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 Lopez, M.
Right arrow Articles by Dubreuil, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lopez, M.
Right arrow Articles by Dubreuil, P.

 Previous Article  |  Next Article 

Journal of Virology, June 2001, p. 5684-5691, Vol. 75, No. 12
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.12.5684-5691.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Novel, Soluble Isoform of the Herpes Simplex Virus (HSV) Receptor Nectin1 (or PRR1-HIgR-HveC) Modulates Positively and Negatively Susceptibility to HSV Infection

Marc Lopez,1 Francesca Cocchi,2 Elisa Avitabile,2 Annouck Leclerc,1 Jose Adelaide,1 Gabriella Campadelli-Fiume,2 and Patrice Dubreuil1,*

Institute of Cancer Biology and Immunology, Institut de la Santé et de la Recherche Médicale U.119, 13009 Marseille, France,1 and Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, 40126 Bologna, Italy2

Received 23 January 2001/Accepted 18 March 2001

A novel member of the nectin family, nectin1gamma , was molecularly cloned. The cDNA has the same ectodomain as nectin1alpha and nectin1beta , the two known transmembrane isoforms that serve as receptors for herpes simplex virus (HSV) entry into human cell lines (nectin1alpha and nectin1beta , also called PRR1-HveC and HIgR, respectively). The 1.4-kb transcript, which originated by alternative splicing, is expressed in human cell lines, and appears to have a narrow distribution in human tissues. The sequence does not have a hydrophobic anchoring region, and the protein is secreted in the culture medium of cells transfected with the cDNA. Nectin1gamma , purified from culture medium, can compete with membrane-bound nectin1beta and reduce HSV infectivity. The expression of nectin1gamma cDNA in cells resistant to HSV infection and lacking HSV receptors enables HSV to enter the cell, which implies that it is present at the cell surface. Thus, nectin1gamma has the potential both to mediate and to reduce HSV entry into cells.


* Corresponding author. Mailing address: INSERM U.119, 27 bd Lei-Roure, 13009 Marseille, France. Phone: 33-4-91-75-84-18. Fax: 33-4-91-26-03-64. E-mail: dubreuil{at}marseille.inserm.fr.


Journal of Virology, June 2001, p. 5684-5691, Vol. 75, No. 12
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.12.5684-5691.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Kwon, H., Bai, Q., Baek, H.-J., Felmet, K., Burton, E. A., Goins, W. F., Cohen, J. B., Glorioso, J. C. (2006). Soluble V Domain of Nectin-1/HveC Enables Entry of Herpes Simplex Virus Type 1 (HSV-1) into HSV-Resistant Cells by Binding to Viral Glycoprotein D. J. Virol. 80: 138-148 [Abstract] [Full Text]  
  • Fabre-Lafay, S., Garrido-Urbani, S., Reymond, N., Goncalves, A., Dubreuil, P., Lopez, M. (2005). Nectin-4, a New Serological Breast Cancer Marker, Is a Substrate for Tumor Necrosis Factor-{alpha}-converting Enzyme (TACE)/ADAM-17. J. Biol. Chem. 280: 19543-19550 [Abstract] [Full Text]  
  • Connolly, S. A., Landsburg, D. J., Carfi, A., Whitbeck, J. C., Zuo, Y., Wiley, D. C., Cohen, G. H., Eisenberg, R. J. (2005). Potential Nectin-1 Binding Site on Herpes Simplex Virus Glycoprotein D. J. Virol. 79: 1282-1295 [Abstract] [Full Text]  
  • Cocchi, F., Menotti, L., Di Ninni, V., Lopez, M., Campadelli-Fiume, G. (2004). The Herpes Simplex Virus JMP Mutant Enters Receptor-Negative J Cells through a Novel Pathway Independent of the Known Receptors nectin1, HveA, and nectin2. J. Virol. 78: 4720-4729 [Abstract] [Full Text]  
  • Takai, Y., Nakanishi, H. (2003). Nectin and afadin: novel organizers of intercellular junctions. J. Cell Sci. 116: 17-27 [Abstract] [Full Text]  
  • Struyf, F., Martinez, W. M., Spear, P. G. (2002). Mutations in the N-Terminal Domains of Nectin-1 and Nectin-2 Reveal Differences in Requirements for Entry of Various Alphaherpesviruses and for Nectin-Nectin Interactions. J. Virol. 76: 12940-12950 [Abstract] [Full Text]  
  • Zhou, G., Roizman, B. (2002). Cation-Independent Mannose 6-Phosphate Receptor Blocks Apoptosis Induced by Herpes Simplex Virus 1 Mutants Lacking Glycoprotein D and Is Likely the Target of Antiapoptotic Activity of the Glycoprotein. J. Virol. 76: 6197-6204 [Abstract] [Full Text]  
  • Menotti, L., Casadio, R., Bertucci, C., Lopez, M., Campadelli-Fiume, G. (2002). Substitution in the Murine Nectin1 Receptor of a Single Conserved Amino Acid at a Position Distal from the Herpes Simplex Virus gD Binding Site Confers High-Affinity Binding to gD. J. Virol. 76: 5463-5471 [Abstract] [Full Text]  
  • Martinez, W. M., Spear, P. G. (2001). Structural Features of Nectin-2 (HveB) Required for Herpes Simplex Virus Entry. J. Virol. 75: 11185-11195 [Abstract] [Full Text]  
  • Reymond, N., Fabre, S., Lecocq, E., Adelaide, J., Dubreuil, P., Lopez, M. (2001). Nectin4/PRR4, a New Afadin-associated Member of the Nectin Family That Trans-interacts with Nectin1/PRR1 through V Domain Interaction. J. Biol. Chem. 276: 43205-43215 [Abstract] [Full Text]  
  • Cocchi, F., Lopez, M., Dubreuil, P., Campadelli Fiume, G., Menotti, L. (2001). Chimeric Nectin1-Poliovirus Receptor Molecules Identify a Nectin1 Region Functional in Herpes Simplex Virus Entry. J. Virol. 75: 7987-7994 [Abstract] [Full Text]