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tisdag 11 november 2014

EBOV musiinin kaltainen domaani ja N- ja O-linkkiytyneitä glykaaneja.

Kuva  http://www.plospathogens.org/article/fetchObject.action?uri=info:doi/10.1371/journal.ppat.1003258.g001&representation=PNG_L

How Does Glycosylation of Ebola Virus Envelope Proteins Facilitate Immune Evasion?

In EBOV, four variants of the envelope glycoprotein are synthesized as a result of transcriptional stuttering or post-translational processing (Figure 1A).

About 25% of transcripts from the GP gene produce the virion-attached or envelope spike GP that is important for entry.

The surface of the envelope GP is covered with N- and O-linked glycans.

Depending on the EBOV species, the envelope GP contains 11–18 N-linked glycan sites.

Furthermore, EBOV GP contains an unstructured ~150-residue mucin-like domain that is heavily modified with O-linked glycans (~80 sites) [4].

 The N-linked glycans are a heterogeneous mixture of ~60 different species of high-mannose, hybrid, and complex oligosaccharides,

 while the O-linked glycans consist of primarily smaller trisaccharide structures (core 2) that contain varying amounts of sialic acids [5].

  • Kohdistan  nyt pohdinnan  MUSIININ kaltaiseen domeeniin.  Mikä merkitys sillä  virukselle on?
 The O-linked glycosylated mucin-like domain  is modeled onto EBOV GP,
 and thought to form an extended structure that provides another glycan layer of protection to the virus.

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