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J Biol Chem, Vol. 274, Issue 36, 25330-25334, September 3, 1999

Antimicrobial Activity of a Bovine Hemoglobin Fragment in the Tick Boophilus microplus

Andréa C. Fogaça, Pedro I. da Silva Jr.^§, M. Terêsa M. Miranda^¶, Antonio G. Bianchi, Antonio Miranda, Paulo E. M. Ribolla, and Sirlei Daffre

From the  Departamento de Parasitologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, Av. Prof. Lineu Prestes, 1374, CEP 05508-900, the ^§ Laboratório de Artrópodes, Instituto Butantan, Av. Vital Brazil, 1500, CEP 05503-900, the ^¶ Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes, 748, CEP 05508-900, and the  Departamento de Biofísica, Universidade Federal de São Paulo, Rua 03 de Maio, 100, CEP 04044-020, São Paulo, Brazil

Antifungal and antibacterial activities were detected in the hemolymph and gut contents of the cattle tick, Boophilus microplus. A peptide with antibacterial activity from the tick gut contents was purified to homogeneity by reversed-phase chromatography. The molecular mass of the purified peptide was 3,205.7 Da, measured by matrix-assisted laser desorption/ionization mass spectrometry. The amino acid sequence was obtained by Edman degradation and showed that the peptide was identical to a fragment of the bovine -hemoglobin. A synthetic peptide based on the sequence obtained showed characterization data identical to those of the isolated material, confirming its structure. The synthetic peptide was active in micromolar concentrations against Gram-positive bacteria and fungi. These data led us to conclude that the antibacterial activity detected in tick gut contents is the result of enzymatic processing of a host protein, hemoglobin. This activity may be used by ticks as a defense against microorganisms.

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