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Background  Mosquito midgut glycoproteins may act as key recognition sites for the invading malarial ookinete. Effective transmission blocking strategies require the identification of novel target molecules. We have partially characterised the surface glycoproteins of two cell lines from two mosquito species;  Anopheles stephensi  and  Anopheles gambiae , and investigated the binding of  Plasmodium berghei  ookinetes to carbohydrate ligands on the cells. Cell line extracts were run on SDS-PAGE gels and carbohydrate moieties determined by blotting against a range of biotinylated lectins. In addition, specific glycosidases were used to cleave the oligosaccharides.    Results   An. stephensi  43 and  An. gambiae  55 cell line glycoproteins expressed oligosaccharides containing oligomannose and hybrid oligosaccharides, with and without α1-6 core fucosylation; N-linked oligosaccharides with terminal Galβ1-3GalNAc or GalNAcβ1-3Gal;  O -linked α/βGalNAc.  An. stephensi  43 cell line glycoproteins also expressed  N -linked Galβ1-4R and  O -linked Galβ1-3GalNAc. Although  P. berghei  ookinetes bound to both mosquito cell lines, binding could not be inhibited by GlcNAc, GalNAc or Galactose.    Conclusions  Anopheline cell lines displayed a limited range of oligosaccharides. Differences between the glycosylation patterns of the cell lines and mosquito midgut epithelial cells could be a factor why ookinetes did not bind in a carbohydrate inhibitable manner. Anopheline cell lines are not suitable as a potential model system for carbohydrate-mediated adhesion of  Plasmodium  ookinetes.

Mosquito cell line glycoproteins: an unsuitable model system for the Plasmodium ookinete-mosquito midgut interaction?