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Originally published In Press as doi:10.1074/jbc.M001491200 on August 14, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33464-33470, October 27, 2000
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Isolation and Characterization of Gomesin, an 18-Residue Cysteine-rich Defense Peptide from the Spider Acanthoscurria gomesiana Hemocytes with Sequence Similarities to Horseshoe Crab Antimicrobial Peptides of the Tachyplesin Family*

Pedro I. Silva Jr.Dagger §, Sirlei Daffre§, and Philippe Bulet||

From the Dagger  Laboratório de Artrópodes, Instituto Butantan, Avenue Vital Brazil, 1500, CEP 05503-900, São Paulo, Brazil, the § Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, Avenue Prof. Lineu Prestes, 1374, CEP 05508-900, São Paulo, Brazil, and the || Institut de Biologie Moléculaire et Cellulaire, UPR 9022, CNRS, "Réponse Immunitaire et Développement chez les Insectes," 15, rue René Descartes, 67084 Strasbourg, France

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 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine alpha -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.

* This work was supported by grants from Fundação de Amparo à Pesquisa do Estado de São Paulo, Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brazil), and from Center National de la Recherche Scientifique (Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The protein sequence reported in this paper has been submitted to the Swiss-Prot Data Bank with accession number P82358.

To whom correspondence should be addressed. Tel.: 55-11-38187272; Fax: 55-11-38187417; E-mail: sidaffre@icb.usp.br.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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