Glycans as receptors for influenza pathogenesis
| Autor: | Rahul Raman, Aarthi Chandrasekaran, Viswanathan Sasisekharan, Ram Sasisekharan, Karthik Viswanathan, Aravind Srinivasan |
|---|---|
| Přispěvatelé: | Harvard University--MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. School of Engineering, Viswanathan, Karthik, Chandrasekaran, Aarthi, Srinivasan, Aravind, Raman, Rahul, Sasisekharan, Ram, Sasisekharan, V. |
| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Glycan
Mini Review Orthomyxoviridae Hemagglutinin (influenza) Hemagglutinin Glycoproteins Influenza Virus Biology Biochemistry Pathogenesis 03 medical and health sciences chemistry.chemical_compound Polysaccharides Influenza Human Animals Humans Hemagglutinin Receptor Pandemics Molecular Biology Binding selectivity 030304 developmental biology chemistry.chemical_classification Sialylated glyans 0303 health sciences 030302 biochemistry & molecular biology Cell Biology biology.organism_classification Virology Glycan binding preference 3. Good health Sialic acid carbohydrates (lipids) chemistry biology.protein Multivalency Receptors Virus Glycoprotein |
| Zdroj: | PMC Glycoconjugate Journal |
| Popis: | Influenza A viruses, members of the Orthomyxoviridae family, are responsible for annual seasonal influenza epidemics and occasional global pandemics. The binding of viral coat glycoprotein hemagglutinin (HA) to sialylated glycan receptors on host epithelial cells is the critical initial step in the infection and transmission of these viruses. Scientists believe that a switch in the binding specificity of HA from Neu5Acα2-3Gal linked (α2-3) to Neu5Acα2-6Gal linked (α2-6) glycans is essential for the crossover of the viruses from avian to human hosts. However, studies have shown that the classification of glycan binding preference of HA based on sialic acid linkage alone is insufficient to establish a correlation between receptor specificity of HA and the efficient transmission of influenza A viruses. A recent study reported extensive diversity in the structure and composition of α2-6 glycans (which goes beyond the sialic acid linkage) in human upper respiratory epithelia and identified different glycan structural topologies. Biochemical examination of the multivalent HA binding to these diverse sialylated glycan structures also demonstrated that high affinity binding of HA to α2-6 glycans with a characteristic umbrella-like structural topology is critical for efficient human adaptation and human-human transmission of influenza A viruses. This review summarizes studies which suggest a new paradigm for understanding the role of the structure of sialylated glycan receptors in influenza virus pathogenesis. National Institute of General Medical Sciences (U.S.) (Glue Grant U54 GM62116) National Institutes of Health (U.S.) (Grant GM57073) Singapore-MIT Alliance for Research and Technology |
| Databáze: | OpenAIRE |
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