ArticleThe Journal of biological chemistry2011
Structure and function of a "yellow" protein from saliva of the sand fly Lutzomyia longipalpis that confers protective immunity against Leishmania major infection.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 116 citations in OpenAlex.
- Yellow protein co-opted to sustain obligate symbiosis in leaf beetles.Nature communications · 2026Article
- New insights on the Feeding Site and Salivation by Lutzomyia longipalpis (Diptera: Psychodidae) During Blood Ingestion on Host Skin.PLoS neglected tropical diseases · 2026Article
- Evaluating the effect of immunization with DNA encoding Phlebotomus sergenti apyrase protein (PsSP42) against Leishmania tropica infection in BALB/c mouse model.Parasites & vectors · 2026Article
- Development of new screening tools to evaluate dog exposure to Phlebotomus tobbi and Phlebotomus papatasi sand flies.Parasites & vectors · 2026Article
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- Human sand fly challenge elicits saliva-specific innate and TbioRxiv : the preprint server for biology · 2025Article
- Optimized genetic tools for neuroanatomical and functional mapping of the Aedes aegypti olfactory system.G3 (Bethesda, Md.) · 2025Article
- Acid phosphatase-like proteins, a biogenic amine and leukotriene-binding salivary protein family from the flea Xenopsylla cheopis.Communications biology · 2023Article
- An Overview of D7 Protein Structure and Physiological Roles in Blood-Feeding Nematocera.Biology · 2022Review
- An overview of the sand fly salivary proteins in vaccine development against leishmaniases.Iranian journal of microbiology · 2022Review
- Functional aspects of evolution in a cluster of salivary protein genes from mosquitoes.Insect biochemistry and molecular biology · 2022Article
- TheProceedings. Biological sciences · 2022Article
- Some Good and Some Bad: Sand Fly Salivary Proteins in the Control of Leishmaniasis and in Autoimmunity.Frontiers in cellular and infection microbiology · 2022Review
- From Insect Bites to a Skin Autoimmune Disease: A Conceivable Pathway to Endemic Pemphigus Foliaceus.Frontiers in immunology · 2022Review
- A sand fly salivary protein acts as a neutrophil chemoattractant.Nature communications · 2021Observational
- Bumble bee queens activate dopamine production and gene expression in nutritional signaling pathways in the brain.Scientific reports · 2021Article
- Biochemical characterization of AeD7L2 and its physiological relevance in blood feeding in the dengue mosquito vector, Aedes aegypti.The FEBS journal · 2021Article
- Identification of a primary antigenic target of epitope spreading in endemic pemphigus foliaceus.Journal of autoimmunity · 2021Article
- Engineering a vector-based pan-Leishmania vaccine for humans: proof of principle.Scientific reports · 2020Article
- RNA-sequencing of the Nyssomyia neivai sialome: a sand fly-vector from a Brazilian endemic area for tegumentary leishmaniasis and pemphigus foliaceus.Scientific reports · 2020Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.