Structure and function of a "yellow" protein from saliva of the sand fly Lutzomyia longipalpis that confers protective immunity against Leishmania major infection.

Détails

ID Serval
serval:BIB_877CF0B07E40
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Structure and function of a "yellow" protein from saliva of the sand fly Lutzomyia longipalpis that confers protective immunity against Leishmania major infection.
Périodique
Journal of Biological Chemistry
Auteur(s)
Xu X., Oliveira F., Chang B.W., Collin N., Gomes R., Teixeira C., Reynoso D., My Pham V., Elnaiem D.E., Kamhawi S., Ribeiro J.M., Valenzuela J.G., Andersen J.F.
ISSN
1083-351X (Electronic)
ISSN-L
0021-9258
Statut éditorial
Publié
Date de publication
2011
Volume
286
Numéro
37
Pages
32383-32393
Langue
anglais
Résumé
LJM11, an abundant salivary protein from the sand fly Lutzomyia longipalpis, belongs to the insect "yellow" family of proteins. In this study, we immunized mice with 17 plasmids encoding L. longiplapis salivary proteins and demonstrated that LJM11 confers protective immunity against Leishmania major infection. This protection correlates with a strong induction of a delayed type hypersensitivity (DTH) response following exposure to L. longipalpis saliva. Additionally, splenocytes of exposed mice produce IFN-γ upon stimulation with LJM11, demonstrating the systemic induction of Th1 immunity by this protein. In contrast to LJM11, LJM111, another yellow protein from L. longipalpis saliva, does not produce a DTH response in these mice, suggesting that structural or functional features specific to LJM11 are important for the induction of a robust DTH response. To examine these features, we used calorimetric analysis to probe a possible ligand binding function for the salivary yellow proteins. LJM11, LJM111, and LJM17 all acted as high affinity binders of prohemostatic and proinflammatory biogenic amines, particularly serotonin, catecholamines, and histamine. We also determined the crystal structure of LJM11, revealing a six-bladed β-propeller fold with a single ligand binding pocket located in the central part of the propeller structure on one face of the molecule. A hypothetical model of LJM11 suggests a positive electrostatic potential on the face containing entry to the ligand binding pocket, whereas LJM111 is negative to neutral over its entire surface. This may be the reason for differences in antigenicity between the two proteins.
Mots-clé
Animals, Biogenic Amines/immunology, Female, Hypersensitivity, Delayed/genetics, Hypersensitivity, Delayed/immunology, Inflammation/genetics, Inflammation/immunology, Insect Proteins/genetics, Insect Proteins/immunology, Interferon-gamma/genetics, Interferon-gamma/immunology, Leishmania major/immunology, Leishmaniasis, Cutaneous/genetics, Leishmaniasis, Cutaneous/immunology, Mice, Protein Structure, Tertiary, Psychodidae/genetics, Psychodidae/immunology, Recombinant Proteins/genetics, Recombinant Proteins/immunology, Saliva/immunology, Th1 Cells/immunology
Pubmed
Web of science
Open Access
Oui
Création de la notice
26/10/2011 13:19
Dernière modification de la notice
08/05/2019 21:29
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