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
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nejmeddine, M.
Right arrow Articles by Cohen, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nejmeddine, M.
Right arrow Articles by Cohen, J.

 Previous Article  |  Next Article 

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.



This article has been cited by other articles:

  • Roohvand, F., Maillard, P., Lavergne, J.-P., Boulant, S., Walic, M., Andreo, U., Goueslain, L., Helle, F., Mallet, A., McLauchlan, J., Budkowska, A. (2009). Initiation of Hepatitis C Virus Infection Requires the Dynamic Microtubule Network: ROLE OF THE VIRAL NUCLEOCAPSID PROTEIN. J. Biol. Chem. 284: 13778-13791 [Abstract] [Full Text]  
  • Delmas, O., Breton, M., Sapin, C., Le Bivic, A., Colard, O., Trugnan, G. (2007). Heterogeneity of Raft-Type Membrane Microdomains Associated with VP4, the Rotavirus Spike Protein, in Caco-2 and MA 104 Cells. J. Virol. 81: 1610-1618 [Abstract] [Full Text]  
  • Broquet, A. H., Lenoir, C., Gardet, A., Sapin, C., Chwetzoff, S., Jouniaux, A.-M., Lopez, S., Trugnan, G., Bachelet, M., Thomas, G. (2007). Hsp70 Negatively Controls Rotavirus Protein Bioavailability in Caco-2 Cells Infected by the Rotavirus RF Strain. J. Virol. 81: 1297-1304 [Abstract] [Full Text]  
  • Trask, S. D., Dormitzer, P. R. (2006). Assembly of Highly Infectious Rotavirus Particles Recoated with Recombinant Outer Capsid Proteins. J. Virol. 80: 11293-11304 [Abstract] [Full Text]  
  • Corthesy, B., Benureau, Y., Perrier, C., Fourgeux, C., Parez, N., Greenberg, H., Schwartz-Cornil, I. (2006). Rotavirus Anti-VP6 Secretory Immunoglobulin A Contributes to Protection via Intracellular Neutralization but Not via Immune Exclusion. J. Virol. 80: 10692-10699 [Abstract] [Full Text]  
  • Gardet, A., Breton, M., Fontanges, P., Trugnan, G., Chwetzoff, S. (2006). Rotavirus Spike Protein VP4 Binds to and Remodels Actin Bundles of the Epithelial Brush Border into Actin Bodies.. J. Virol. 80: 3947-3956 [Abstract] [Full Text]  
  • Lopez, T., Rojas, M., Ayala-Breton, C., Lopez, S., Arias, C. F. (2005). Reduced expression of the rotavirus NSP5 gene has a pleiotropic effect on virus replication. J. Gen. Virol. 86: 1609-1617 [Abstract] [Full Text]  
  • Ruthel, G., Demmin, G. L., Kallstrom, G., Javid, M. P., Badie, S. S., Will, A. B., Nelle, T., Schokman, R., Nguyen, T. L., Carra, J. H., Bavari, S., Aman, M. J. (2005). Association of Ebola Virus Matrix Protein VP40 with Microtubules. J. Virol. 79: 4709-4719 [Abstract] [Full Text]  
  • Lopez, T., Camacho, M., Zayas, M., Najera, R., Sanchez, R., Arias, C. F., Lopez, S. (2005). Silencing the Morphogenesis of Rotavirus. J. Virol. 79: 184-192 [Abstract] [Full Text]  
  • Delmas, O., Durand-Schneider, A.-M., Cohen, J., Colard, O., Trugnan, G. (2004). Spike Protein VP4 Assembly with Maturing Rotavirus Requires a Postendoplasmic Reticulum Event in Polarized Caco-2 Cells. J. Virol. 78: 10987-10994 [Abstract] [Full Text]  
  • Enouf, V., Chwetzoff, S., Trugnan, G., Cohen, J. (2003). Interactions of Rotavirus VP4 Spike Protein with the Endosomal Protein Rab5 and the Prenylated Rab Acceptor PRA1. J. Virol. 77: 7041-7047 [Abstract] [Full Text]  
  • Sapin, C., Colard, O., Delmas, O., Tessier, C., Breton, M., Enouf, V., Chwetzoff, S., Ouanich, J., Cohen, J., Wolf, C., Trugnan, G. (2002). Rafts Promote Assembly and Atypical Targeting of a Nonenveloped Virus, Rotavirus, in Caco-2 Cells. J. Virol. 76: 4591-4602 [Abstract] [Full Text]  
  • Mohan, K. V. K., Som, I., Atreya, C. D. (2002). Identification of a Type 1 Peroxisomal Targeting Signal in a Viral Protein and Demonstration of Its Targeting to the Organelle. J. Virol. 76: 2543-2547 [Abstract] [Full Text]  
  • Poisson, N., Real, E., Gaudin, Y., Vaney, M.-C., King, S., Jacob, Y., Tordo, N., Blondel, D. (2001). Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: dissociation of dynein-binding properties and transcriptional functionality of P. J. Gen. Virol. 82: 2691-2696 [Abstract] [Full Text]  
  • Zhang, M., Zeng, C. Q.-Y., Morris, A. P., Estes, M. K. (2000). A Functional NSP4 Enterotoxin Peptide Secreted from Rotavirus-Infected Cells. J. Virol. 74: 11663-11670 [Abstract] [Full Text]