Structure, heterologous expression, and adhesive properties of the P(0)-like myelin glycoprotein IP1 of trout CNS.

The IP1 protein of trout CNS myelin as well as an IP1/P(0) chimeric protein were stably expressed in CHO cells. Successful targeting of the recombinant proteins to the membrane surface was verified by immunofluorescence staining. Full-length expression of IP1 could be confirmed by Western blot analysis of proteins extracted from stably transfected CHO-cells. The adhesive properties of IP1 were studied by an in vitro aggregation assay in which microscopic examination was combined with electronic particle counting. While IP1 conveyed only a weak increase in cell aggregation of transfected CHO cells, the IP1/P0 chimera was much more effective. In the presence of specific antibodies, cell aggregation was strongly reduced. The adhesive properties of P(0)-like proteins are discussed considering recent crystallographic data on the atomic structure of the extracellular domain of mammalian P(0).