Abstract
A cDNA encoding a putative antimicrobial peptide (named PP-1) was obtained using a rapid amplification of cDNA ends from the Asian earthworm, Pheretima tschiliensis. PP-1 showed 77.6% homology with the antimicrobial peptide lumbricin I isolated from the earthworm Lumbricus rubellus. PP-1 lacked an obvious signal peptide sequence. RT-PCR analysis demonstrated that this gene was expressed mainly in the body wall. PP-1 was expressed in Escherichia coli as a fusion protein with a maltoze-binding protein. A polyclonal antiserum was raised in mice using this recombinant fusion protein as antigen. Immunohistochemical studies showed that PP-1 was only in the mucus of the epidermis.
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