HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 30, 27006-27013, July 26, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/30/27006    most recent M203228200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fabre, S. Articles by Lopez, M. Search for Related Content PubMed PubMed Citation Articles by Fabre, S. Articles by Lopez, M. Social Bookmarking                      What's this?

Prominent Role of the Ig-like V Domain in trans-Interactions of Nectins
NECTIN3 AND NECTIN4 BIND TO THE PREDICTED C-C'-C"-D -STRANDS OF THE NECTIN1 V DOMAIN^*

Stéphanie Fabre, Nicolas Reymond, Francesca Cocchi^§, Laura Menotti^§, Patrice Dubreuil, Gabriella Campadelli-Fiume^§, and Marc Lopez^¶

From the  Institute of Cancer Biology and Immunology, Institut de la Santé et de la Recherche Médicale U.119, 27 bd Lei-Roure 13009, Marseille, France and the ^§ Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo, 12, 40126 Bologna, Italy

Nectins form a family of integral molecules that belong to the immunoglobulin superfamily. Their ectodomain is made of three Ig-like domains (V, C, C). This family comprises at least five members, namely nectin1, -2, -3, -4, and poliovirus receptor (PVR), that are involved in different physiological and pathological processes. (i) Nectins are adhesion molecules localized at adherens junctions in epithelial cells. (ii) Some nectins act as poliovirus or -herpesvirus receptors (nectin1). (iii) Nectin1 mutations are involved in orofacial developmental abnormalities in humans. Adhesion properties of nectins are mediated by Ca²⁺-independent homophilic and heterophilic processes through ectodomain trans-interactions. We have described a nectin trans-hetero-interaction network: nectin3 binds to nectin1, nectin2, and PVR; nectin1 also binds to nectin4. In the present study we compared the affinities of the different trans-interactions mediated by nectin1. We found that the K_D of nectin1/nectin3 and nectin1/nectin4 interactions is 1 and 100 nM, respectively, whereas the K_D of the nectin1-mediated homophilic interaction is 1 µM. We show that nectin1/nectin3 and nectin1/nectin4 trans-hetero-interactions were mediated through trans V to V domain interactions, whereas C domains contributed to increase the affinity of the interaction. Nectin3 and nectin4 share a common binding region in the nectin1 V domain: (i) nectin3 strongly competed with nectin4 binding, (ii) nectin3 and nectin4 binding to nectin1 was reduced by a number of monoclonal antibodies directed against the nectin1 V domain, and (iii) the glycoprotein D of herpes simplex virus-1 that binds to the V domain of nectin1 reduced nectin3 and nectin4 binding. Finally, using chimeric nectin1/PVR receptors where PVR V domain -strands were substituted with the corresponding regions of nectin1, the nectin3 and nectin4 minimal binding region on nectin1 V domain was mapped to the C-C'-C"-D -strands.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				E. Ono, Y. Tomioka, Y. Watanabe, K. Amagai, M. Morimatsu, K. Shinya, and P. Cherel Comparison of the antiviral potentials among the pseudorabies-resistant transgenes encoding different soluble forms of porcine nectin-1 in transgenic mice J. Gen. Virol., October 1, 2007; 88(10): 2636 - 2641. [Abstract] [Full Text] [PDF]

				H. Togashi, J. Miyoshi, T. Honda, T. Sakisaka, Y. Takai, and M. Takeichi Interneurite affinity is regulated by heterophilic nectin interactions in concert with the cadherin machinery J. Cell Biol., July 3, 2006; 174(1): 141 - 151. [Abstract] [Full Text] [PDF]

				X. Dong, F. Xu, Y. Gong, J. Gao, P. Lin, T. Chen, Y. Peng, B. Qiang, J. Yuan, X. Peng, et al. 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., April 14, 2006; 281(15): 10610 - 10617. [Abstract] [Full Text] [PDF]

				H. Kwon, Q. Bai, H.-J. Baek, K. Felmet, E. A. Burton, W. F. Goins, J. B. Cohen, and J. C. Glorioso 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., January 1, 2006; 80(1): 138 - 148. [Abstract] [Full Text] [PDF]

				K. S. Boles, W. Barchet, T. Diacovo, M. Cella, and M. Colonna The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAM Blood, August 1, 2005; 106(3): 779 - 786. [Abstract] [Full Text] [PDF]

				D. Fusco, C. Forghieri, and G. Campadelli-Fiume The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors PNAS, June 28, 2005; 102(26): 9323 - 9328. [Abstract] [Full Text] [PDF]

				S. Fabre-Lafay, S. Garrido-Urbani, N. Reymond, A. Goncalves, P. Dubreuil, and M. Lopez Nectin-4, a New Serological Breast Cancer Marker, Is a Substrate for Tumor Necrosis Factor-{alpha}-converting Enzyme (TACE)/ADAM-17 J. Biol. Chem., May 20, 2005; 280(20): 19543 - 19550. [Abstract] [Full Text] [PDF]

				F. Struyf, A. E. Plate, and P. G. Spear 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., March 15, 2005; 79(6): 3841 - 3845. [Abstract] [Full Text] [PDF]

				N. Reymond, A.-M. Imbert, E. Devilard, S. Fabre, C. Chabannon, L. Xerri, C. Farnarier, C. Cantoni, C. Bottino, A. Moretta, et al. DNAM-1 and PVR Regulate Monocyte Migration through Endothelial Junctions J. Exp. Med., May 17, 2004; 199(10): 1331 - 1341. [Abstract] [Full Text] [PDF]

				F. Cocchi, L. Menotti, V. Di Ninni, M. Lopez, and G. Campadelli-Fiume 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., May 1, 2004; 78(9): 4720 - 4729. [Abstract] [Full Text] [PDF]

				C. Krummenacher, I. Baribaud, R. J. Eisenberg, and G. H. Cohen Cellular Localization of Nectin-1 and Glycoprotein D during Herpes Simplex Virus Infection J. Virol., August 15, 2003; 77(16): 8985 - 8999. [Abstract] [Full Text] [PDF]

				Y. Tanaka, H. Nakanishi, S. Kakunaga, N. Okabe, T. Kawakatsu, K. Shimizu, and Y. Takai Role of Nectin in Formation of E-Cadherin-based Adherens Junctions in Keratinocytes: Analysis with the N-Cadherin Dominant Negative Mutant Mol. Biol. Cell, April 1, 2003; 14(4): 1597 - 1609. [Abstract] [Full Text] [PDF]

				G. Zhou, E. Avitabile, G. Campadelli-Fiume, and B. Roizman 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., March 15, 2003; 77(6): 3759 - 3767. [Abstract] [Full Text] [PDF]

				Y. Takai and H. Nakanishi Nectin and afadin: novel organizers of intercellular junctions J. Cell Sci., January 1, 2003; 116(1): 17 - 27. [Abstract] [Full Text] [PDF]

				F. Struyf, W. M. Martinez, and P. G. Spear 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., November 13, 2002; 76(24): 12940 - 12950. [Abstract] [Full Text] [PDF]