Studies on the role of glycosylation in the functions and antigenic properties of influenza virus glycoproteins

Basak, Sukla; Compans, Richard W.

doi:10.1016/0042-6822(83)90320-3

Cited by 28 publications

(18 citation statements)

References 45 publications

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“…The proper glycosylation or the resulting proper configuration of the molecule appeared to be essential for functional activity, as evidenced by the aberrant virus formed in the presence of tunicamycin. While unglycosylated HA and NA synthesized in the presence of tunicamycin were expressed at the cell surface and even incorporated into virions, released virions had markedly reduced HA and NA activities (Basak & Compans, 1983). Since in the above study totally unglycosylated HA reached the cell surface, the lack of proper glycosylation per se does not seem to be responsible for the accumulation of HA polypeptide of the group VI mutants in the Golgi area, but the failure of migration is the likely cause of impaired glycosylation.…”

Section: Heat Stability O F H a Activitymentioning

confidence: 82%

Physiological Characterization of Influenza Virus Temperature-sensitive Mutants Defective in the Haemagglutinin Gene

Ueda

Sugiura

1984

Journal of General Virology

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SUMMARYWe have characterized the physiological defect in two temperature-sensitive mutants of the WSN strain of influenza virus which possessed a lesion in the haemagglutinin (HA) gene. In mutant virus-infected cells at the non-permissive temperature, the precursor HA polypeptide containing predominantly mannose-rich carbohydrate chains was not converted to the mature, functional HA polypeptide. Immunofluorescence showed that the HA polypeptide did not appear on the cell surface but was confined largely to the Golgi apparatus. It was concluded that the major physiological defect of these mutants was a block in the transport of the HA polypeptide beyond the Golgi apparatus. The block could be reversed, however, by lowering the temperature to 34 °C, resulting in normal processing of the precursor polypeptide and emergence of infectious progeny virus within 30 min. The HA activity of the two mutants, but not wild-type virus, was rapidly inactivated at 51 °C. Most, but not all, revertants derived from these mutants had HA with the heat stability of wildtype virus, suggesting that the temperature sensitivity and the heat lability of HA were two pleiotropic manifestations of a single lesion in the HA gene.

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Section: Heat Stability O F H a Activitymentioning

confidence: 82%

Physiological Characterization of Influenza Virus Temperature-sensitive Mutants Defective in the Haemagglutinin Gene

Ueda

Sugiura

1984

Journal of General Virology

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“…Our data suggest that NetNGlyc may not be capable of predicting differences in sequon usage attributable to species or cell type origin. As seen in Figure 6, the Asn 302 in peptide 6 is in the stem region of HA, which is another area known to be antigenic 11, 59, 60 . As for glycopeptides containing sequon 5, differences in glycosylation of sequon/peptide 6 are likely to impact vaccine performance by altering antigenicity.…”

Section: Discussionmentioning

confidence: 99%

Comparative Glycomics Analysis of Influenza Hemagglutinin (H5N1) Produced in Vaccine Relevant Cell Platforms

Rininger²,

Jarvis

et al. 2013

J. Proteome Res.

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Hemagglutinin (HA) is the major antigen in influenza vaccines and glycosylation is known to influence its antigenicity. Embryonated hen eggs are traditionally used for influenza vaccine production, but vaccines produced in mammalian and insect cells were recently licensed. This raises the concern that vaccines produced with different cell systems might not be equivalent due to differences in their glycosylation patterns. Thus, we developed an analytical method to monitor vaccine glycosylation through a combination of nanoLC/MSE and quantitative MALDI-TOF MS permethylation profiling. We then used this method to examine glycosylation of HA’s from two different influenza H5N1 strains produced in five different platforms, including hen eggs, three different insect cell lines (High Five™, expresSF+® and glycoengineered expresSF+), and a human cell line (HEK293). Our results demonstrated that (1) sequon utilization is not necessarily equivalent in different cell types, (2) there are quantitative and qualitative differences in the overall N-glycosylation patterns and structures produced by different cell types, (3) ~20% of the N-glycans on the HAs produced by High Five™ cells are core α1,3-fucosylated structures, which may be allergenic in humans, and (4) our method can be used to monitor differences in glycosylation during the cellular glycoengineering stages of vaccine development.

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“…However occasionally, viral glycoproteins were located inside the virion (18,27,4,7). As far as we know, this internal localization of the glycoproteins inside the virion could have some significance especially at some intermediary steps of the viral cycle (1).…”

Section: Diseussionmentioning

confidence: 99%

Identification of the glycoproteins of Lymphocystis Disease Virus (LDV) of fish

Robin

LaPerriere²,

Berthiaume

1986

Archives of Virology

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Analysis of highly purified fish Lymphocystis Disease Virus (LDV), strain Leetown NFH, by three different methods, namely periodic Acid Schiff reaction, radiolabelling with tritiated fucose and N-acetyl-D-glucosamine and staining with three lectins, indicated that ten glycoproteins were associated with the virus structure. Six of them were detected by all of the three methods, three by both radiolabelling and lectin staining but only one by the lectin technique. Localization of these glycoproteins at the surface or inside the virion is discussed.

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Studies on the role of glycosylation in the functions and antigenic properties of influenza virus glycoproteins

Cited by 28 publications

References 45 publications

Physiological Characterization of Influenza Virus Temperature-sensitive Mutants Defective in the Haemagglutinin Gene

Physiological Characterization of Influenza Virus Temperature-sensitive Mutants Defective in the Haemagglutinin Gene

Comparative Glycomics Analysis of Influenza Hemagglutinin (H5N1) Produced in Vaccine Relevant Cell Platforms

Identification of the glycoproteins of Lymphocystis Disease Virus (LDV) of fish

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