J Gen Virol Faster Access
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Luo, C.
Right arrow Articles by Nakajima, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Luo, C.
Right arrow Articles by Nakajima, K.
Agricola
Right arrow Articles by Luo, C.
Right arrow Articles by Nakajima, K.
Journal of General Virology (2002), 83, 1729-1734.
© 2002 Society for General Microbiology


Animal: RNA Viruses

Analysis of the desialidation process of the haemagglutinin protein of influenza B virus: the host-dependent desialidation step

C. Luo1, E. Nobusawa1 and K. Nakajima1

Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho-chou, Mizuho-ku, Nagoya 467-8601, Japan1

Author for correspondence: Katsuhisa Nakajima. Fax +81 52 853 3638. e-mail nakajima{at}med.nagoya-cu.ac.jp

It was reported previously that haemadsorption by the haemagglutinin (HA) protein of influenza B virus required that the protein must undergo desialidation. When MDCK and COS cells were infected with influenza B/Kanagawa/73 virus in the presence of a neuraminidase (NA) inhibitor, Zanamivir, haemadsorption on MDCK cells was inhibited but that on COS cells was not. The activity of the NA protein of the two types of infected cells was similar and both were inhibited by Zanamivir in a dose-dependent manner. A comparison of the desialidation of the HA protein was made on MDCK and COS cells in the presence of bacterial NA and both cells were found to have similar sensitivity. On the accumulation of the HA and NA proteins in the trans-Golgi network of MDCK cells by means of low-temperature treatment, desialidation of the HA protein in the presence of Zanamivir was detected by two-dimensional gel electrophoresis. Because this agent was reported to be unable to penetrate cells, these data suggest that, in MDCK cells, desialidation of the HA protein occurs on the cell surface but, in COS cells, the HA and NA proteins might accumulate in the trans-Golgi network, thus allowing NA desialidation before their migration to the cell surface.




This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
M. Ujike, K. Nakajima, and E. Nobusawa
A point mutation at the C terminus of the cytoplasmic domain of influenza B virus haemagglutinin inhibits syncytium formation
J. Gen. Virol., June 1, 2006; 87(6): 1669 - 1676.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
V. P. Mishin, D. Novikov, F. G. Hayden, and L. V. Gubareva
Effect of Hemagglutinin Glycosylation on Influenza Virus Susceptibility to Neuraminidase Inhibitors
J. Virol., October 1, 2005; 79(19): 12416 - 12424.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
T. Suzuki, T. Takahashi, C.-T. Guo, K. I.-P. J. Hidari, D. Miyamoto, H. Goto, Y. Kawaoka, and Y. Suzuki
Sialidase Activity of Influenza A Virus in an Endocytic Pathway Enhances Viral Replication
J. Virol., September 15, 2005; 79(18): 11705 - 11715.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2002 by the Society for General Microbiology.