Full Sequence and Characterization of Two Insect Defensins: Immune Peptides from the Mosquito Aedes aegypti

We report the complete amino acid sequence and biological activity of two immune peptides, from the yellow fever mosquito Aedes aegypti, that are induced in response to infection. Both peptides display biological activity against the Gram positive microbe Micrococcus luteus and substantial sequence...

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Published inProceedings of the Royal Society. B, Biological sciences Vol. 261; no. 1361; pp. 217 - 221
Main Authors Chalk, Rod, Albuquerque, Cleide M. R., Ham, Peter J., Townson, Harold
Format Journal Article
LanguageEnglish
Published London The Royal Society 22.08.1995
Subjects
Aedes - genetics
Aedes - immunology
Amino Acid Sequence
Animals
Anti-Infective Agents - chemistry
Anti-Infective Agents - immunology
Antibacterials
Defensins
Diptera - genetics
Diptera - immunology
Electrophoresis
Female
Gels
Hemolymph
Insect biochemistry
Insect biology
Insect Hormones - chemistry
Insect Hormones - genetics
Insect Hormones - immunology
Insect vectors
Molecular Sequence Data
Molecular Weight
Molecules
Mosquitos
Peptides - chemistry
Peptides - genetics
Peptides - immunology
Protein isoforms
Sequence Homology, Amino Acid
Species Specificity
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Abstract We report the complete amino acid sequence and biological activity of two immune peptides, from the yellow fever mosquito Aedes aegypti, that are induced in response to infection. Both peptides display biological activity against the Gram positive microbe Micrococcus luteus and substantial sequence homology to insect defensins, small heat-stable, antibiotic peptides previously described from several non-vector insects. These mosquito peptides, designated Ae. aegypti defensins A and B, are isoforms. Defensin B is the most abundant antibacterial peptide in this species whereas defensin A is much less abundant and carries two amino acid substitutions compared to defensin B, making it more basic in character. Apparent convergence between isoforms from Ae. aegypti and the fleshfly Phormia terranovae is discussed. The synergistic activity previously described between Ae. aegypti immune haemolymph and lysozyme is not caused by these peptides because synergy occurred only at concentrations far outside the physiological range seen in Ae. aegypti.
AbstractList We report the complete amino acid sequence and biological activity of two immune peptides, from the yellow fever mosquito Aedes aegypti, that are induced in response to infection. Both peptides display biological activity against the Gram positive microbe Micrococcus luteus and substantial sequence homology to insect defensins, small heat-stable, antibiotic peptides previously described from several non-vector insects. These mosquito peptides, designated Ae. aegypti defensins A and B, are isoforms. Defensin B is the most abundant antibacterial peptide in this species whereas defensin A is much less abundant and carries two amino acid substitutions compared to defensin B, making it more basic in character. Apparent convergence between isoforms from Ae. aegypti and the fleshfly Phormia terranovae is discussed. The synergistic activity previously described between Ae. aegypti immune haemolymph and lysozyme is not caused by these peptides because synergy occurred only at concentrations far outside the physiological range seen in Ae. aegypti.
We report the complete amino acid sequence and biological activity of two immune peptides, from the yellow fever mosquito Aedes aegypti, that are induced in response to infection. Both peptides display biological activity against the Gram positive microbe Micrococcus luteus and substantial sequence homology to insect defensins, small heat-stable, antibiotic peptides previously described from several non-vector insects. These mosquito peptides, designated Ae. aegypti defensins A and B, are isoforms. Defensin B is the most abundant antibacterial peptide in this species whereas defensin A is much less abundant and carries two amino acid substitutions compared to defensin B, making it more basic in character. Apparent convergence between isoforms from Ae. aegypti and the fleshfly Phormia terranovae is discussed. The synergistic activity previously described between Ae. aegypti immune haemolymph and lysozyme is not caused by these peptides because synergy occurred only at concentrations far outside the physiological range seen in Ae. aegypti.
Author Ham, Peter J.
Chalk, Rod
Albuquerque, Cleide M. R.
Townson, Harold
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Snippet We report the complete amino acid sequence and biological activity of two immune peptides, from the yellow fever mosquito Aedes aegypti, that are induced in...
We report the complete amino acid sequence and biological activity of two immune peptides, from the yellow fever mosquito Aedes aegypti, that are induced in...
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SubjectTerms Aedes - genetics
Aedes - immunology
Amino Acid Sequence
Animals
Anti-Infective Agents - chemistry
Anti-Infective Agents - immunology
Antibacterials
Defensins
Diptera - genetics
Diptera - immunology
Electrophoresis
Female
Gels
Hemolymph
Insect biochemistry
Insect biology
Insect Hormones - chemistry
Insect Hormones - genetics
Insect Hormones - immunology
Insect vectors
Molecular Sequence Data
Molecular Weight
Molecules
Mosquitos
Peptides - chemistry
Peptides - genetics
Peptides - immunology
Protein isoforms
Sequence Homology, Amino Acid
Species Specificity
Title Full Sequence and Characterization of Two Insect Defensins: Immune Peptides from the Mosquito Aedes aegypti
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