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Background   Leishmania  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.    Results  We 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.    Conclusions  We 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.

Characterization of a midgut mucin-like glycoconjugate of Lutzomyia longipalpis with a potential role in Leishmania attachment