Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 275, Issue 43, Pages 33464-33470Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M001491200
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We have purified a small size antimicrobial peptide, named gomesin, from the hemocytes of the unchallenged tarantula spider Acanthoscurria gomesiana, Gomesin has a molecular mass of 2270.4 Ha, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine Lu-amide, and four cysteine residues forming two disulfide bridges, This peptide shows marked sequence similarities to antimicrobial peptides from other arthropods such as tachyplesin and polyphemusin from horseshoe crabs and androctonin from scorpions, Interestingly, it also shows sequence similarities to protegrins, antimicrobial peptides from porcine leukocytes, Gomesin strongly affects bacterial growth, as well as the development of filamentous fungi and yeast. In addition, we showed that gomesin affects the viability of the parasite Leishmania amazonensis.
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