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Journal articles on the topic 'Nectin-1'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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1

Yoshida, Toshiyuki, Yoshimi Takai, and Irma Thesleff. "Cooperation of Nectin-1 and Nectin-3 Is Required for Maintenance of Epidermal Stratification and Proper Hair Shaft Formation in the Mouse." Developmental Biology Journal 2014 (June 30, 2014): 1–12. http://dx.doi.org/10.1155/2014/432043.

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Nectins constitute a family of four cell adhesion molecules which are localized on cell membrane. Mutations in NECTIN-1 gene cause the human ectodermal dysplasia syndrome (CLPED1) manifesting severe defects in skin and its appendages. However, nectin-1 null mutant mice have only a mild defect in epidermal stratification suggesting compensation by other nectins. We have analysed the epidermal and hair phenotypes of nectin-1; nectin-3 compound mutants. Epidermis was fragile and displayed severe defects in stratification, hair follicles were hypoplastic, and hair shaft structure was abnormal. Imm

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2

Struyf, Frank, Aileen E. Plate, and Patricia 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." Journal of Virology 79, no. 6 (2005): 3841–45. http://dx.doi.org/10.1128/jvi.79.6.3841-3845.2005.

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ABSTRACT Nectin-1 is an immunoglobulin (Ig)-like entry receptor for herpes simplex virus (HSV). Like other nectins, nectin-1 forms dimers and mediates cell adhesion through interactions with other nectins. We constructed a second-domain deletion mutant of nectin-1 (nectin-1-Δ2) to examine the role of the second Ig-like domain in HSV entry. Nectin-1-Δ2 exhibited a severely reduced ability to mediate HSV entry and accumulated in the endoplasmic reticulum but retained the ability to interact with its HSV ligand, gD. The failure of nectin-1-Δ2 to mediate HSV entry probably resulted from its failur

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3

Struyf, Frank, Wanda M. Martinez, and Patricia 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." Journal of Virology 76, no. 24 (2002): 12940–50. http://dx.doi.org/10.1128/jvi.76.24.12940-12950.2002.

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ABSTRACT Nectin-1 and nectin-2 are related molecules that can function with different specificities as entry receptors for mammalian alphaherpesviruses through interaction with viral glycoprotein D (gD). The normal function of members of the nectin family is to mediate cell-cell adhesion through homotypic and heterotypic nectin-nectin interactions in cadherin-based adherens junctions. We examined mutations in three equivalent regions of the N-terminal V-like domains of nectin-1 and nectin-2 to test the effects on entry of various alphaherpesviruses, nectin-nectin interactions, and interactions

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4

Krummenacher, Claude, Isabelle Baribaud, Roselyn J. Eisenberg, and Gary H. Cohen. "Cellular Localization of Nectin-1 and Glycoprotein D during Herpes Simplex Virus Infection." Journal of Virology 77, no. 16 (2003): 8985–99. http://dx.doi.org/10.1128/jvi.77.16.8985-8999.2003.

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ABSTRACT During viral entry, herpes simplex virus (HSV) glycoprotein D (gD) interacts with a specific cellular receptor such as nectin-1 (PRR1/HveC/CD111) or the herpesvirus entry mediator A (HVEM/HveA). Nectin-1 is involved in cell-to-cell adhesion. It is located at adherens junctions, where it bridges cells through homophilic or heterophilic interactions with other nectins. Binding of HSV gD prevents nectin-1-mediated cell aggregation. Since HSV gD affects the natural function of nectin-1, we further investigated the effects of gD expression on nectin-1 during HSV infection or in transfected

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5

Brakeman, Paul R., Kathleen D. Liu, Kazuya Shimizu, Yoshimi Takai, and Keith E. Mostov. "Nectin proteins are expressed at early stages of nephrogenesis and play a role in renal epithelial cell morphogenesis." American Journal of Physiology-Renal Physiology 296, no. 3 (2009): F564—F574. http://dx.doi.org/10.1152/ajprenal.90328.2008.

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Development of the nephron requires conversion of the metanephric mesenchyme into tubular epithelial structures with specifically organized intercellular junctions. The nectin proteins are a family of transmembrane proteins that dimerize to form intercellular junctional complexes between epithelial cells. In this study, we demonstrate that nectin junctions appear during the earliest stages of epithelial cell morphogenesis in the murine nephron concurrently with the transition of mesenchymal cells into epithelial cells. We have defined the role of nectin during epithelial cell morphogenesis by

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6

Patrusheva, Irina, Ludmila Perelygina, Ivan Torshin, Julia LeCher, and Julia Hilliard. "B Virus (Macacine Herpesvirus 1) Divergence: Variations in Glycoprotein D from Clinical and Laboratory Isolates Diversify Virus Entry Strategies." Journal of Virology 90, no. 20 (2016): 9420–32. http://dx.doi.org/10.1128/jvi.00799-16.

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ABSTRACTB virus (Macacine herpesvirus 1) can cause deadly zoonotic disease in humans. Molecular mechanisms of B virus cell entry are poorly understood for both macaques and humans. Here we investigated the abilities of clinical B virus isolates to use entry receptors of herpes simplex viruses (HSV). We showed that resistant B78H1 cells became susceptible to B virus clinical strains upon expression of either human nectin-2 or nectin-1. Antibody against glycoprotein D (gD) protected these nectin-bearing cells from B virus infection, and a gD-negative recombinant B virus failed to enter these cel

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7

Chu, Carissa, Martin Sjöström, Emily A. Egusa, et al. "Heterogeneity in Nectin-4 expression across molecular subtypes of urothelial cancer mediates sensitivity to enfortumab vedotin." Journal of Clinical Oncology 39, no. 6_suppl (2021): 463. http://dx.doi.org/10.1200/jco.2021.39.6_suppl.463.

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463 Background: Enfortumab vedotin (EV) is an antibody-drug conjugate (ADC) targeting Nectin-4 (encoded by the PVRL4/NECTIN4 gene ) approved for treatment-refractory metastatic urothelial cancer. Factors that mediate sensitivity or resistance to EV are unknown. In the present study, we sought to 1) examine heterogeneity of NECTIN4 gene expression across molecular subtypes of bladder cancer and 2) determine if Nectin-4 expression mediates EV sensitivity or resistance. Methods: NECTIN4 expression data from seven muscle-invasive bladder cancer clinical cohorts (n = 1912 total patients) were used

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8

Uchida, Hiroaki, Janet Chan, William F. Goins, et al. "A Double Mutation in Glycoprotein gB Compensates for Ineffective gD-Dependent Initiation of Herpes Simplex Virus Type 1 Infection." Journal of Virology 84, no. 23 (2010): 12200–12209. http://dx.doi.org/10.1128/jvi.01633-10.

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ABSTRACT Herpes simplex virus (HSV) entry into cells is triggered by the binding of envelope glycoprotein D (gD) to a specific receptor, such as nectin-1 or herpesvirus entry mediator (HVEM), resulting in activation of the fusion effectors gB and gH and virus penetration. Here we report the identification of a hyperactive gB allele, D285N/A549T, selected by repeat passage of a gD mutant virus defective for nectin-1 binding through cells that express a gD-binding-impaired mutant nectin-1. The gB allele in a wild-type virus background enabled the use of other nectins as virus entry receptors. In

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9

Mizoguchi, Akira, Hiroyuki Nakanishi, Kazushi Kimura, et al. "Nectin." Journal of Cell Biology 156, no. 3 (2002): 555–65. http://dx.doi.org/10.1083/jcb.200103113.

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The nectin–afadin system is a novel cell–cell adhesion system that organizes adherens junctions cooperatively with the cadherin–catenin system in epithelial cells. Nectin is an immunoglobulin-like adhesion molecule, and afadin is an actin filament–binding protein that connects nectin to the actin cytoskeleton. Nectin has four isoforms (-1, -2, -3, and -4). Each nectin forms a homo-cis-dimer followed by formation of a homo-trans-dimer, but nectin-3 furthermore forms a hetero-trans-dimer with nectin-1 or -2, and the formation of each hetero-trans-dimer is stronger than that of each homo-trans-di

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10

Krummenacher, Claude, Isabelle Baribaud, James F. Sanzo, Gary H. Cohen, and Roselyn J. Eisenberg. "Effects of Herpes Simplex Virus on Structure and Function of Nectin-1/HveC." Journal of Virology 76, no. 5 (2002): 2424–33. http://dx.doi.org/10.1128/jvi.76.5.2424-2433.2002.

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ABSTRACT Herpes simplex virus (HSV) entry requires the interaction between the envelope glycoprotein D (gD) and a cellular receptor such as nectin-1 (also named herpesvirus entry mediator C [HveC]) or HveA/HVEM. Nectin-1 is a cell adhesion molecule found at adherens junctions associated with the cytoplasmic actin-binding protein afadin. Nectin-1 can act as its own ligand in a homotypic interaction to bridge cells together. We used a cell aggregation assay to map an adhesive functional site on nectin-1 and identify the effects of gD binding and HSV early infection on nectin-1 function. Soluble

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11

Petermann, Philipp, Katharina Thier, Elena Rahn, et al. "Entry Mechanisms of Herpes Simplex Virus 1 into Murine Epidermis: Involvement of Nectin-1 and Herpesvirus Entry Mediator as Cellular Receptors." Journal of Virology 89, no. 1 (2014): 262–74. http://dx.doi.org/10.1128/jvi.02917-14.

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ABSTRACTSkin keratinocytes represent a primary entry site for herpes simplex virus 1 (HSV-1)in vivo. The cellular proteins nectin-1 and herpesvirus entry mediator (HVEM) act as efficient receptors for both serotypes of HSV and are sufficient for disease development mediated by HSV-2 in mice. How HSV-1 enters skin and whether both nectin-1 and HVEM are involved are not known. We addressed the impact of nectin-1 during entry of HSV-1 into murine epidermis and investigated the putative contribution of HVEM. Usingex vivoinfection of murine epidermis, we showed that HSV-1 entered the basal keratino

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12

Yue, Dan, Zhujun Chen, Fanli Yang, et al. "Crystal structure of bovine herpesvirus 1 glycoprotein D bound to nectin-1 reveals the basis for its low-affinity binding to the receptor." Science Advances 6, no. 20 (2020): eaba5147. http://dx.doi.org/10.1126/sciadv.aba5147.

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Bovine herpesvirus 1 (BHV-1) has received increasing attention for its potential oncolytic applications. BHV-1 recognizes nectin-1 for cell entry via viral glycoprotein D (gD) but represents a low-affinity nectin-1 binding virus. The molecular basis underlying this low receptor-binding affinity, however, remains unknown. Here, the crystal structures of BHV-1 gD in the free and nectin-1–bound forms are presented. While showing an overall resembled nectin-1 binding mode to other alphaherpesvirus gDs, BHV-1 gD has a unique G-strand/α2-helix interloop that disturbs gD/nectin-1 interactions. Residu

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13

Sakisaka, Toshiaki, Tomokuni Taniguchi, Hiroyuki Nakanishi та ін. "Requirement of Interaction of Nectin-1α/HveC with Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus Type 1". Journal of Virology 75, № 10 (2001): 4734–43. http://dx.doi.org/10.1128/jvi.75.10.4734-4743.2001.

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ABSTRACT We recently found a novel cell-cell adhesion system at cadherin-based adherens junctions (AJs), consisting at least of nectin, a Ca2+-independent homophilic immunoglobulin-like adhesion molecule, and afadin, an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin is associated with cadherin through afadin and α-catenin. The cadherin-catenin system increases the concentration of nectin at AJs in an afadin-dependent manner. Nectin constitutes a family consisting of three members: nectin-1, -2, and -3. Nectin-1 serves as an entry and cell-cell spread medi

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14

McKean, Meredith, Gerald Steven Falchook, Johanna C. Bendell, et al. "Association of combined phase I/II study of a novel bicyclic peptide and MMAE conjugate BT8009 in patients with advanced malignancies with Nectin-4 expression." Journal of Clinical Oncology 39, no. 15_suppl (2021): TPS2668. http://dx.doi.org/10.1200/jco.2021.39.15_suppl.tps2668.

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TPS2668 Background: BT8009 is a Bicycle Toxin Conjugate (BTC), a novel class of chemically synthesized molecules, comprising a bicyclic peptide targeting Nectin-4 tumor antigen, linked to cytotoxin (monomethyl auristatin E [MMAE]) via a valine-citrulline (val-cit) cleavable linker. Nectins (Nectin-1, -2, -3, and -4) and nectin-like molecules (Necl) are Ca2+ independent immunoglobulin-like cell adhesion molecules. Recent studies have shown the importance of Nectin-4 in several human cancers, including lung, ovarian, breast and bladder cancer; however, the precise roles and clinical relevance of

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15

Richart, Sarah M., Scott A. Simpson, Claude Krummenacher, et al. "Entry of Herpes Simplex Virus Type 1 into Primary Sensory Neurons In Vitro Is Mediated by Nectin-1/HveC." Journal of Virology 77, no. 5 (2003): 3307–11. http://dx.doi.org/10.1128/jvi.77.5.3307-3311.2003.

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ABSTRACT Primary cultures of rat and mouse sensory neurons were used to study the entry of herpes simplex virus type 1 (HSV-1). Soluble, truncated nectin-1 but not HveA prevented viral entry. Antibodies against nectin-1 also blocked infection of rat neurons. These results indicate that nectin-1 is the primary receptor for HSV-1 infection of sensory neurons.

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Petermann, Philipp, Elena Rahn, Katharina Thier, et al. "Role of Nectin-1 and Herpesvirus Entry Mediator as Cellular Receptors for Herpes Simplex Virus 1 on Primary Murine Dermal Fibroblasts." Journal of Virology 89, no. 18 (2015): 9407–16. http://dx.doi.org/10.1128/jvi.01415-15.

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ABSTRACTThe cellular proteins nectin-1 and herpesvirus entry mediator (HVEM) can both mediate the entry of herpes simplex virus 1 (HSV-1). We have recently shown how these receptors contribute to infection of skin by investigating HSV-1 entry into murine epidermis.Ex vivoinfection studies reveal nectin-1 as the primary receptor in epidermis, whereas HVEM has a more limited role. Although the epidermis represents the outermost layer of skin, the contribution of nectin-1 and HVEM in the underlying dermis is still open. Here, we analyzed the role of each receptor during HSV-1 entry in murine derm

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17

Linehan, Melissa M., Susan Richman, Claude Krummenacher, Roselyn J. Eisenberg, Gary H. Cohen, and Akiko Iwasaki. "In Vivo Role of Nectin-1 in Entry of Herpes Simplex Virus Type 1 (HSV-1) and HSV-2 through the Vaginal Mucosa." Journal of Virology 78, no. 5 (2004): 2530–36. http://dx.doi.org/10.1128/jvi.78.5.2530-2536.2004.

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ABSTRACT Herpes simplex virus type 2 (HSV-2) is transmitted through the genital mucosa during sexual encounters. In recent years, HSV-1 has also become commonly associated with primary genital herpes. The mechanism of viral entry of HSV-1 and HSV-2 in the female genital tract is unknown. In order to understand the molecular interactions required for HSV entry into the vaginal epithelium, we examined the expression of herpesvirus entry mediator nectin-1 in the vagina of human and mouse at different stages of their hormonal cycle. Nectin-1 was highly expressed in the epithelium of human vagina t

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Yoon, Miri, and Patricia G. Spear. "Disruption of Adherens Junctions Liberates Nectin-1 To Serve as Receptor for Herpes Simplex Virus and Pseudorabies Virus Entry." Journal of Virology 76, no. 14 (2002): 7203–8. http://dx.doi.org/10.1128/jvi.76.14.7203-7208.2002.

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ABSTRACT Nectin-1, a cell adhesion molecule belonging to the immunoglobulin superfamily, can bind to virion glycoprotein D (gD) to mediate entry of herpes simplex viruses (HSV) and pseudorabies virus (PRV). Nectin-1 colocalizes with E-cadherin at adherens junctions in epithelial cells. The disruption of cell junctions can result in the redistribution of nectin-1. To determine whether disruption of junctions by calcium depletion influenced the susceptibility of epithelial cells to viral entry, Madin-Darby canine kidney cells expressing endogenous nectin-1 or transfected human nectin-1 were test

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Yokoyama, Shigekazu, Kouichi Tachibana, Hiroyuki Nakanishi та ін. "α-Catenin-independent Recruitment of ZO-1 to Nectin-based Cell-Cell Adhesion Sites through Afadin". Molecular Biology of the Cell 12, № 6 (2001): 1595–609. http://dx.doi.org/10.1091/mbc.12.6.1595.

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ZO-1 is an actin filament (F-actin)–binding protein that localizes to tight junctions and connects claudin to the actin cytoskeleton in epithelial cells. In nonepithelial cells that have no tight junctions, ZO-1 localizes to adherens junctions (AJs) and may connect cadherin to the actin cytoskeleton indirectly through β- and α-catenins as one of many F-actin–binding proteins. Nectin is an immunoglobulin-like adhesion molecule that localizes to AJs and is associated with the actin cytoskeleton through afadin, an F-actin–binding protein. Ponsin is an afadin- and vinculin-binding protein that als

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Guzman, Grace, Stephen Oh, Deepak Shukla, and Tibor Valyi-Nagy. "Nectin-1 Expression in the Normal and Neoplastic Human Uterine Cervix." Archives of Pathology & Laboratory Medicine 130, no. 8 (2006): 1193–95. http://dx.doi.org/10.5858/2006-130-1193-neitna.

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Abstract Context.—Nectin-1 is an immunoglobulin-like adhesion molecule that is widely expressed in epithelial tissues and participates in the formation of adherens junctions. Reduced expression of nectin-1 has been reported in invasive carcinomas of the human skin. Objective.—To determine the pattern of nectin-1 expression in the normal, dysplastic, and neoplastic human uterine cervix. Design.—This retrospective study was performed using immunohistochemistry of specimens of normal mucosa (n = 18) and preneoplastic and neoplastic conditions of the human uterine cervix including squamous dysplas

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Martinez, Wanda M., and Patricia G. Spear. "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." Journal of Virology 76, no. 14 (2002): 7255–62. http://dx.doi.org/10.1128/jvi.76.14.7255-7262.2002.

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ABSTRACT The entry of herpes simplex virus (HSV) into cells requires the interaction of viral glycoprotein D (gD) with a cellular gD receptor to trigger the fusion of viral and cellular membranes. Nectin-1, a member of the immunoglobulin superfamily, can serve as a gD receptor for HSV types 1 and 2 (HSV-1 and HSV-2, respectively) as well as for the animal herpesviruses porcine pseudorabies virus (PRV) and bovine herpesvirus 1 (BHV-1). The HSV-1 gD binding domain of nectin-1 is hypothesized to overlap amino acids 64 to 104 of the N-terminal variable domain-like immunoglobulin domain. Moreover,

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Rotunno, Roberta, Andrea Diociaiuti, Maria Lisa Dentici, et al. "Ectodermal Dysplasia-Syndactyly Syndrome with Toe-Only Minimal Syndactyly Due to a Novel Mutation in NECTIN4: A Case Report and Literature Review." Genes 12, no. 5 (2021): 748. http://dx.doi.org/10.3390/genes12050748.

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Ectodermal dysplasia-syndactyly syndrome 1 (EDSS1) is characterized by cutaneous syndactyly of the toes and fingers and abnormalities of the hair and teeth, variably associated with nail dystrophy and palmoplantar keratoderma (PPK). EDSS1 is caused by biallelic mutations in the NECTIN4 gene, encoding the adherens junction component nectin-4. Nine EDSS1 cases have been described to date. We report a 5.5-year-old female child affected with EDSS1 due to the novel homozygous frameshift mutation c.1150delC (p.Gln384ArgfsTer7) in the NECTIN4 gene. The patient presents brittle scalp hair, sparse eyeb

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Martinez, Wanda M., and Patricia G. Spear. "Structural Features of Nectin-2 (HveB) Required for Herpes Simplex Virus Entry." Journal of Virology 75, no. 22 (2001): 11185–95. http://dx.doi.org/10.1128/jvi.75.22.11185-11195.2001.

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ABSTRACT One step in the process of herpes simplex virus (HSV) entry into cells is the binding of viral glycoprotein D (gD) to a cellular receptor. Human nectin-2 (also known as HveB and Prr2), a member of the immunoglobulin (Ig) superfamily, serves as a gD receptor for the entry of HSV-2, variant forms of HSV-1 that have amino acid substitutions at position 25 or 27 of gD (for example, HSV-1/Rid), and porcine pseudorabies virus (PRV). The gD binding region of nectin-2 is believed to be localized to the N-terminal variable-like (V) Ig domain. In order to identify specific amino acid sequences

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Bősze, Szilvia, Ferenc Zsila, Beáta Biri-Kovács, et al. "Tailoring Uptake Efficacy of HSV-1 gD Tailoring Uptake Efficacy of Hsv-1 GD Derived Carrier Peptides." Biomolecules 10, no. 5 (2020): 721. http://dx.doi.org/10.3390/biom10050721.

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Regions of the Herpes simplex virus-1 (HSV-1) glycoprotein D (gD) were chosen to design carrier peptides based on the known tertiary structure of the virus entry receptor complexes. These complexes consist of the following: HSV-1 gD–nectin-1 and HSV-1 gD–herpesvirus entry mediator (HVEM). Three sets of peptides were synthesised with sequences covering the (i) N-terminal HVEM- and nectin-1 binding region -5–42, (ii) the 181–216 medium region containing nectin-1 binding sequences and (iii) the C-terminal nectin-1 binding region 214–255. The carrier candidates were prepared with acetylated and 5(

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Ono, Etsuro, Yukiko Tomioka, Yuki Watanabe, et al. "Comparison of the antiviral potentials among the pseudorabies-resistant transgenes encoding different soluble forms of porcine nectin-1 in transgenic mice." Journal of General Virology 88, no. 10 (2007): 2636–41. http://dx.doi.org/10.1099/vir.0.83080-0.

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Nectin-1 is an alphaherpesvirus receptor that binds to virion glycoprotein D by the first immunoglobulin (Ig)-like domain. The possibility of making animals resistant to pseudorabies virus (PRV) infection has been investigated by generating transgenic mice expressing soluble forms of porcine nectin-1. Previously, transgenic mice were generated that expressed a fusion protein made of the entire ectodomain of nectin-1 fused to the Fc portion of human IgG, or the first Ig-like domain fused to the Fc portion of porcine IgG. Here, the contribution of the second and third Ig-like domains of nectin-1

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Shukla, Deepak, Mauro C. Dal Canto, Cynthia L. Rowe та Patricia G. Spear. "Striking Similarity of Murine Nectin-1α to Human Nectin-1α (HveC) in Sequence and Activity as a Glycoprotein D Receptor for Alphaherpesvirus Entry". Journal of Virology 74, № 24 (2000): 11773–81. http://dx.doi.org/10.1128/jvi.74.24.11773-11781.2000.

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ABSTRACT A cDNA encoding the murine homolog of human nectin-1α (also known as poliovirus receptor-related protein 1 [Prr1] and herpesvirus entry protein C [HveC]) was isolated. The protein encoded by this cDNA proved to be 95% identical in sequence to the human protein and to have similar herpesvirus entry activity. Upon expression of the murine cDNA in hamster cells resistant to alphaherpesvirus entry, the cells became susceptible to the entry of herpes simplex virus types 1 and 2 (HSV-1 and -2), pseudorabies virus, and bovine herpesvirus 1. HSV envelope glycoprotein D (gD), a viral ligand fo

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Andrade, Lucas Ferrari, Mark J. Smyth, and Ludovic Martinet. "DNAM‐1 control of natural killer cells functions through nectin and nectin‐like proteins." Immunology & Cell Biology 92, no. 3 (2013): 237–44. http://dx.doi.org/10.1038/icb.2013.95.

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Inagaki, M. "Roles of cell-adhesion molecules nectin 1 and nectin 3 in ciliary body development." Development 132, no. 7 (2005): 1525–37. http://dx.doi.org/10.1242/dev.01697.

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Cocchi, Francesca, Laura Menotti, Patrice Dubreuil, Marc Lopez, and Gabriella Campadelli-Fiume. "Cell-to-Cell Spread of Wild-Type Herpes Simplex Virus Type 1, but Not of Syncytial Strains, Is Mediated by the Immunoglobulin-Like Receptors That Mediate Virion Entry, Nectin1 (PRR1/HveC/HIgR) and Nectin2 (PRR2/HveB)." Journal of Virology 74, no. 8 (2000): 3909–17. http://dx.doi.org/10.1128/jvi.74.8.3909-3917.2000.

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ABSTRACT The immunoglobulin-like receptors that mediate entry of herpes simplex virus type 1 (HSV-1) into human cells were found to mediate the direct cell-to-cell spread of wild-type virus. The receptors here designated Nectin1α and -δ and Nectin2α were originally designated HIgR, PRR1/HveC, and PRR2α/HveB, respectively. We report the following. (i) Wild-type HSV-1 spreads from cell to cell in J cells expressing nectin1α or nectin1δ but not in parental J cells that are devoid of entry receptors. A monoclonal antibody to nectin1, which blocks entry, also blocked cell-to-cell spread in nectin1-

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Tomiyama, Eisuke, Kazutoshi Fujita, Maria Del Carmen Rodriguez Pena, et al. "Expression of Nectin-4 and PD-L1 in Upper Tract Urothelial Carcinoma." International Journal of Molecular Sciences 21, no. 15 (2020): 5390. http://dx.doi.org/10.3390/ijms21155390.

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Enfortumab vedotin is a novel antibody–drug conjugate targeting Nectin-4, which is highly expressed in urothelial carcinoma. However, the expression status of Nectin-4 in upper tract urothelial carcinoma (UTUC) remains unclear. The relationship between Nectin-4 and Programmed Death Ligand 1 (PD-L1) in UTUC is also ambiguous. We performed immunohistochemical analysis of 99 UTUC tissue microarray to assess the expression of Nectin-4 and PD-L1 in UTUC. Nectin-4-positivity was detected in 65 (65.7%) samples, and PD-L1 was detected in 24 (24.2%) samples. There was no correlation between the express

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Kim, Doo Yeon, Laura A. MacKenzie Ingano та Dora M. Kovacs. "Nectin-1α, an Immunoglobulin-like Receptor Involved in the Formation of Synapses, Is a Substrate for Presenilin/γ-Secretase-like Cleavage". Journal of Biological Chemistry 277, № 51 (2002): 49976–81. http://dx.doi.org/10.1074/jbc.m210179200.

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Nectin-1 is a member of the immunoglobulin superfamily and a Ca2+-independent adherens junction protein involved in synapse formation. Here we show that nectin-1α undergoes intramembrane proteolytic processing analogous to that of the Alzheimer's disease amyloid precursor protein, mediated by a presenilin (PS)-dependent γ-secretase-like activity. 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment of Chinese hamster ovary cells activated a first proteolytic event, resulting in ectodomain shedding of nectin-1α. Subsequent cleavage of the remaining 26-kDa membrane-anchored C-terminal fragment (

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Mollo, Maria Rosaria, Dario Antonini, Karen Mitchell, et al. "p63‐dependent and independent mechanisms of nectin‐1 and nectin‐4 regulation in the epidermis." Experimental Dermatology 24, no. 2 (2015): 114–19. http://dx.doi.org/10.1111/exd.12593.

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Liu, Xiao, Tai An, Dongdong Li, et al. "Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules." Proceedings of the National Academy of Sciences 116, no. 6 (2019): 2068–77. http://dx.doi.org/10.1073/pnas.1810969116.

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Nectin-like (Necl) molecules are Ca2+-independent Ig-like transmembrane cell adhesion molecules that participate in junctions between different cell types. The specific cell–cell adhesions mediated by Necl proteins are important in neural development and have been implicated in neurodegenerative diseases. Here, we present the crystal structure of the mouse Necl-4 full ectodomain and the structure of the heterophilic Necl ectodomain complex formed by the mNecl-4 and mNecl-1 ectodomains. We demonstrate that, while the ectodomain of mNecl-4 is monomeric, it forms a stable heterodimer with Ig1 of

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Uchida, Hiroaki, Waris A. Shah, Ali Ozuer, et al. "Generation of Herpesvirus Entry Mediator (HVEM)-Restricted Herpes Simplex Virus Type 1 Mutant Viruses: Resistance of HVEM-Expressing Cells and Identification of Mutations That Rescue Nectin-1 Recognition." Journal of Virology 83, no. 7 (2009): 2951–61. http://dx.doi.org/10.1128/jvi.01449-08.

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ABSTRACT Both initial infection and cell-to-cell spread by herpes simplex virus type 1 (HSV-1) require the interaction of the viral glycoprotein D (gD) with an entry receptor on the cell surface. The two major HSV entry receptors, herpesvirus entry mediator (HVEM) and nectin-1, mediate infection independently but are coexpressed on a variety of cells. To determine if both receptors are active in these instances, we have established mutant viruses that are selectively impaired for recognition of one or the other receptor. In plaque assays, these viruses showed approximately 1,000-fold selectivi

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Frampton, Arthur R., William F. Goins, Justus B. Cohen, et al. "Equine Herpesvirus 1 Utilizes a Novel Herpesvirus Entry Receptor." Journal of Virology 79, no. 5 (2005): 3169–73. http://dx.doi.org/10.1128/jvi.79.5.3169-3173.2005.

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ABSTRACT The well-described herpesvirus entry receptors HveA (TNFRSF14), HveB (nectin 2), and HveC (nectin 1) have been shown to mediate the entry of alphaherpesviruses. Our findings showed that the alphaherpesvirus equine herpesvirus 1 (EHV-1) efficiently entered and replicated in CHO-K1 cells that lack the entry receptors HveA, HveB, and HveC, demonstrating that EHV-1 utilizes a unique entry receptor. As with other alphaherpesviruses, efficient EHV-1 entry was dependent on glycoprotein D and cell surface glycosaminoglycans.

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Hoffman-Censits, Jean H., Woonyoung Choi, Kara Lombardo, et al. "Expression of nectin-4 in bladder cancer with variant histology." Journal of Clinical Oncology 38, no. 6_suppl (2020): 546. http://dx.doi.org/10.1200/jco.2020.38.6_suppl.546.

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546 Background: The antibody-drug conjugate enfortumab vedotin is poised to change the bladder cancer (BC) treatment landscape by targeting Nectin-4, near ubiquitously expressed in urothelial cancer (UC). Less is known about this and other targets in BC with pure or mixed variant histology (VH). Methods: Immunohistochemistry (IHC) was performed on a Ventana Discovery Autostainer (Roche Diagnostics) using an ultraView DAB detection kit (Roche Diagnostics) and a Nectin-4 polyclonal antibody (1:100 dilution; Abcam, Cambridge, UK). The intensity and extent of Nectin-4 expression was determined by

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Schwertner, Barbara, Georg Lindner, Camila Toledo Toledo Stauner, et al. "Nectin-1 Expression Correlates with the Susceptibility of Malignant Melanoma to Oncolytic Herpes Simplex Virus In Vitro and In Vivo." Cancers 13, no. 12 (2021): 3058. http://dx.doi.org/10.3390/cancers13123058.

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Talimogene laherparepvec (T-VEC), an oncolytic herpes simplex virus, is approved for intralesional injection of unresectable stage IIIB/IVM1a melanoma. However, it is still unclear which parameter(s) predict treatment response or failure. Our study aimed at characterizing surface receptors Nectin-1 and the herpes virus entry mediator (HVEM) in addition to intracellular molecules cyclic GMP-AMP synthase (cGAS) and stimulator of interferon genes (STING) as potential bio-markers for oncolytic virus treatment. In 20 melanoma cell lines, oncolytic activity of T-VEC was correlated with the expressio

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Bottino, Cristina, Roberta Castriconi, Daniela Pende, et al. "Identification of PVR (CD155) and Nectin-2 (CD112) as Cell Surface Ligands for the Human DNAM-1 (CD226) Activating Molecule." Journal of Experimental Medicine 198, no. 4 (2003): 557–67. http://dx.doi.org/10.1084/jem.20030788.

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Human natural killer (NK) cells express a series of activating receptors and coreceptors that are involved in recognition and killing of target cells. In this study, in an attempt to identify the cellular ligands for such triggering surface molecules, mice were immunized with NK-susceptible target cells. On the basis of a functional screening, four mAbs were selected that induced a partial down-regulation of the NK-mediated cytotoxicity against the immunizing target cells. As revealed by biochemical analysis, three of such mAbs recognized molecules of ∼70 kD. The other mAb reacted with two dis

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Yoon, Miri, Anna Zago, Deepak Shukla, and Patricia G. Spear. "Mutations in the N Termini of Herpes Simplex Virus Type 1 and 2 gDs Alter Functional Interactions with the Entry/Fusion Receptors HVEM, Nectin-2, and 3-O-Sulfated Heparan Sulfate but Not with Nectin-1." Journal of Virology 77, no. 17 (2003): 9221–31. http://dx.doi.org/10.1128/jvi.77.17.9221-9231.2003.

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ABSTRACT Multiple cell surface molecules (herpesvirus entry mediator [HVEM], nectin-1, nectin-2, and 3-O-sulfated heparan sulfate) can serve as entry receptors for herpes simplex virus type 1 (HSV-1) or HSV-2 and also as receptors for virus-induced cell fusion. Viral glycoprotein D (gD) is the ligand for these receptors. A previous study showed that HVEM makes contact with HSV-1 gD at regions within amino acids 7 to 15 and 24 to 32 at the N terminus of gD. In the present study, amino acid substitutions and deletions were introduced into the N termini of HSV-1 and HSV-2 gDs to determine the eff

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Vedula, Sri Ram Krishna, Tong Seng Lim, Shi Hui, et al. "Molecular force spectroscopy of homophilic nectin-1 interactions." Biochemical and Biophysical Research Communications 362, no. 4 (2007): 886–92. http://dx.doi.org/10.1016/j.bbrc.2007.08.096.

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Ishino, Ryo, Yumi Kawase, Toshio Kitawaki, et al. "Oncolytic Virus Therapy with HSV-1 for Hematologic Malignancies." Blood 134, Supplement_1 (2019): 3242. http://dx.doi.org/10.1182/blood-2019-127754.

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Background: Oncolytic virus (OV) is an attractive and rapidly developing antitumor therapy. OVs preferentially replicate in tumor cells and exhibit a tumoricidal activity without damaging normal cells. G47Δ is a herpes simplex virus (HSV)-1 genetically engineered to enhance tumor selectivity and immunogenicity. Clinical trials of G47Δ have been conducted for brain and prostate cancers. Anecdotal reports that leukemia and lymphoma shrink following viral infection imply effectiveness of OV therapy against hematological malignancies. Aim: We examined whether G47Δ has the potential for treatment o

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Boles, Kent S., Winfried Barchet, Tom Diacovo, Marina Cella, and Marco Colonna. "The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAM." Blood 106, no. 3 (2005): 779–86. http://dx.doi.org/10.1182/blood-2005-02-0817.

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AbstractThe tumor suppressor in lung cancer-1 (TSLC1) gene is frequently silenced in human lung carcinomas, and its expression suppresses tumorigenesis in nude mice. TSLC1 encodes a cell-surface protein called Necl-2 that belongs to the Nectin and Nectin-like (Necl) family of molecules. Necl-2 mediates epithelial cell junctions by homotypic contacts and/or heterotypic interactions with other Nectins and Necls. Thus, it inhibits tumorigenesis by ensuring that epithelial cells grow in organized layers. Here, we demonstrate that natural killer (NK) cells and CD8+ T cells recognize Necl-2 through

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ZELANO, J., W. WALLQUIST, N. HAILER, and S. CULLHEIM. "Expression of nectin-1, nectin-3, N-cadherin, and NCAM in spinal motoneurons after sciatic nerve transection." Experimental Neurology 201, no. 2 (2006): 461–69. http://dx.doi.org/10.1016/j.expneurol.2006.04.026.

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Knebel-Mörsdorf, Dagmar. "Nectin-1 and HVEM: cellular receptors for HSV-1 in skin." Oncotarget 7, no. 15 (2016): 19087–88. http://dx.doi.org/10.18632/oncotarget.8340.

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Connolly, Sarah A., Daniel J. Landsburg, Andrea Carfi, et al. "Potential Nectin-1 Binding Site on Herpes Simplex Virus Glycoprotein D." Journal of Virology 79, no. 2 (2005): 1282–95. http://dx.doi.org/10.1128/jvi.79.2.1282-1295.2005.

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ABSTRACT Four glycoproteins (gD, gB, gH, and gL) are essential for herpes simplex virus (HSV) entry into cells. An early step of fusion requires gD to bind one of several receptors, such as nectin-1 or herpesvirus entry mediator (HVEM). We hypothesize that a conformational change in gD occurs upon receptor binding that triggers the other glycoproteins to mediate fusion. Comparison of the crystal structures of gD alone and gD bound to HVEM reveals that upon HVEM binding, the gD N terminus transitions from a flexible stretch of residues to a hairpin loop. To address the contribution of this tran

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Narita, Hirotaka, Yasunori Yamamoto, Mamoru Suzuki, et al. "Crystal Structure of the cis-Dimer of Nectin-1." Journal of Biological Chemistry 286, no. 14 (2011): 12659–69. http://dx.doi.org/10.1074/jbc.m110.197368.

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Cocchi, Francesca, Laura Menotti, Valentina Di Ninni, Marc Lopez, and Gabriella 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." Journal of Virology 78, no. 9 (2004): 4720–29. http://dx.doi.org/10.1128/jvi.78.9.4720-4729.2004.

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ABSTRACT The herpes simplex virus type 1(JMP) [HSV-1(JMP)] mutant was selected for its ability to grow and form plaques in receptor-negative J cells. It enters J cells through a novel gD-dependent pathway, independent of all known HSV receptors, nectin1, nectin2, and HveA. Evidence that the pathway is dependent on a nectin3 binding site on HSV-1(JMP) and requires three mutations in gD rests on the following. We derived monoclonal antibodies to nectin3 and show that J cells express nectin3. HSV-1(JMP) entry and cell-to-cell spread were inhibited by soluble nectin3-Fc, demonstrating that virions

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Reymond, Nicolas, Anne-Marie Imbert, Elisabeth Devilard, et al. "DNAM-1 and PVR Regulate Monocyte Migration through Endothelial Junctions." Journal of Experimental Medicine 199, no. 10 (2004): 1331–41. http://dx.doi.org/10.1084/jem.20032206.

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DNAX accessory molecule 1 (DNAM-1; CD226) is a transmembrane glycoprotein involved in T cell and natural killer (NK) cell cytotoxicity. We demonstrated recently that DNAM-1 triggers NK cell–mediated killing of tumor cells upon engagement by its two ligands, poliovirus receptor (PVR; CD155) and Nectin-2 (CD112). In the present paper, we show that PVR and Nectin-2 are expressed at cell junctions on primary vascular endothelial cells. Moreover, the specific binding of a soluble DNAM-1–Fc molecule was detected at endothelial junctions. This binding was almost completely abrogated by anti-PVR monoc

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Struyf, Frank, Christine M. Posavad, Els Keyaerts, Marc Van Ranst, Lawrence Corey, and Patricia G. Spear. "Search for Polymorphisms in the Genes for Herpesvirus Entry Mediator, Nectin‐1, and Nectin‐2 in Immune Seronegative Individuals." Journal of Infectious Diseases 185, no. 1 (2002): 36–44. http://dx.doi.org/10.1086/338116.

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Kwon, Heechung, Qing Bai, Hyun-Jung Baek, et al. "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." Journal of Virology 80, no. 1 (2006): 138–48. http://dx.doi.org/10.1128/jvi.80.1.138-148.2006.

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ABSTRACT Interaction of herpes simplex virus (HSV) glycoprotein D (gD) with specific cellular receptors is essential for HSV infection of susceptible cells. Virus mutants that lack gD can bind to the cell surface (attachment) but do not enter, implying that interaction of gD with its receptor(s) initiates the postattachment (entry) phase of HSV infection. In this report, we have studied HSV entry in the presence of the gD-binding variable (V) domain of the common gD receptor nectin-1/HveC to determine whether cell association of the gD receptor is required for HSV infection. In the presence of

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