Probing the receptor interactions of an H5 avian influenza virus using a baculovirus expression system and functionalised poly(acrylic acid) ligands.
Influenza viruses attach to host cells by binding to terminal sialic acid (Neu5Ac) on glycoproteins or glycolipids. Both the linkage of Neu5Ac and the identity of other carbohydrates within the oligosaccharide are thought to play roles in restricting the host range of the virus. In this study, the receptor specificity of an H5 avian influenza virus haemagglutinin protein that has recently infected man (influenza strain A/Vietnam/1194/04) has been probed using carbohydrate functionalised poly(acrylic acid) polymers. A baculovirus expression system that allows facile and safe analysis of the Neu5Ac binding specificity of mutants of H5 HA engineered at sites that are predicted to effect a switch in host range has also been developed.
Barclay
Wendy S
WS
School of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AJ, UK.
Jones
Ian M
IM
Osborn
Helen M I
HM
Phillipson
Louisa
L
Ren
Junyuan
J
Talevera
Guadalupe A
GA
Thompson
Catherine I
CI
D000180:Acrylic Resins / Q000737:chemistry / Q000378:metabolism*; D016367:Baculoviridae / Q000235:genetics*; D002240:Carbohydrate Sequence; D002850:Chromatography, Gel; D006031:Glycosylation; D009980:Influenza A virus / Q000235:genetics / Q000378:metabolism*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D015335:Molecular Probes; D008969:Molecular Sequence Data; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*
D000180:Acrylic Resins; D008024:Ligands; D015335:Molecular Probes; D011991:Receptors, Virus; C006903:carbopol 940