Glossina Proteolytic Lectin Does Not Require a Carbohydrate Moiety for Enzymatic or Trypanosome-Transforming Activities

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dc.contributor.author Muluvi, Geoffrey M.
dc.contributor.author Amin, Daniel N.
dc.contributor.author Kamita, Shizuo G.
dc.contributor.author Machuka, Jesse
dc.contributor.author Hammock, Bruce D.
dc.contributor.author Osir, Ellie O.
dc.date.accessioned 2014-11-19T07:26:20Z
dc.date.available 2014-11-19T07:26:20Z
dc.date.issued 2006
dc.identifier.citation Journal of Medical Entomology, 43(2):301-308. 2006 en_US
dc.identifier.uri http://www.bioone.org/doi/full/10.1603/0022-2585%282006%29043%5B0301%3AGPLDNR%5D2.0.CO%3B2
dc.identifier.uri http://hdl.handle.net/123456789/45
dc.description doi: http://dx.doi.org/10.1603/0022-2585(2006)043[0301:GPLDNR]2.0.CO;2 en_US
dc.description.abstract The developmental cycle of the cyclically transmitted African trypanosome involves an obligatory passage through the tsetse fly, Glossina spp. This intricate relationship requires the presence of molecules within the insect vector, including a midgut lectin, that interact with the trypanosome. Recently, a gene encoding for a proteolytic lectin, with trypanosome-transforming activity, was isolated from a midgut cDNA library of Glossina fuscipes fuscipes Austen in our laboratory. Using the same approach, we have identified a similar gene from a midgut cDNA library of Glossina austeni (Newstead). The protein encoded by this gene was expressed in bacteria and a baculovirus-based expression system. The baculovirus-expressed lectin was found in the medium of baculovirus-infected Sf-21 cell cultures, indicating that the tsetse fly-derived signal peptide was recognized and cleaved by the Sf-21 cells. The baculovirus-expressed protein also was glycosylated despite the absence of classical O-linked and N-linked sugar attachment motifs. Both the baculovirus- and bacterium-expressed lectin proteins were shown to agglutinate trypanosomes and rabbit red blood cells in vitro. This agglutination was strongly inhibited by d-glucosamine. d-Glucosamine also inhibited the action of the authentic and recombinant lectins upon the chromogenic substrate Chromozym TRY. Interestingly, both baculovirus- and bacterium-expressed lectins showed no significant differences in terms of these activities, indicating that a sugar moiety is not essential for biological activity. Our results provide an important molecular tool for further characterization of Glossina proteolytic lectin. en_US
dc.language.iso en en_US
dc.publisher Entomological Society of America en_US
dc.subject tsetse fly en_US
dc.subject Glossina en_US
dc.subject proteolytic lectin en_US
dc.subject trypanosome en_US
dc.title Glossina Proteolytic Lectin Does Not Require a Carbohydrate Moiety for Enzymatic or Trypanosome-Transforming Activities en_US
dc.type Article en_US


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