The hemagglutinins of the human influenza viruses A and B recognize different receptor microdomains

Suzuki, Yasuo; Nagao, Yasuhiro; Kato, Hideshige; Suzuki, Takashi; Matsumoto, Makoto; Murayama, Jun-Ichiro

doi:10.1016/0005-2736(87)90048-4

Cited by 47 publications

(27 citation statements)

References 25 publications

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“…The techniques most widely used to study the interactions of the influenza virus with host cell receptors employ animal cells in various assay formats (36,57,59,64,69). To overcome the problems of cell-based techniques, new assays that rely on labeled sialyl-glycoproteins or polymeric sialoglycans have been developed (18).…”

mentioning

confidence: 99%

Receptor Specificity of Influenza A H3N2 Viruses Isolated in Mammalian Cells and Embryonated Chicken Eggs

Stevens

Chen

Carney

et al. 2010

J Virol

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Isolation of human subtype H3N2 influenza viruses in embryonated chicken eggs yields viruses with amino acid substitutions in the hemagglutinin (HA) that often affect binding to sialic acid receptors. We used a glycan array approach to analyze the repertoire of sialylated glycans recognized by viruses from the same clinical specimen isolated in eggs or cell cultures. The binding profiles of whole virions to 85 sialoglycans on the microarray allowed the categorization of cell isolates into two groups. Group 1 cell isolates displayed binding to a restricted set of ␣2-6 and ␣2-3 sialoglycans, whereas group 2 cell isolates revealed receptor specificity broader than that of their egg counterparts. Egg isolates from group 1 showed binding specificities similar to those of cell isolates, whereas group 2 egg isolates showed a significantly reduced binding to ␣2-6-and ␣2-3-type receptors but retained substantial binding to specific O-and N-linked ␣2-3 glycans, including ␣2-3GalNAc and fucosylated ␣2-3 glycans (including sialyl Lewis x), both of which may be important receptors for H3N2 virus replication in eggs. These results revealed an unexpected diversity in receptor binding specificities among recent H3N2 viruses, with distinct patterns of amino acid substitution in the HA occurring upon isolation and/or propagation in eggs. These findings also suggest that clinical specimens containing viruses with group 1-like receptor binding profiles would be less prone to undergoing receptor binding or antigenic changes upon isolation in eggs. Screening cell isolates for appropriate receptor binding properties might help focus efforts to isolate the most suitable viruses in eggs for production of antigenically well-matched influenza vaccines.

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mentioning

confidence: 99%

Receptor Specificity of Influenza A H3N2 Viruses Isolated in Mammalian Cells and Embryonated Chicken Eggs

Stevens

Chen

Carney

et al. 2010

J Virol

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“…23,24) Briefly, 25 ml of virus suspension (4 HA unit) was incubated for 1 h at 4°C with 25 ml of inhibitors serially diluted two-fold with PBS (pH 7.2, 131 mM NaCl, 14 mM Na 2 HPO 4 , 1.5 mM KH 2 PO 4 , and 2.7 mM KCl) in 96-well microtiter plates. After adding 50 ml of 0.5% (v/v) guinea pig erythrocytes to each well, the plates were kept for 8 h at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Glucosyl Hesperidin Prevents Influenza A Virus Replication <i>in Vitro</i> by Inhibition of Viral Sialidase

Saha

Takahashi

Suzuki

2009

Biological & Pharmaceutical Bulletin

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Hesperidin, a flavonoid obtained from citrus fruits, is known to have multiple biological activities and antimicrobial activities for human viruses; however, hesperidin has very low solubility in water and the target molecule of hesperidin for influenza virus remains unknown. A water-soluble derivative of hesperidin, glucosyl hesperidin (GH), which was synthesized by regioselective transglycosylation with cyclodextrin glucanotransferase, has been reported to have biological activities that are as or stronger than those of hesperidin. To determine the inhibitory effect of GH on influenza A virus (IAV) infection, Madin-Darby canine kidney (MDCK) cells were treated with GH before, at the same time as, and after IAV inoculation. GH treatment before IAV inoculation had no effect on virus replication, whereas, treatment with GH at the same time as or after IAV inoculation induced distinct reduction in IAV replication. Inhibition analysis of GH against two surface glycoprotein spikes of IAV revealed that GH prevents IAV replication by inhibition of viral sialidase activity that is involved in the entry and release stages on IAV infection but not by receptor binding inhibition. GH had no cytotoxic effects on MDCK cells in a dose range of 0-25 mM. Our results provide useful information for the development of novel sialidase inhibitors for influenza prevention.

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“…These results could be explained by the selection of an escape variant strain (M1/5HS8) containing virus subpopulations with probably different fusogenic sequences in the hemagglutinin amino acid chain (25), without affinity for N-glycolyl-containing structures present at high percentage in horse cells. Indeed, clear diversity of virus samples in terms of receptor binding activity to Nglycolyl sialic acid residues has been previously reported (21,26).…”

Section: Analysis Of Strains Of Influenza a And B Viruses For Interdementioning

confidence: 89%

“…Actually, the cleaving activity of neuraminidase on hemagglutinins already bound to cell receptors permits a 35-70 o tilt from the normal membrane (23,24), conformational changes and the insertion of their hemagglutinin fusion peptides into cell membranes (25), resulting in the final fusion process (26). The lower level of cell surface charges per horse erythrocyte when compared to human and chicken cells may be another possible explanation for these results.…”

Section: Analysis Of Strains Of Influenza a And B Viruses For Interdementioning

confidence: 99%

Analysis of viral and cellular parameters which affect the fusion process of influenza viruses

Barbosa

Luiz

Gusmão

et al. 1997

Braz J Med Biol Res

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In the present investigation we studied the fusogenic process developed by influenza A, B and C viruses on cell surfaces and different factors associated with virus and cell membrane structures. The biological activity of purified virus strains was evaluated in hemagglutination, sialidase and fusion assays. Hemolysis by influenza A, B and C viruses ranging from 77.4 to 97.2%, from 20.0 to 65.0%, from 0.2 to 93.7% and from 9.0 to 76.1% was observed when human, chicken, rabbit and monkey erythrocytes, respectively, were tested at pH 5.5. At this pH, low hemolysis indexes for influenza A, B and C viruses were observed if horse erythrocytes were used as target cells for the fusion process, which could be explained by an inefficient receptor binding activity of influenza on N-glycolyl sialic acids. Differences in hemagglutinin receptor binding activity due to its specificity to N-acetyl or N-glycolyl cell surface oligosaccharides, density of these cellular receptors and level of negative charges on the cell surface may possibly explain these results, showing influence on the sialidase activity and the fusogenic process. Comparative analysis showed a lack of dependence between the sialidase and fusion activities developed by influenza B viruses. Influenza A viruses at low sialidase titers (<2) also exhibited clearly low hemolysis at pH 5.5 (15.8%), while influenza B viruses with similarly low sialidase titers showed highly variable hemolysis indexes (0.2 to 78.0%). These results support the idea that different virus and cell-associated factors such as those presented above have a significant effect on the multifactorial fusion process.

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The hemagglutinins of the human influenza viruses A and B recognize different receptor microdomains

Cited by 47 publications

References 25 publications

Receptor Specificity of Influenza A H3N2 Viruses Isolated in Mammalian Cells and Embryonated Chicken Eggs

Receptor Specificity of Influenza A H3N2 Viruses Isolated in Mammalian Cells and Embryonated Chicken Eggs

Glucosyl Hesperidin Prevents Influenza A Virus Replication <i>in Vitro</i> by Inhibition of Viral Sialidase

Analysis of viral and cellular parameters which affect the fusion process of influenza viruses

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