메뉴 건너뛰기




Volumn 88, Issue 24, 2014, Pages 14161-14171

Different roles of the three loops forming the adhesive interface of nectin-4 in measles virus binding and cell entry, nectin-4 homodimerization, and heterodimerization with nectin-1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN; NECTIN 1; NECTIN 4 PROTEIN; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ; VIRUS PROTEIN; CELL ADHESION MOLECULE; HEMAGGLUTININ PROTEIN G, MEASLES VIRUS; LNIR PROTEIN, HUMAN; NECTINS; VIRUS RECEPTOR;

EID: 84911478242     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02379-14     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 84974736054 scopus 로고    scopus 로고
    • Measles virus
    • 6th ed, Wolters Kluwer, Lippincott Williams & Wilkins, Philadelphia, PA.
    • Griffin DE. 2013. Measles virus, p 1042-1069. Fields virology, 6th ed, vol 1. Wolters Kluwer, Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2013) Fields virology , vol.1 , pp. 1042-1069
    • Griffin, D.E.1
  • 2
    • 84860170196 scopus 로고    scopus 로고
    • Public health. Europe's embarrassing problem
    • Kupferschmidt K. 2012. Public health. Europe's embarrassing problem. Science 336:406-407. http://dx.doi.org/10.1126/science.336.6080.406.
    • (2012) Science , vol.336 , pp. 406-407
    • Kupferschmidt, K.1
  • 3
    • 84893312377 scopus 로고    scopus 로고
    • Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses
    • Mateo M, Navaratnarajah CK, Cattaneo R. 2014. Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses. Curr. Opin. Virol. 5:16-23. http://dx.doi.org/10.1016/j.coviro.2014.01.004.
    • (2014) Curr. Opin. Virol. , vol.5 , pp. 16-23
    • Mateo, M.1    Navaratnarajah, C.K.2    Cattaneo, R.3
  • 4
    • 0034710650 scopus 로고    scopus 로고
    • SLAM (CDw150) is a cellular receptor for measles virus
    • Tatsuo H, Ono N, Tanaka K, Yanagi Y. 2000. SLAM (CDw150) is a cellular receptor for measles virus. Nature 406:893-897. http://dx.doi.org/10.1038/35022579.
    • (2000) Nature , vol.406 , pp. 893-897
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 6
    • 80052315535 scopus 로고    scopus 로고
    • Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus
    • Noyce RS, Bondre DG, Ha MN, Lin LT, Sisson G, Tsao MS, Richardson CD. 2011. Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus. PLoS Pathog. 7:e1002240. http://dx.doi.org/10.1371/journal.ppat.1002240.
    • (2011) PLoS Pathog. , vol.7
    • Noyce, R.S.1    Bondre, D.G.2    Ha, M.N.3    Lin, L.T.4    Sisson, G.5    Tsao, M.S.6    Richardson, C.D.7
  • 7
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • Dorig RE, Marcil A, Chopra A, Richardson CD. 1993. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75:295-305.
    • (1993) Cell , vol.75 , pp. 295-305
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 11
    • 45549105566 scopus 로고    scopus 로고
    • Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150)
    • Navaratnarajah CK, Vongpunsawad S, Oezguen N, Stehle T, Braun W, Hashiguchi T, Maenaka K, Yanagi Y, Cattaneo R. 2008. Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150). J. Biol. Chem. 283: 11763-11771. http://dx.doi.org/10.1074/jbc.M800896200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11763-11771
    • Navaratnarajah, C.K.1    Vongpunsawad, S.2    Oezguen, N.3    Stehle, T.4    Braun, W.5    Hashiguchi, T.6    Maenaka, K.7    Yanagi, Y.8    Cattaneo, R.9
  • 12
    • 84883328898 scopus 로고    scopus 로고
    • Envelope protein dynamics in paramyxovirus entry
    • Plattet P, Plemper RK. 2013. Envelope protein dynamics in paramyxovirus entry. mBio 4(4):e00413-13. http://dx.doi.org/10.1128/mBio.00413-13.
    • (2013) mBio , vol.4 , Issue.4
    • Plattet, P.1    Plemper, R.K.2
  • 14
    • 77449145697 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to the CD46 receptor
    • Santiago C, Celma ML, Stehle T, Casasnovas JM. 2010. Structure of the measles virus hemagglutinin bound to the CD46 receptor. Nat. Struct. Mol. Biol. 17:124-129. http://dx.doi.org/10.1038/nsmb.1726.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 124-129
    • Santiago, C.1    Celma, M.L.2    Stehle, T.3    Casasnovas, J.M.4
  • 16
    • 84881264159 scopus 로고    scopus 로고
    • The measles virus hemagglutinin beta-propeller head beta4-beta5 hydrophobic groove governs functional interactions with nectin-4 and CD46 but not those with the signaling lymphocytic activation molecule
    • Mateo M, Navaratnarajah CK, Syed S, Cattaneo R. 2013. The measles virus hemagglutinin beta-propeller head beta4-beta5 hydrophobic groove governs functional interactions with nectin-4 and CD46 but not those with the signaling lymphocytic activation molecule. J. Virol. 87:9208-9216. http://dx.doi.org/10.1128/JVI.01210-13.
    • (2013) J. Virol. , vol.87 , pp. 9208-9216
    • Mateo, M.1    Navaratnarajah, C.K.2    Syed, S.3    Cattaneo, R.4
  • 17
    • 55849135745 scopus 로고    scopus 로고
    • The immunoglobulin-like cell adhesion molecule nectin and its associated protein afadin
    • Takai Y, Ikeda W, Ogita H, Rikitake Y. 2008. The immunoglobulin-like cell adhesion molecule nectin and its associated protein afadin. Annu. Rev. Cell Dev. Biol. 24:309-342. http://dx.doi.org/10.1146/annurev.cellbio.24.110707.175339.
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 309-342
    • Takai, Y.1    Ikeda, W.2    Ogita, H.3    Rikitake, Y.4
  • 18
    • 0037232646 scopus 로고    scopus 로고
    • Nectin and afadin: novel organizers of intercellular junctions
    • Takai Y, Nakanishi H. 2003. Nectin and afadin: novel organizers of intercellular junctions. J. Cell Sci. 116:17-27. http://dx.doi.org/10.1242/jcs.00167.
    • (2003) J. Cell Sci. , vol.116 , pp. 17-27
    • Takai, Y.1    Nakanishi, H.2
  • 19
    • 84869115765 scopus 로고    scopus 로고
    • The role of nectins in different types of cell-cell adhesion
    • Rikitake Y, Mandai K, Takai Y. 2012. The role of nectins in different types of cell-cell adhesion. J. Cell Sci. 125:3713-3722. http://dx.doi.org/10.1242/jcs.099572.
    • (2012) J. Cell Sci. , vol.125 , pp. 3713-3722
    • Rikitake, Y.1    Mandai, K.2    Takai, Y.3
  • 21
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. 1994. The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol. 242:309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 22
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y, Chothia C. 1994. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238:528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 24
    • 84866274323 scopus 로고    scopus 로고
    • Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion
    • Samanta D, Ramagopal UA, Rubinstein R, Vigdorovich V, Nathenson SG, Almo SC. 2012. Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion. Proc. Natl. Acad. Sci. U. S. A. 109:14836-14840. http://dx.doi.org/10.1073/pnas.1212912109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 14836-14840
    • Samanta, D.1    Ramagopal, U.A.2    Rubinstein, R.3    Vigdorovich, V.4    Nathenson, S.G.5    Almo, S.C.6
  • 26
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280:1618-1620.
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 27
    • 0031820802 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry
    • Krummenacher C, Nicola AV, Whitbeck JC, Lou H, Hou W, Lambris JD, Geraghty RJ, Spear PG, Cohen GH, Eisenberg RJ. 1998. Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry. J. Virol. 72:7064-7074.
    • (1998) J. Virol. , vol.72 , pp. 7064-7074
    • Krummenacher, C.1    Nicola, A.V.2    Whitbeck, J.C.3    Lou, H.4    Hou, W.5    Lambris, J.D.6    Geraghty, R.J.7    Spear, P.G.8    Cohen, G.H.9    Eisenberg, R.J.10
  • 28
    • 0024519677 scopus 로고
    • Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn CL, Wimmer E, Racaniello VR. 1989. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 56:855-865.
    • (1989) Cell , vol.56 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 30
    • 84455194239 scopus 로고    scopus 로고
    • Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion
    • Zhang N, Yan J, Lu G, Guo Z, Fan Z, Wang J, Shi Y, Qi J, Gao GF. 2011. Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion. Nat. Commun. 2:577. http://dx.doi.org/10.1038/ncomms1571.
    • (2011) Nat. Commun. , vol.2 , pp. 577
    • Zhang, N.1    Yan, J.2    Lu, G.3    Guo, Z.4    Fan, Z.5    Wang, J.6    Shi, Y.7    Qi, J.8    Gao, G.F.9
  • 31
    • 0036892864 scopus 로고    scopus 로고
    • 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
    • Struyf F, Martinez WM, Spear PG. 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. http://dx.doi.org/10.1128/JVI.76.24.12940-12950.2002.
    • (2002) J. Virol. , vol.76 , pp. 12940-12950
    • Struyf, F.1    Martinez, W.M.2    Spear, P.G.3
  • 33
    • 0037178837 scopus 로고    scopus 로고
    • 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
    • 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. http://dx.doi.org/10.1074/jbc.M203228200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27006-27013
    • Fabre, S.1    Reymond, N.2    Cocchi, F.3    Menotti, L.4    Dubreuil, P.5    Campadelli-Fiume, G.6    Lopez, M.7
  • 34
    • 0035900768 scopus 로고    scopus 로고
    • Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction
    • 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. http://dx.doi.org/10.1074/jbc.M103810200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43205-43215
    • Reymond, N.1    Fabre, S.2    Lecocq, E.3    Adelaide, J.4    Dubreuil, P.5    Lopez, M.6
  • 37
    • 46749117203 scopus 로고    scopus 로고
    • Measles virus blind to its epithelial cell receptor remains virulent in rhesus monkeys but cannot cross the airway epithelium and is not shed
    • Leonard VH, Sinn PL, Hodge G, Miest T, Devaux P, Oezguen N, Braun W, McCray PB, Jr, McChesney MB, Cattaneo R. 2008. Measles virus blind to its epithelial cell receptor remains virulent in rhesus monkeys but cannot cross the airway epithelium and is not shed. J. Clin. Invest. 118: 2448-2458. http://dx.doi.org/10.1172/JCI35454.
    • (2008) J. Clin. Invest. , vol.118 , pp. 2448-2458
    • Leonard, V.H.1    Sinn, P.L.2    Hodge, G.3    Miest, T.4    Devaux, P.5    Oezguen, N.6    Braun, W.7    McCray Jr., P.B.8    McChesney, M.B.9    Cattaneo, R.10
  • 39
    • 0031797729 scopus 로고    scopus 로고
    • The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells
    • Cocchi F, Menotti L, Mirandola P, Lopez M, Campadelli-Fiume G. 1998. The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. J. Virol. 72:9992-10002.
    • (1998) J. Virol. , vol.72 , pp. 9992-10002
    • Cocchi, F.1    Menotti, L.2    Mirandola, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 40
    • 84873750119 scopus 로고    scopus 로고
    • Neutralization capacity of measles virus H protein specific IgG determines the balance between antibody-enhanced infectivity and protection in microglial cells
    • Iankov ID, Penheiter AR, Griesmann GE, Carlson SK, Federspiel MJ, Galanis E. 2013. Neutralization capacity of measles virus H protein specific IgG determines the balance between antibody-enhanced infectivity and protection in microglial cells. Virus Res. 172:15-23. http://dx.doi.org/10.1016/j.virusres.2012.12.002.
    • (2013) Virus Res. , vol.172 , pp. 15-23
    • Iankov, I.D.1    Penheiter, A.R.2    Griesmann, G.E.3    Carlson, S.K.4    Federspiel, M.J.5    Galanis, E.6
  • 41
  • 42
    • 73549084311 scopus 로고    scopus 로고
    • Immunoglobulin superfamily virus receptors and the evolution of adaptive immunity
    • Dermody TS, Kirchner E, Guglielmi KM, Stehle T. 2009. Immunoglobulin superfamily virus receptors and the evolution of adaptive immunity. PLoS Pathog. 5:e1000481. http://dx.doi.org/10.1371/journal.ppat.1000481.
    • (2009) PLoS Pathog. , vol.5
    • Dermody, T.S.1    Kirchner, E.2    Guglielmi, K.M.3    Stehle, T.4
  • 46
    • 0027475337 scopus 로고
    • Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59
    • Dveksler GS, Dieffenbach CW, Cardellichio CB, McCuaig K, Pensiero MN, Jiang GS, Beauchemin N, Holmes KV. 1993. Several members of the mouse carcinoembryonic antigen-related glycoprotein family are functional receptors for the coronavirus mouse hepatitis virus-A59. J. Virol. 67:1-8.
    • (1993) J. Virol. , vol.67 , pp. 1-8
    • Dveksler, G.S.1    Dieffenbach, C.W.2    Cardellichio, C.B.3    McCuaig, K.4    Pensiero, M.N.5    Jiang, G.S.6    Beauchemin, N.7    Holmes, K.V.8
  • 47
    • 0026095354 scopus 로고
    • Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins
    • Williams RK, Jiang GS, Holmes KV. 1991. Receptor for mouse hepatitis virus is a member of the carcinoembryonic antigen family of glycoproteins. Proc. Natl. Acad. Sci. U. S. A. 88:5533-5536.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5533-5536
    • Williams, R.K.1    Jiang, G.S.2    Holmes, K.V.3
  • 48
    • 84896827184 scopus 로고    scopus 로고
    • The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cellto- cell spread
    • Delpeut S, Noyce RS, Richardson CD. 2014. The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cellto- cell spread. Virology 454-455:109-117. http://dx.doi.org/10.1016/j .virol.2014.02.014.
    • (2014) Virology , vol.454-455 , pp. 109-117
    • Delpeut, S.1    Noyce, R.S.2    Richardson, C.D.3
  • 49
    • 84859468877 scopus 로고    scopus 로고
    • Structure of TIGIT immunoreceptor bound to poliovirus receptor reveals a cell-cell adhesion and signaling mechanism that requires cis-trans receptor clustering
    • Stengel KF, Harden-Bowles K, Yu X, Rouge L, Yin J, Comps-Agrar L, Wiesmann C, Bazan JF, Eaton DL, Grogan JL. 2012. Structure of TIGIT immunoreceptor bound to poliovirus receptor reveals a cell-cell adhesion and signaling mechanism that requires cis-trans receptor clustering. Proc. Natl. Acad. Sci. U. S. A. 109:5399-5404. http://dx.doi.org/10.1073/pnas .1120606109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5399-5404
    • Stengel, K.F.1    Harden-Bowles, K.2    Yu, X.3    Rouge, L.4    Yin, J.5    Comps-Agrar, L.6    Wiesmann, C.7    Bazan, J.F.8    Eaton, D.L.9    Grogan, J.L.10
  • 50
    • 0021066630 scopus 로고
    • Inhibition of measles virus budding by phenothiazines
    • Bohn W, Rutter G, Hohenberg H, Mannweiler K. 1983. Inhibition of measles virus budding by phenothiazines. Virology 130:44-55.
    • (1983) Virology , vol.130 , pp. 44-55
    • Bohn, W.1    Rutter, G.2    Hohenberg, H.3    Mannweiler, K.4
  • 51
    • 0031907095 scopus 로고    scopus 로고
    • Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence
    • Cathomen T, Naim HY, Cattaneo R. 1998. Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence. J. Virol. 72:1224-1234.
    • (1998) J. Virol. , vol.72 , pp. 1224-1234
    • Cathomen, T.1    Naim, H.Y.2    Cattaneo, R.3
  • 52
    • 0018073027 scopus 로고
    • Electron microscopic study of measles virus infection: cell fusion and hemadsorption
    • Rentier B, Hooghe-Peters EL, Dubois-Dalcq M. 1978. Electron microscopic study of measles virus infection: cell fusion and hemadsorption. J. Virol. 28:567-577.
    • (1978) J. Virol. , vol.28 , pp. 567-577
    • Rentier, B.1    Hooghe-Peters, E.L.2    Dubois-Dalcq, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.