Receptor affinity mutants of influenza a virus

Schulze, Irene T.; Stewart, Renee; Rajakumar, Augustine; Aytay, S.

doi:10.1016/0168-1702(88)90209-2

Cited by 1 publication

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“…It may, however, be that electrostatic effects arise from interactions between His 183 and His 184 in the HA. This type of interaction has been demonstrated for RNase A, where proton exchange between two adjacent His residues in the active site (His 12 and His…”

Section: Discussionmentioning

confidence: 99%

“…The three plaque-type variants of A/WSN/33 (H1N1) used in this study have been previously described (1,3,10), and the predicted amino acid sequences of their HA1 subunits have been published (2,12). Virus stocks were maintained in CEFs in which the sequence of the HA at the critical sites was known to remain unchanged.…”

Section: Methodsmentioning

confidence: 99%

“…The remaining variant, Co, also grows well in MDBK cells despite having a glycosylation site at residue 129. This variant has His at residue 184 instead of Asn (11,12), as do most of the HAs sequenced to date. Thus, the low receptor binding of the Fo variant appeared to be due to either the combined effects of MDBK cell glycosylation and an amino acid substitution at 184 or to the glycans on Fo being different from those on Co.…”

Section: The Influenza Virus Hemagglutinin (Ha)mentioning

confidence: 99%

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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: Discussionmentioning

confidence: 99%