Establishing expression methods for successful crystal of MID962-1200

TL;DRAbstract

Abstract Moraxella catarrhalis is a new pathogenic, gram negative bacterium that is the cause of many respiratory tract infections. MID was found to be a unique protein with Ig binding capacities. Moraxella catarrhalis immunoglobulin D (IgD)-binding protein (MID) is an outer membrane protein that has specific binding affinity to the soluble cell bound human IgD. A short fragment of MID comprised of 238 amino acid (MID962-1200) contains this IgD binding capacity. MID-deficient Moraxella catarrhalis does not bind to human IgD B cells. MID962-1200 stimulates B cell in the presence of IL-2 and IL-6. The monomeric form of the fragment of the MID protein is about ~200 kDa. The oligomeric form of the fragment has 20 fold stronger binding to IgD than the monomer from. The truncated MID962-1200 is efficiently binding to the IgD serum and purified IgD(κ) and IgD(λ) but not to the IgM,IgG,IgA myeloma sera. In this paper we examined the expression and purification of MID962-1200 by the affinity

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