Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3
Abstract
Fragments of complement component C3 tag surfaces such as those presented by microbial pathogens or dying host cells for recognition by cells from the innate immune system. Complement receptor (CR) 3 enables efficient binding of complement-tagged surfaces by macrophages and dendritic cells, which eventually transport the CR3-bound material into lymph nodes. The study identifies in atomic details the fragments of CR3 and C3 required for such binding. The structural organization permits concomitant recognition by another complement receptor, namely CR2, expressed on cells of the adaptive immune system, suggesting a structural rationale for the exchange of antigens between leukocytes of the innate and adaptive immune systems critical in the formation of humoral immune responses.
- Publication:
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Proceedings of the National Academy of Science
- Pub Date:
- October 2013
- DOI:
- 10.1073/pnas.1311261110
- Bibcode:
- 2013PNAS..11016426B