The defensin peptide of the malaria vector mosquito Anopheles gambiae: antimicrobial activities and expression in adult mosquitoes

Archive ouverte

Vizioli, Jacopo | Richman, Adam | Uttenweiler-Joseph, Sandrine | Blass, Claudia | Bulet, Philippe

Edité par CCSD ; Elsevier -

International audience. A recombinant Anopheles gambiae defensin peptide was used to define the antimicrobial activity spectrum against bacteria, filamentous fungi and yeast. Results showed that most of the Gram-positive bacterial species tested were sensitive to the recombinant peptide in a range of concentrations from 0.1 to 0.75 microM. No activity was detected against Gram-negative bacteria, with the exception of some E. coli strains. Growth inhibitory activity was detected against some species of filamentous fungi. Defensin was not active against yeast. The kinetics of bactericidal and fungicidal effects were determined for Micrococcus luteus and Neurospora crassa, respectively. Differential mass spectrometry analysis was used to demonstrate induction of defensin in the hemolymph of bacteria-infected adult female mosquitoes. Native peptide levels were quantitated in both hemolymph and midgut tissues. The polytene chromosome position of the defensin locus was mapped by in situ hybridization.

Consulter en ligne

Suggestions

Du même auteur

Antimicrobial Activity Spectrum, cDNA Cloning, and mRNA Expression of a Newly Isolated Member of the Cecropin Family from the Mosquito Vector Aedes aegypti

Archive ouverte | Lowenberger, Carl | CCSD

International audience

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

Archive ouverte | Vizioli, Jacopo | CCSD

International audience. A novel mosquito antimicrobial peptide, gambicin, and the corresponding gene were isolated in parallel through differential display-PCR, an expressed sequence tag (EST) project, and character...

A Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry Approach to Identify the Origin of the Glycan Heterogeneity of Diptericin, anO-Glycosylated Antibacterial Peptide from Insects

Archive ouverte | Uttenweiler-Joseph, Sandrine | CCSD

International audience. In a previous study, electrospray ionization mass spectrometry was used to analyze the structure of theO-glycopeptide diptericin, an antibacterial peptide from the fleshflyPhormia terranovae....

Chargement des enrichissements...