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Journal of Virology, December 2002, p. 12405-12413, Vol. 76, No. 24
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.24.12405-12413.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Tight Binding of Influenza Virus Hemagglutinin to Its Receptor Interferes with Fusion Pore Dilation

Masanobu Ohuchi,1* Reiko Ohuchi,1 Tatsuya Sakai,1 and Akira Matsumoto2

Department of Microbiology, Kawasaki Medical School, Kurashiki 701-0192,1 Department of Urology, School of Medicine, Okayama University, Okayama 700-8558, Japan2

Received 6 May 2002/ Accepted 4 September 2002

Deletion of oligosaccharide side chains near the receptor binding site of influenza virus A/USSR/90/77 (H1N1) hemagglutinin (HA) enhanced the binding of HA to erythrocyte receptors, as was also observed with A/FPV/Rostock/34 (H7N1). Correlated with the enhancement of binding activity, the cell fusion activity of HA was reduced. A mutant HA in which three oligosaccharide side chains were deleted showed the highest level of binding and the lowest level of fusion among the HAs tested. The cell fusion activity of the oligosaccharide deletion mutant of HA, however, was drastically elevated when the binding activity was reduced by deletion of four amino acids adjacent to the receptor binding site. Thus, a reciprocal relationship was observed between the receptor binding and the cell fusion activities of H1/USSR HA. No difference was observed, however, in lipid mixing activity, so-called hemifusion, between wild-type (WT) and oligosaccharide deletion mutant HAs. Soluble dye transfer testing showed that even the HA with the lowest cell fusion activity was able to form fusion pores through which a small molecule such as calcein could pass. However, electron microscopic studies revealed that a large molecule such as hemoglobin hardly passed through the fusion pores formed by the mutant HA, whereas hemoglobin did efficiently pass through those formed by the WT HA. These results suggested that interference in the process of dilation of fusion pores occurs when the binding of HA to the receptor is too tight. Since the viral nucleocapsid is far larger than hemoglobin, appropriate receptor binding affinity is important for virus entry.

* Corresponding author. Mailing address: Department of Microbiology, Kawasaki Medical School, 577 Matsushima, Kurashiki 701-0192, Japan. Phone: 81-86-462-1111. Fax: 81-86-462-1199. E-mail: mohuchi{at}med.kawasaki-m.ac.jp.

Journal of Virology, December 2002, p. 12405-12413, Vol. 76, No. 24
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.24.12405-12413.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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