Previous Article | Next Article 
Journal of Virology, September 2001, p. 7987-7994, Vol. 75, No. 17
Section on Microbiology and Virology, Department of
Experimental Pathology, University of Bologna, 40126 Bologna,
Italy,1 and Institute of Cancer Biology
and Immunology, Institut de la Santé et de la Recherche
Médicale U.119, Marseille, France2
Received 22 February 2001/Accepted 4 June 2001
Human nectin1 (hNectin1), an adhesion molecule belonging to the
nectin family of the immunoglobulin superfamily, mediates entry of
herpes simplex virus (HSV) into cells. The hNectin1 domain that
mediates virus entry into cells and also binds glycoprotein D (gD) has
been localized to the first N-terminal V-type domain. The poliovirus
receptor (PVR) is a structural homolog to nectins, but it cannot
function as an HSV entry receptor. hNectin1-PVR chimeras were
constructed to functionally locate the site on hNectin1 involved in HSV
entry (HSV entry site). The epitope recognized by monoclonal antibody
(MAb) R1.302, which is able to block HSV entry, was also located. The
chimeric receptors were designed to preserve the overall structure of
the V domain. The HSV entry activity mapped entirely to the hNectin1
portion located between residues 64 and 94 (64-94), likely to encode
the C, C', and C"
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.17.7987-7994.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Chimeric Nectin1-Poliovirus Receptor Molecules Identify a Nectin1
Region Functional in Herpes Simplex Virus Entry
-strands and intervening loops. In turn, this site
consisted of two portions: one with low-level basal activity for HSV
entry (77-94), and one immediately upstream (residues 64 to 76) which greatly enhanced the HSV entry activity of the downstream region. The
gD-binding site mapped substantially to the same site, whereas the MAb
R1.302 epitope also required a further downstream portion (95-102). The
involvement of the 64-76 portion is at difference with previous
indirect mapping results that were based on competitive binding studies
(C. Krummenacher et al., J. Virol. 74:10863-10872, 2000). The A,
A', B, D, E, F, and G -strands and intervening loops did not appear
to play any role in HSV entry. According to the predicted
three-dimensional structure of PVR, the C C' C" site is located
peripherally in the V domain and very likely represents an accessible
portion at the cell surface.
*
Corresponding author. Mailing address: Department of
Experimental Pathology, Section on Microbiology and Virology,
University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy.
Phone: 39 051 2094733/2094731. Fax: 39 051 2094735. E-mail:
menotti{at}kaiser.alma.unibo.it.
Journal of Virology, September 2001, p. 7987-7994, Vol. 75, No. 17
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.17.7987-7994.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
This article has been cited by other articles:
-
Ono, E., Tomioka, Y., Watanabe, Y., Amagai, K., Morimatsu, M., Shinya, K., Cherel, P.
(2007). Comparison of the antiviral potentials among the pseudorabies-resistant transgenes encoding different soluble forms of porcine nectin-1 in transgenic mice. J. Gen. Virol.
88: 2636-2641
[Abstract] [Full Text] -
Dong, X., Xu, F., Gong, Y., Gao, J., Lin, P., Chen, T., Peng, Y., Qiang, B., Yuan, J., Peng, X., Rao, Z.
(2006). Crystal Structure of the V Domain of Human Nectin-like Molecule-1/Syncam3/Tsll1/Igsf4b, a Neural Tissue-specific Immunoglobulin-like Cell-Cell Adhesion Molecule. J. Biol. Chem.
281: 10610-10617
[Abstract] [Full Text] -
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] -
Struyf, F., Plate, A. E., Spear, P. G.
(2005). Deletion of the Second Immunoglobulin-Like Domain of Nectin-1 Alters Its Intracellular Processing and Localization and Ability To Mediate Entry of Herpes Simplex Virus. J. Virol.
79: 3841-3845
[Abstract] [Full Text] -
Gianni, T., Campadelli-Fiume, G., Menotti, L.
(2004). Entry of Herpes Simplex Virus Mediated by Chimeric Forms of Nectin1 Retargeted to Endosomes or to Lipid Rafts Occurs through Acidic Endosomes. J. Virol.
78: 12268-12276
[Abstract] [Full Text] -
Cocchi, F., Fusco, D., Menotti, L., Gianni, T., Eisenberg, R. J., Cohen, G. H., Campadelli-Fiume, G.
(2004). The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry. Proc. Natl. Acad. Sci. USA
101: 7445-7450
[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] -
Spear, P. G., Longnecker, R.
(2003). Herpesvirus Entry: an Update. J. Virol.
77: 10179-10185
[Full Text] -
Krummenacher, C., Baribaud, I., Eisenberg, R. J., Cohen, G. H.
(2003). Cellular Localization of Nectin-1 and Glycoprotein D during Herpes Simplex Virus Infection. J. Virol.
77: 8985-8999
[Abstract] [Full Text] -
Avitabile, E., Lombardi, G., Campadelli-Fiume, G.
(2003). Herpes Simplex Virus Glycoprotein K, but Not Its Syncytial Allele, Inhibits Cell-Cell Fusion Mediated by the Four Fusogenic Glycoproteins, gD, gB, gH, and gL. J. Virol.
77: 6836-6844
[Abstract] [Full Text] -
Zhou, G., Avitabile, E., Campadelli-Fiume, G., Roizman, B.
(2003). The Domains of Glycoprotein D Required To Block Apoptosis Induced by Herpes Simplex Virus 1 Are Largely Distinct from Those Involved in Cell-Cell Fusion and Binding to Nectin1. J. Virol.
77: 3759-3767
[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] -
Fabre, S., Reymond, N., Cocchi, F., Menotti, L., Dubreuil, P., Campadelli-Fiume, G., Lopez, M.
(2002). Prominent Role of the Ig-like V Domain in trans-Interactions of Nectins. NECTIN3 AND NECTIN4 BIND TO THE PREDICTED C-C'-C"-D beta -STRANDS OF THE NECTIN1 V DOMAIN. J. Biol. Chem.
277: 27006-27013
[Abstract] [Full Text] -
Martinez, W. M., Spear, P. G.
(2002). Amino Acid Substitutions in the V Domain of Nectin-1 (HveC) That Impair Entry Activity for Herpes Simplex Virus Types 1 and 2 but Not for Pseudorabies Virus or Bovine Herpesvirus 1. J. Virol.
76: 7255-7262
[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] -
Krummenacher, C., Baribaud, I., Sanzo, J. F., Cohen, G. H., Eisenberg, R. J.
(2002). Effects of Herpes Simplex Virus on Structure and Function of Nectin-1/HveC. J. Virol.
76: 2424-2433
[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]
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»