tetano
Editor, Senior Moderator
Virus Res. 2013 Sep 10. pii: S0168-1702(13)00286-4. doi: 10.1016/j.virusres.2013.08.007. [Epub ahead of print]
Recognition of Sulphated and Fucosylated Receptor Sialosides by A/Vietnam/1194/2004 (H5N1) Influenza Virus.
Xiong X, Tuzikov A, Coombs P, Martin S, Walker PA, Gamblin SJ, Bovin N, Skehel JJ.
Source
National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.
Abstract
Like most avian influenza viruses, H5 viruses preferentially, bind to sialic acid in α2-3-linkage to galactose, the second saccharide, of carbohydrate side-chains (Ha et al., 2001; Matrosovich et al., 1999). H5 viruses isolated from different, avian species also show preferences for different linkages of galactose, to N-acetyl glucosamine, the third saccharide; wild duck viruses prefer, Galβ1-3GlcNAc, and domesticated poultry prefer Galβ1-4GlcNAc- linked, sialosides (Gambaryan et al., 2006, 2005, 2008, 2004). Probably as a consequence of their route of, transmission to humans, H5 viruses isolated from humans show the same, preference as poultry viruses., GlcNAc in these different linkages can also be fucosylated and/or, sulphated (Gambaryan et al., 2006, 2008, 2004) and the effects of these modifications on receptor, binding are also species specific. Since the fucosylated and sulphated, sialoside Neu5Acα2-3Galβ1-4(Fucα1-3)(6-HSO3)GlcNac (Su-SLex) is a, component of endothelial cells (Gambaryan et al., 2012), for which highly pathogenic H5, viruses have been seen to display strong cell tropism (Klenk, 2005; Ocana-Macchi et al., 2009; Zeng et al., 2012), we have, studied the nature of this analogue's interactions with a human H5 virus. For this purpose we have used X-ray crystallography to examine complexes, formed by A/Vietnam/1194/2003 (H5N1) HA with four related, Galβ1-4GlcNAclinked, sialoside receptor analogues: Neu5Acα2-3Galβ1-4GlcNAc (3'SLN), Neu5Acα2-3Galβ1-4(6-HSO3)GlcNAc (Su-3'SLN), Neu5Acα2-3Galβ1-4(Fucα1-, 3)GlcNac (SLex), and Neu5Acα2-3Galβ1-4(Fucα1-3)(6-HSO3)GlcNAc (Su-SLex)., We have also determined virus affinity for the analogues by surface, biolayer interferometry.
Copyright ? 2013. Published by Elsevier B.V.
KEYWORDS:
X-ray crystallography, acid, influenza viruses, sialic, sialosides, surface biolayer interferometry
PMID:
24036174
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24036174
Recognition of Sulphated and Fucosylated Receptor Sialosides by A/Vietnam/1194/2004 (H5N1) Influenza Virus.
Xiong X, Tuzikov A, Coombs P, Martin S, Walker PA, Gamblin SJ, Bovin N, Skehel JJ.
Source
National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.
Abstract
Like most avian influenza viruses, H5 viruses preferentially, bind to sialic acid in α2-3-linkage to galactose, the second saccharide, of carbohydrate side-chains (Ha et al., 2001; Matrosovich et al., 1999). H5 viruses isolated from different, avian species also show preferences for different linkages of galactose, to N-acetyl glucosamine, the third saccharide; wild duck viruses prefer, Galβ1-3GlcNAc, and domesticated poultry prefer Galβ1-4GlcNAc- linked, sialosides (Gambaryan et al., 2006, 2005, 2008, 2004). Probably as a consequence of their route of, transmission to humans, H5 viruses isolated from humans show the same, preference as poultry viruses., GlcNAc in these different linkages can also be fucosylated and/or, sulphated (Gambaryan et al., 2006, 2008, 2004) and the effects of these modifications on receptor, binding are also species specific. Since the fucosylated and sulphated, sialoside Neu5Acα2-3Galβ1-4(Fucα1-3)(6-HSO3)GlcNac (Su-SLex) is a, component of endothelial cells (Gambaryan et al., 2012), for which highly pathogenic H5, viruses have been seen to display strong cell tropism (Klenk, 2005; Ocana-Macchi et al., 2009; Zeng et al., 2012), we have, studied the nature of this analogue's interactions with a human H5 virus. For this purpose we have used X-ray crystallography to examine complexes, formed by A/Vietnam/1194/2003 (H5N1) HA with four related, Galβ1-4GlcNAclinked, sialoside receptor analogues: Neu5Acα2-3Galβ1-4GlcNAc (3'SLN), Neu5Acα2-3Galβ1-4(6-HSO3)GlcNAc (Su-3'SLN), Neu5Acα2-3Galβ1-4(Fucα1-, 3)GlcNac (SLex), and Neu5Acα2-3Galβ1-4(Fucα1-3)(6-HSO3)GlcNAc (Su-SLex)., We have also determined virus affinity for the analogues by surface, biolayer interferometry.
Copyright ? 2013. Published by Elsevier B.V.
KEYWORDS:
X-ray crystallography, acid, influenza viruses, sialic, sialosides, surface biolayer interferometry
PMID:
24036174
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24036174