Autor(es)Lowenberger, C; Charlet, M; Vizioli, J; Kamal, S; Richman, A; Christensen, BM; Bulet, P

ResumoAn antimicrobial peptide belonging to the cecropin family was isolated from the hemolymph of bacteria-challenged adult Aedes aegypti. This new peptide, named cecropin A, was purified to homogeneity and fully characterized after cDNA cloning. The 34-residue A. aegypti cecropin A is different from the majority of reported insect cecropins in that it is devoid of a tryptophan residue and C-terminal amidation. The importance of these two structural features on the activity spectrum was investigated using a chemically synthesized peptide. A comparison of the antimicrobial activity spectrum of A. aegypti and Drosophila cecropin A showed a lower activity for the mosquito molecule. A. aegypti cecropin mRNA expression was not detected by Northern blot or reverse transcription-polymerase chain reaction analysis in any immature stage of the mosquito, nor in naive adults, but it was observed in challenged adults 6 h after bacteria inoculation, and it continued over 7-10 days.

Palavras-ChaveSporogonic Development; Antibacterial Peptide; Plasmodium-Berghei; Insect Immunity; Differential Display; Synthetic Peptide; Anopheles-Gambiae; Bombyx-Mori; Sequence; Drosophila

ImprentaJournal of Biological Chemistry, v. 274, n. 29, p. 20092-20097, 1999

DescritoresAedes aegypti - PCR detection ; Aedes aegypti - RT-PCR

Data de Publicação:1999