This study used selected MUT and Mur peptides and KODE cell surface engineering technology to create MUT+Mur kodecytes suitable for the detection and identification of RBC antibodies in human serum or plasma. This technology has the potential to create a large range of specialized RBCs for antibody screening and identification.

The cyclic GMP phosphodiesterase gamma-subunit (PDEgamma) was shown to belong to the family of natively unfolded proteins. Increasing temperature transforms the protein into a more ordered (but still relatively disordered) conformation. The C-terminal part of PDEgamma has a high-affinity zinc-binding site (Kd approximately 1 microM), with His75 and His79 being directly involved into the coordination of Zn2+. Zinc-loaded protein remains effectively unfolded. Possible implications of these findings to the functioning of PDEgamma are discussed.

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