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Journal of Virology, October 2005, p. 12416-12424, Vol. 79, No. 19
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.19.12416-12424.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Effect of Hemagglutinin Glycosylation on Influenza Virus Susceptibility to Neuraminidase Inhibitors

Vasiliy P. Mishin,1,{dagger} Dmitri Novikov,1,{ddagger} Frederick G. Hayden,1,2 and Larisa V. Gubareva1*

Department of Internal Medicine, School of Medicine, University of Virginia, Charlottesville, Virginia,1 Department of Pathology, School of Medicine, University of Virginia, Charlottesville, Virginia2

Received 22 March 2005/ Accepted 7 July 2005

Inhibition of neuraminidase (NA) activity prevents release of progeny virions from influenza-infected cells and removal of neuraminic (sialic) acid moieties from glycans attached to hemagglutinin (HA). Neuraminic acid moieties situated near the HA receptor-binding site can reduce the efficiency of virus binding and decrease viral dependence on NA activity for replication. With the use of reverse genetics technique, we investigated the effect of glycans attached at Asn 94a, 129, and 163 on the virus susceptibility to NA inhibitors in MDCK cells and demonstrated that the glycan attached at Asn 163 plays a dominant role in compensation for the loss of NA activity.

* Corresponding author. Mailing address: 1300 Jefferson Park Ave., Jordan Hall, Room 2231, P.O. Box 800473, Charlottesville VA 22908. Phone: (434) 243-2705. Fax: (434) 982-0384. E-mail: lvg9b{at}virginia.edu.

{dagger} Present address: Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tenn.

{ddagger} Present address: University of Nizhny Novgorod, Nizhny Novgorod, Russia.

Journal of Virology, October 2005, p. 12416-12424, Vol. 79, No. 19
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.19.12416-12424.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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