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CD45 protein tyrosine phosphatase is a largemolecular mass transmembrane glycoprotein expressed on all hematopoietic cells except erythrocytes.1) It is a member of the receptor-like transmembrane protein tyrosine phosphatase2) (PTPase) family. Expression of CD45 has been shown to be important for activation of both B and T cells via their antigen-specific receptors3,4) and has generated considerable interest in the study of lymphocyte activation as well as a possible target for drug intervention in various auto-immune and/or inflammatory diseases. As a part of our effort to find enzyme inhibitors from microbial sources, we identified a fungal extract which exhibited very potent activity in our CD45 assay. Bioassay directed fractionation of the crude extract yielded a novel pulchellalactam (1) as the active component of this extract. Here we describe the isolation, structure determination and biological characteristics of 1. The recombinant baculovirus was constructed to encode the entire cytoplasmic domain of the human CD45 tyrosine phosphatase protein (CD45-IPD), consisting of two tandem PTPase domains. The recombinant protein was produced in a baculovirus expression system using Sf9 insect cells. Furthermore, the vector was designed to produce a fusion protein containing a poly-

Pulchellalactam: A CD45 Protein Tyrosine Phosphatase Inhibitor from the Marine Fungus Corollospora pulchella.