tetano
Editor, Senior Moderator
Cancer Biomark. 2014 Jan 1;14(1):43-53. doi: 10.3233/CBM-130376.
Glycan array analysis of influenza H1N1 binding and release.
Gulati S1, Lasanajak Y2, Smith DF2, Cummings RD2, Air GM1.
Author information
Abstract
Influenza viruses initiate infection by attaching to sialic acid receptors on the surface of host cells. It has been recognized for some time that avian influenza viruses usually bind to terminal sialic acid that is linked in the α2-3 configuration to the next sugar while human viruses show preference for α2-6 linked sialic acid. With developments in synthetic chemistry and chemo-enzymatic methods of synthesizing quite complex glycans, it has become clear that the binding specificity extends beyond the sialic acid, and this has led to considerable interest in developing glycan reagents that could be used either as a diagnostic tool for particular influenza viruses, or to identify cells that are susceptible to infection by certain influenza viruses. Here we describe the use of the Consortium for Functional Glycomics Glycan Array to investigate binding specificity of influenza hemagglutinin and cleavage by neuraminidase, using seasonal and pandemic H1N1 influenza viruses as examples, and compare the results with published data using other array methods.
KEYWORDS:
Consortium for Functional Glycomics, Glycan array, Influenza virus, hemagglutinin, neuraminidase
PMID:
24643041
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24643041
Glycan array analysis of influenza H1N1 binding and release.
Gulati S1, Lasanajak Y2, Smith DF2, Cummings RD2, Air GM1.
Author information
Abstract
Influenza viruses initiate infection by attaching to sialic acid receptors on the surface of host cells. It has been recognized for some time that avian influenza viruses usually bind to terminal sialic acid that is linked in the α2-3 configuration to the next sugar while human viruses show preference for α2-6 linked sialic acid. With developments in synthetic chemistry and chemo-enzymatic methods of synthesizing quite complex glycans, it has become clear that the binding specificity extends beyond the sialic acid, and this has led to considerable interest in developing glycan reagents that could be used either as a diagnostic tool for particular influenza viruses, or to identify cells that are susceptible to infection by certain influenza viruses. Here we describe the use of the Consortium for Functional Glycomics Glycan Array to investigate binding specificity of influenza hemagglutinin and cleavage by neuraminidase, using seasonal and pandemic H1N1 influenza viruses as examples, and compare the results with published data using other array methods.
KEYWORDS:
Consortium for Functional Glycomics, Glycan array, Influenza virus, hemagglutinin, neuraminidase
PMID:
24643041
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24643041