Studies on the adaptation of influenza viruses to MDCK cells
The amino acid sequences and biological properties of the haemagglutinin of three variants of the influenza virus X‐31 (H3N2) selected for their capacity to grow in MDCK cells are reported. In two variants, amino acid substitutions at HA1 residues 8 and 144 correlated with the loss of a site for gly...
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Published in | The EMBO journal Vol. 3; no. 13; pp. 3329 - 3332 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group
20.12.1984
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Subjects | |
Online Access | Get full text |
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Summary: | The amino acid sequences and biological properties of the haemagglutinin of three variants of the influenza virus X‐31 (H3N2) selected for their capacity to grow in MDCK cells are reported. In two variants, amino acid substitutions at HA1 residues 8 and 144 correlated with the loss of a site for glycosylation and specific changes in antigenicity, respectively. In all three variants substitution of an arginine residue for histidine at HA1 position 17 was correlated with increased pH optima of haemolysis. The importance of this substitution for cleavage of the haemagglutinin precursor required to produce infectious virus is discussed in relation to the three‐dimensional structure of X‐31 haemagglutinin. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
ISSN: | 0261-4189 1460-2075 |
DOI: | 10.1002/j.1460-2075.1984.tb02299.x |