibody
CD8
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 98
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....30fb4f5b67b5d7702b25408216bd1dbb