Recombinant expression of human mannan-binding lectin

Mannan-binding lectin (MBL) constitutes an important part of the innate imm une defend by effecting the deposition of complement on microbial surfaces. MBL deficiency is among the most common primary immunodeficiencies and is associated with recurrent infections and symptoms of poor immune complex cl earance. Plasma-derived MBL has been used in reconstitution therapy but con cerns over viral contamination and production capacity point to recombinant MBL (rMBL) as a future source of this protein for clinical use. Natural hu man MBL is an oligomer of up to 18 identical polypeptide chains. The synthe sis of rMBL has been accomplished in several mammalian cell lines, however, the recombinant protein differed structurally from natural MEL. In this, s tudy we compare rMBL produced in myeloma cells, Chinese hamster ovary (CHO) cells, human hepatocytes, and human embryonic kidney (HEK) cells. We repor t that rMBL structurally and functionally similar to natural MBL can be obt ained through synthesis in the human embryonic kidney cells followed by sel ective carbohydrate affinity chromatography. (C) 2001 Elsevier Science B.V. All rights reserved.