CEACAM3: An innate immune receptor directed against human-restricted bacterial pathogens
| Autor: | Stefan Pils, Christof R. Hauck, Axel Meyer, Dave T. Gerrard |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Microbiology (medical)
Gram-negative bacteria Signal transduction Cell adhesion molecule 3 Microbiology Evolution Molecular Phagocytosis ITAM ddc:570 Gram-Negative Bacteria Humans Receptor Gene chemistry.chemical_classification Genetics Innate immune system biology Host pathogen coevolution General Medicine biology.organism_classification Carcinoembryonic Antigen Infectious Diseases chemistry Glycoprotein Function (biology) Signal Transduction |
| Zdroj: | International Journal of Medical Microbiology. 298:553-560 |
| ISSN: | 1438-4221 |
| DOI: | 10.1016/j.ijmm.2008.04.005 |
| Popis: | Carcinoembryonic antigen-related cell adhesion molecule 3 (CEACAM3) is an immunoglobulin-related glycoprotein exclusively expressed on granulocytes. In contrast to other members of the CEACAM family, CEACAM3 does not support cell-cell adhesion, but rather mediates the opsonin-independent recognition and elimination of a restricted set of human-specific Gram-negative bacterial pathogens including Neisseria gonorrhoeae, Haemophilus influenzae, and Moraxella catarrhalis. Within the last 4 years, molecular determinants of CEACAM3 function and CEACAM3-initiated signaling pathways have been elucidated. Sequence comparison between CEACAM3 and other CEACAM family members points to a chimeric origin of this receptor with the bacteria-binding extracellular domain and the function-promoting intracellular domain derived from different genes. This review summarizes the current knowledge about the structure-function relationship of CEACAM3 and tries to combine these molecular aspects with a plausible scenario concerning the evolutionary origin of this phagocyte receptor in the light of host-pathogen adaptation. |
| Databáze: | OpenAIRE |
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