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Isolation, cloning and functional characterization of porcine mannose-binding lectin
A Agah1, M C Montalto, K Young
1Center for Experimental Therapeutics and Reperfusion Injury, Department of Anesthesiology, Perioperative and Pain Medicine, Brigham & Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
Immunology
|April 12, 2001
Summary
Researchers isolated and characterized porcine mannose-binding lectin (MBL), a key innate immunity protein. Porcine MBL shares structural and functional similarities with human MBL, important for xenotransplantation research.
Area of Science:
- Immunology
- Biochemistry
Background:
- Mannose-binding lectin (MBL) is crucial for innate immunity, activating the lectin complement pathway.
- Understanding MBL in pigs is vital for xenotransplantation, but knowledge is limited.
Purpose of the Study:
- To isolate and characterize porcine MBL.
- To investigate its structural and functional conservation with human MBL.
Main Methods:
- Isolation of monomeric forms of MBL from porcine serum.
- Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and protein sequencing.
- Western blot, Northern blot, and functional assays using MBL-deficient human sera.
Main Results:
- Identified three monomeric forms of porcine MBL (30, 32, 34 kDa), suggesting post-translational modification.
- Porcine MBL cDNA showed 64.9% amino acid identity to human MBL.
- Purified porcine MBL restored complement activation in MBL-deficient human sera.
Conclusions:
- Porcine MBL is structurally and functionally conserved with human MBL.
- These findings support the potential use of pigs in xenotransplantation and MBL research.