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Glycan structures and antiviral effect of the structural subunit RvH2 of Rapana hemocyanin
Dolashka, P.; Velkova, L.; Shishkov, S.; Kostova, K.; Dolashki, A.; Dimitrov, I.; Atanasov, B.; Devreese, B.; Voelter, W.; Van Beeumen, J. (2010). Glycan structures and antiviral effect of the structural subunit RvH2 of Rapana hemocyanin. Carbohydrate Research 345(16): 2361-2367. dx.doi.org/10.1016/j.carres.2010.08.005
In: Carbohydrate Research. Elsevier SCI Ltd: Oxford. ISSN 0008-6215, more
Peer reviewed article  

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Keywords
    Rapana venosa (Valenciennes, 1846) [WoRMS]; Marine
Author keywords
    Glycosylation; Hemocyanin; MALDI-TOF/TOF; Q-Trap; Rapana venosa; HSVvirus

Authors  Top 
  • Dolashka, P.
  • Velkova, L.
  • Shishkov, S.
  • Kostova, K.
  • Dolashki, A.
  • Dimitrov, I.
  • Atanasov, B.
  • Devreese, B.
  • Voelter, W.
  • Van Beeumen, J., more

Abstract
    Molluscan hemocyanins are very large biological macromolecules and they act as oxygen-transporting glycoproteins. Most of them are glycoproteins with molecular mass around 9000 kDa. The oligosaccharide structures of the structural subunit RvH2 of Rapana venosa hemocyanin (RvH) were studied by sequence analysis of glycans using MALDI-TOF-MS and tandem mass spectrometry on a Q-Trap mass spectrometer after enzymatical liberation of the N-glycans from the polypeptides. Our study revealed a highly heterogeneous mixture of glycans of the compositions Hex0–9 HexNAc2–4 Hex0–3 Pent0–3 Fuc0–3. A novel type of N-glycan, with an internal fucose residue connecting one GalNAc(β1-2) and one hexuronic acid, was detected, as also occurs in subunit RvH1. A glycan with the same structure but with two deoxyhexose residues was observed as a doubly charged ion. Antiviral effects of the native molecules of RvH and also of Helix lucorum hemocyanin (HlH), of their structural subunits, and of the glycosylated functional unit RvH2-e and the non-glycosylated unit RvH2-c on HSV virus type 1 were investigated. Only glycosylated FU RvH2-e exhibits this antiviral activity. The carbohydrate chains of the FU are likely to interact with specific regions of glycoproteins of HSV, through van der Waals interactions in general or with certain amino acid residues in particular. Several clusters of these residues can be identified on the surface of RvH2-e.

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