An antimicrobial peptide of the earthworm Pheretima tschiliensis: cDNA cloning, expression and immunolocalization.
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.
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D000890:Anti-Infective Agents / Q000378:metabolism; D003001:Cloning, Molecular / Q000379:methods*; D018076:DNA, Complementary / Q000235:genetics; D004817:Epidermis / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000235:genetics; D007118:Immunoassay; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009092:Mucous Membrane / Q000378:metabolism*; D009835:Oligochaeta / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D010455:Peptides; D015202:Protein Engineering / Q000379:methods; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014018:Tissue Distribution
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D018076:DNA, Complementary; D010455:Peptides; D011993:Recombinant Fusion Proteins