کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1225515 1494754 2015 17 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Targeted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Targeted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects
چکیده انگلیسی


• The N- and O-glycans of mosquito larvae were analysed by off-line MALDI-TOF MS and by ESI-MS or LC–MS.
• Powerful combination of HPLC, exoglycosidase treatments and mass spectrometry for detailed structure elucidation
• Sulphated and glucuronylated N- and O-glycans are present also in Drosophila.

Mosquitoes are important vectors of parasitic and viral diseases with Anopheles gambiae transmitting malaria and Aedes aegypti spreading yellow and Dengue fevers. Using two different approaches (solid-phase extraction and reversed-phase or hydrophilic interaction HPLC fractionation followed by MALDI-TOF MS or permethylation followed by NSI-MS), we examined the N-glycans of both A. gambiae and A. aegypti larvae and demonstrate the presence of a range of paucimannosidic glycans as well as bi- and tri-antennary glycans, some of which are modified with fucose or with sulphate or glucuronic acid residues; the latter anionic modifications were also found on N-glycans of larvae from another dipteran species (Drosophila melanogaster). The sulphate groups are attached primarily to core α-mannose residues (especially the α1,6-linked mannose), whereas the glucuronic acid residues are linked to non-reducing β1,3-galactose. Also, O-glycans were found to possess glucuronic acid and sulphate as well as phosphoethanolamine modifications. The presence of sulphated and glucuronylated N-glycans is a novel feature in dipteran glycomes; these structures have the potential to act as additional anionic glycan ligands involved in parasite interactions with the vector host.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Proteomics - Volume 126, 3 August 2015, Pages 172–188
نویسندگان
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