ArticleParasites & vectors2016
Characterization of a midgut mucin-like glycoconjugate of Lutzomyia longipalpis with a potential role in Leishmania attachment.
Article in Parasites & vectors, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Identification of transporters essential for survival of Leishmania promastigotes in the digestive tract of sand flies.PLoS pathogens · 2026Article
- Partners in time: Cospeciation and host-switching shape the evolution of Leishmania parasites.PLoS neglected tropical diseases · 2025Article
- In vitro interaction profiles and midgut glycoconjugates of Trichophoromyia spp./Leishmania (Viannia) lainsoni.Parasites & vectors · 2025Article
- Review
- Discovery of essential kinetoplastid-insect adhesion proteins and their function in Leishmania-sand fly interactions.Nature communications · 2024Article
- Interactions between Leishmania parasite and sandfly: a review.Parasitology research · 2023Review
- A sticky situation: When trypanosomatids attach to insect tissues.PLoS pathogens · 2023Review
- Article
- Sand flies: Basic information on the vectors of leishmaniasis and their interactions with Leishmania parasites.Communications biology · 2022Review
- Binding of Leishmania infantum Lipophosphoglycan to the Midgut Is Not Sufficient To Define Vector Competence inmSphere · 2020Article
- Insights into the salivary N-glycome of Lutzomyia longipalpis, vector of visceral leishmaniasis.Scientific reports · 2020Article
- Trypanosoma cruzi surface mucins are involved in the attachment to the Triatoma infestans rectal ampoule.PLoS neglected tropical diseases · 2019Article
- Article
- Refractoriness of Sergentomyia schwetzi to Leishmania spp. is mediated by the peritrophic matrix.PLoS neglected tropical diseases · 2018Article
- Lutzomyia umbratilis from an area south of the Negro River is refractory to in vitro interaction with Leishmania guyanensis.Memorias do Instituto Oswaldo Cruz · 2018Article
- Lipophosphoglycan polymorphisms do not affect Leishmania amazonensis development in the permissive vectors Lutzomyia migonei and Lutzomyia longipalpis.Parasites & vectors · 2017Article
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6 authors.
Funding
Abstract
backgroundLeishmania parasites are transmitted by phlebotomine sand flies and a crucial step in their life-cycle is the binding to the sand fly midgut. Laboratory studies on sand fly competence to Leishmania parasites suggest that the sand flies fall into two groups: several species are termed "specific/restricted" vectors that support the development of one Leishmania species only, while the others belong to so-called "permissive" vectors susceptible to a wide range of Leishmania species. In a previous study we revealed a correlation between specificity vs permissivity of the vector and glycosylation of its midgut proteins. Lutzomyia longipalpis and other four permissive species tested possessed O-linked glycoproteins whereas none were detected in three specific vectors examined.
resultsWe used a combination of biochemical, molecular and parasitological approaches to characterize biochemical and biological properties of O-linked glycoprotein of Lu. longipalpis. Lectin blotting and mass spectrometry revealed that this molecule with an apparent molecular weight about 45-50 kDa corresponds to a putative 19 kDa protein with unknown function detected in a midgut cDNA library of Lu. longipalpis. We produced a recombinant glycoprotein rLuloG with molecular weight around 45 kDa. Anti-rLuloG antibodies localize the native glycoprotein on epithelial midgut surface of Lu. longipalpis. Although we could not prove involvement of LuloG in Leishmania attachment by blocking the native protein with anti-rLuloG during sand fly infections, we demonstrated strong binding of rLuloG to whole surface of Leishmania promastigotes.
conclusionsWe characterized a novel O-glycoprotein from sand fly Lutzomyia longipalpis. It has mucin-like properties and is localized on the luminal side of the midgut epithelium. Recombinant form of the protein binds to Leishmania parasites in vitro. We propose a role of this molecule in Leishmania attachment to sand fly midgut.
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