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Journal of Virology, July 2003, p. 7510-7516, Vol. 77, No. 13
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.13.7510-7516.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

N-Linked Glycosylation Is Required for XC Cell-Specific Syncytium Formation by the R Peptide-Containing Envelope Protein of Ecotropic Murine Leukemia Viruses

Yoshinao Kubo,1,2* Akinori Ishimoto,3 and Hiroshi Amanuma1

Molecular Cell Science Laboratory, RIKEN, Wako, Saitama 351-0198,1 Department of Preventive Medicine and AIDS Research, Institute of Tropical Medicine, Nagasaki University, Sakamoto, Nagasaki 852-8523,2 Laboratory of Gene Analysis, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606, Japan3

Received 10 February 2003/ Accepted 18 March 2003

The XC cell line undergoes extensive syncytium formation after infection with ecotropic murine leukemia viruses (MLVs) and is frequently used to titrate these viruses. This cell line is unique in its response to the ecotropic MLV envelope protein (Env) in that it undergoes syncytium formation with cells expressing Env protein containing R peptide (R+ Env), which is known to suppress the fusogenic potential of the Env protein in other susceptible cells. To analyze the ecotropic receptor, CAT1, in XC cells, a mouse CAT1 tagged with the influenza virus hemagglutinin epitope (mCAT1-HA)-expressing retroviral vector was inoculated into XC and NIH 3T3 cells. The molecular size of the mCAT1-HA protein expressed in XC cells was smaller than that in NIH 3T3 cells due to altered N glycosylation in XC cells. Treatment of XC cells with tunicamycin significantly suppressed the formation of XC cell syncytia induced by the R+ Env protein but not that induced by the R- Env protein. This result indicates that N glycosylation is required for XC cell-specific syncytium formation by the R+ Env protein. The R+ Env protein induced syncytia in XC cells expressing a mutant mCAT1 lacking both of two N glycosylation sites, and tunicamycin treatment suppressed syncytium formation by R+ Env in those cells. This suggests that N glycosylation of a molecule(s) other than the receptor is required for the induction of XC cell syncytia by the R+ Env protein.

* Corresponding author. Mailing address: Department of Preventive Medicine and AIDS Research, Institute of Tropical Medicine, Nagasaki University, 1-12-4 Sakamoto, Nagasaki 852-8523, Japan. Phone: 81-95-849-7846. Fax: 81-95-849-7805. E-mail: yoshinao{at}net.nagasaki-u.ac.jp.

Journal of Virology, July 2003, p. 7510-7516, Vol. 77, No. 13
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.13.7510-7516.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kubo, Y., Yokoyama, M., Yoshii, H., Mitani, C., Tominaga, C., Tanaka, Y., Sato, H., Yamamoto, N. (2007). Inhibitory role of CXCR4 glycan in CD4-independent X4-tropic human immunodeficiency virus type 1 infection and its abrogation in CD4-dependent infection. J. Gen. Virol. 88: 3139-3144 [Abstract] [Full Text]  


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