Variation in the salivary peptide, maxadilan, from species in the Lutzomyia longipalpis complex

Maxadilan is an approximately 7kDa peptide that occurs in the saliva of the sand fly Lutzomyia longipalpis. This peptide is a potent vasodilator and may also have immunomodulatory effects related to the pathogenesis of leishmanial infections. Variation in the primary DNA and inferred amino acid sequ...

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Bibliographic Details
Published in:Insect molecular biology 1999-05, Vol.8 (2), p.267-275
Main Authors: Field, L. M., James, A. A., Lanzaro, G. C., Lopes, A. H. C. S., Ribeiro, J. M. C., Shoemaker, C. B., Warburg, A., Soares, M., Titus, R. G.
Format: Article
Language:English
Subjects:
Animals
Base Sequence
DNA
Insect Proteins - chemistry
Insect Proteins - classification
Insect Proteins - genetics
Insect Proteins - pharmacology
Interleukin-6 - biosynthesis
Lutzomyia longipalpis
Macrophages, Peritoneal - drug effects
Macrophages, Peritoneal - metabolism
maxadilan
Molecular Sequence Data
population genetics
Protein Structure, Secondary
Psychodidae
Rabbits
saliva
Salivary Proteins and Peptides - chemistry
Salivary Proteins and Peptides - classification
Salivary Proteins and Peptides - genetics
Salivary Proteins and Peptides - pharmacology
vasodilator
Vasodilator Agents - chemistry
Vasodilator Agents - classification
Vasodilator Agents - pharmacology
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Summary:Maxadilan is an approximately 7kDa peptide that occurs in the saliva of the sand fly Lutzomyia longipalpis. This peptide is a potent vasodilator and may also have immunomodulatory effects related to the pathogenesis of leishmanial infections. Variation in the primary DNA and inferred amino acid sequence of maxadilan is reported. Differences were found within and among natural field populations as well as among sibling species. Extensive amino acid sequence differentiation, up to 23%, was observed among maxadilan from different populations. This is a remarkable degree of polymorphism considering the small size of this peptide. The vasodilatory activity of maxadilan was equivalent among recombinant maxadilan variants. All maxadilan variants induce interleukin‐6. Predicted secondary structure and hydrophobicity plots suggest that these characteristics are conserved among variant peptides. However, profiles based on the antigenic index do differ among peptides.
ISSN:0962-1075
1365-2583
DOI:10.1046/j.1365-2583.1999.820267.x