Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes

Lakshmi, M. Vijaya; Schulze, Irene T.

doi:10.1016/0042-6822(78)90288-x

Cited by 27 publications

(12 citation statements)

References 23 publications

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“…In addition, the lack of outer arm fucosylation would further promote ␣-galactosylation. The presence of terminal ␣-Gal residues on the majority of the glycans in this study explains the previous observation that HA N-glycans obtained from virus grown in MDBK cells are poor acceptors for sialyltransferase (39).…”

Section: Discussionsupporting

confidence: 70%

The Glycosylation of the Influenza A Virus Hemagglutinin by Mammalian Cells

Mir-Shekari

Ashford

Harvey

et al. 1997

Journal of Biological Chemistry

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We have characterized the glycans at individual sites on the hemagglutinin of three influenza A variants to obtain information on the role of cell-specific glycosylation in determining the receptor binding properties of this virus. The variants differ in whether they have a glycosylation site at residue 129 on the tip of the hemagglutinin and whether amino acid 184 (near to the receptor binding site) is His or Asn. We found that all sites on each variant are glycosylated in Madin-Darby bovine kidney cells, that the glycosylation is site-specific, and that the glycans at the same site in each variant are highly similar. One site that is buried in the hemagglutinin trimer contains only oligomannose glycans. The remaining sites carry complex glycans of increasing size as the distance of the site from the viral membrane decreases. Most of these complex glycans are terminated with ␣-galactose residues, a consequence in bovine cells of the removal of terminal sialic acids by the viral neuraminidase. Although the glycans at residue 129 are among the smallest on the molecule, they are large enough to reach the receptor binding pocket on their own and adjacent monomers. The results suggest that the reduction in receptor binding observed with MadinDarby bovine kidney cell-grown virus is due to the combined effect of large complex glycans at the tip of the hemagglutinin and a His to Asn substitution close to the receptor binding pocket.

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Section: Discussionsupporting

confidence: 70%

The Glycosylation of the Influenza A Virus Hemagglutinin by Mammalian Cells

Mir-Shekari

Ashford

Harvey

et al. 1997

Journal of Biological Chemistry

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“…However, Huang et al (1980) argue that NA is needed to expose a second binding site on the NH 2 terminus of HA2 which is the part of the HA protein inserted into the virus envelope. The conclusion that HA is the binding protein is probably correct, although inhibition of haemagglutination does not necessarily show that virus fails to bind to an erythrocyte, merely that it can no longer cross-link them to cause agglutination (Lakshmi & Schultze, 1978). However, neutralized virus attached to chick embryo cells to the same extent as non-neutralized virus (Possee & Dimmock, 1981) recalling Mandel's (1967) data on poliovirus.…”

Section: Virus Surface Components Which Bind To Cell Receptorsmentioning

confidence: 86%

“…Enzymically desialylated SFV also retained full infectivity (Kennedy, 1974). The converse experiment, increasing sialylation of the surface glycoproteins of influenza virus which are normally devoid of NeuAc, did not affect the binding of virus to erythrocytes or MDBK cells but increased infectivity by up to 10-fold (Lakshmi & Schultze, 1978). There is no obvious explanation particularly since addition of NeuAc would be expected to increase repulsion between virus and the cell.…”

Section: Virus Surface Components Which Bind To Cell Receptorsmentioning

confidence: 88%

Initial Stages in Infection with Animal Viruses

Dimmock

1982

Journal of General Virology

171

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“…Observations made with other viruses relate to this. Addition of sialic acid to the haemagglutinin protein of influenza virus destroyed HA activity but not the capacity to attach to cells or infectivity (Lakshmi & Schulze, 1978). Proteolytic removal of the glycoproteins of lymphocytic choriomeningitis virus did not decrease infectivity (Bruns & Lehmann-Grube, 1984).…”

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confidence: 99%

Coronavirus IBV: Removal of Spike Glycopolypeptide S1 by Urea Abolishes Infectivity and Haemagglutination but Not Attachment to Cells

Cavanagh¹,

Davis²

1986

Journal of General Virology

162

130

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SUMMARYUrea has been used to remove the S1 spike glycopolypeptide from avian infectious bronchitis virus (IBV) strains M41 and Beaudette, without removing the $2 spikeanchoring glycopolypeptide. Reduction of the pH to 2-9 did not cause release of S 1 although some S 1 was released spontaneously from IBV Beaudette at pH 7.4. Virus that lacked S1 was no longer infectious or able to cause haemagglutination (HA). However, radiolabelled IBV that lacked S 1 attached to erythrocytes and chick kidney cells to the same or similar extent as did intact virus. Treatment of IBV with a phospholipase C preparation, required to make IBV cause HA, did not increase binding of IBV to erythrocytes. The results indicate that while the attachment to cells of virus that lacks S1 is qualitatively different from that of intact virus, the decline in infectivity is the consequence of the loss of some other spike function.

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Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes

Cited by 27 publications

References 23 publications

The Glycosylation of the Influenza A Virus Hemagglutinin by Mammalian Cells

The Glycosylation of the Influenza A Virus Hemagglutinin by Mammalian Cells

Initial Stages in Infection with Animal Viruses

Coronavirus IBV: Removal of Spike Glycopolypeptide S1 by Urea Abolishes Infectivity and Haemagglutination but Not Attachment to Cells

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