کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5675159 1594215 2017 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins
موضوعات مرتبط
علوم زیستی و بیوفناوری ایمنی شناسی و میکروب شناسی ویروس شناسی
پیش نمایش صفحه اول مقاله
Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins
چکیده انگلیسی


- ~50 different N-glycans are present in GP1,2 from five pathogenic ebolaviruses.
- N-glycan patterns are similar between GP1,2 from five different ebolaviruses.
- O-glycan patterns are remarkably different on GP1,2 from these ebolaviruses.
- There is substantial variation in O-glycans between Yambuku and Makona GP1,2.

Ebolaviruses are emerging pathogens that cause severe and often fatal viral hemorrhagic fevers. Four distinct ebolaviruses are known to cause Ebola virus disease in humans. The ebolavirus envelope glycoprotein (GP1,2) is heavily glycosylated, but the precise glycosylation patterns of ebolaviruses are largely unknown. Here we demonstrate that approximately 50 different N-glycan structures are present in GP1,2 derived from the four pathogenic ebolaviruses, including high mannose, hybrid, and bi-, tri-, and tetra-antennary complex glycans with and without fucose and sialic acid. The overall N-glycan composition is similar between the different ebolavirus GP1,2s. In contrast, the amount and type of O-glycan structures varies widely between ebolavirus GP1,2s. Notably, this O-glycan dissimilarity is also present between two variants of Ebola virus, the original Yambuku variant and the Makona variant responsible for the most recent Western African epidemic. The data presented here should serve as the foundation for future ebolaviral entry and immunogenicity studies.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Virology - Volume 502, February 2017, Pages 39-47
نویسندگان
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