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. 1987 May;6(5):1459–1465. doi: 10.1002/j.1460-2075.1987.tb02387.x

The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies.

P S Daniels, S Jeffries, P Yates, G C Schild, G N Rogers, J C Paulson, S A Wharton, A R Douglas, J J Skehel, D C Wiley
PMCID: PMC553952  PMID: 3608984

Abstract

A monoclonal antibody raised against X-31 influenza virus reacted with the majority of natural H3N2 viruses isolated between 1968 and 1982. A number of variants of X-31 and of a receptor-binding mutant of X-31 were selected by the antibody during virus replication in eggs and MDCK cells. Antibody-binding assays indicated that the viruses selected were not antigenic variants and analyses using derivatized erythrocytes showed that their receptor-binding properties differed from those of the parent viruses. The amino acid substitutions in the variants were all located in the vicinity of the receptor-binding site and the structural consequences are discussed in relation to the three-dimensional structure of X-31 HA. In addition all of the variants fused membranes at higher pH than wild-type virus indicating that structural modifications in the distal globular region of HA influence the low pH-induced conformational change required for membrane fusion.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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