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Journal of Virology, April 2000, p. 3313-3320, Vol. 74, No. 7
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Rotavirus Spike Protein VP4 Is Present at the Plasma Membrane and Is Associated with Microtubules in Infected Cells

M. Nejmeddine,1,2 G. Trugnan,2 C. Sapin,2 E. Kohli,3 L. Svensson,4 S. Lopez,5 and J. Cohen1,*

Laboratoire de Virologie et d'Immunologie Moléculaire, INRA, 78352 Jouy-en-Josas Cedex,1 INSERM U538, Faculté de Médecine Saint-Antoine, 75012 Paris,2 and Microbiologie Médicale et Moléculaire, Facultés de Médecine et Pharmacie, 21034 Dijon Cedex,3 France; Department of Virology, Swedish Institute for Infectious Disease Control, Karolinska Institute, 171 82 Solna, Sweden4; and Instituto de Biotecnologia, UNAM, Cuernavaca, Morelos 62271, Mexico5

Received 11 August 1999/Accepted 30 December 1999

VP4 is an unglycosylated protein of the outer layer of the capsid of rotavirus. It forms spikes that project from the outer layer of mature virions, which is mainly constituted by glycoprotein VP7. VP4 has been implicated in several important functions, such as cell attachment, penetration, hemagglutination, neutralization, virulence, and host range. Previous studies indicated that VP4 is located in the space between the periphery of the viroplasm and the outside of the endoplasmic reticulum in rotavirus-infected cells. Confocal microscopy of infected MA104 monolayers, immunostained with specific monoclonal antibodies, revealed that a significant fraction of VP4 was present at the plasma membrane early after infection. Another fraction of VP4 is cytoplasmic and colocalizes with beta -tubulin. Flow cytometry analysis confirmed that at the early stage of viral infection, VP4 was present on the plasma membrane and that its N-terminal region, the VP8* subunit, was accessible to antibodies. Biotin labeling of the infected cell surface monolayer with a cell-impermeable reagent allowed the identification of the noncleaved form of VP4 that was associated with the glycoprotein VP7. The localization of VP4 was not modified in cells transfected with a plasmid allowing the expression of a fusion protein consisting of VP4 and the green fluorescent protein. The present data suggest that VP4 reaches the plasma membrane through the microtubule network and that other viral proteins are dispensable for its targeting and transport.

* Corresponding author. Mailing address: Laboratoire de Virologie et d'Immunologie Moléculaire, INRA, 78352 Jouy-en-Josas Cedex, France. Phone: 33(0)1 3465 2604. Fax: 33(0)1 3465 2621. E-mail: cohen{at}biotec.jouy.inra.fr.

Journal of Virology, April 2000, p. 3313-3320, Vol. 74, No. 7
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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