메뉴 건너뛰기




Volumn 162, Issue 5, 2015, Pages 1090-1100

Rational Design of an Epstein-Barr Virus Vaccine Targeting the Receptor-Binding Site

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT RECEPTOR; COMPLEMENT RECEPTOR 2; EPSTEIN BARR VIRUS VACCINE; GLYCOPROTEIN 350 220 D 123 ENCAPSULIN; GLYCOPROTEIN 350 220 D 123 FERRITIN; GLYCOPROTEIN 350 220 ECTODOMAIN VACCINE; GLYCOPROTEIN 350 ANTIBODY; NANOPARTICLE; NEUTRALIZING ANTIBODY; PROTEIN ANTIBODY; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS LIKE PARTICLE VACCINE; COMPLEMENT COMPONENT C3D RECEPTOR; HERPES VACCINE;

EID: 84940461031     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2015.07.043     Document Type: Article
Times cited : (267)

References (58)
  • 3
    • 77957585573 scopus 로고    scopus 로고
    • Cryo-EM of macromolecular assemblies at near-atomic resolution
    • M.L. Baker, J. Zhang, S.J. Ludtke, and W. Chiu Cryo-EM of macromolecular assemblies at near-atomic resolution Nat. Protoc. 5 2010 1697 1708
    • (2010) Nat. Protoc. , vol.5 , pp. 1697-1708
    • Baker, M.L.1    Zhang, J.2    Ludtke, S.J.3    Chiu, W.4
  • 4
    • 0029021814 scopus 로고
    • Selection of recombinant vaccinia viruses on the basis of plaque formation
    • R. Blasco, and B. Moss Selection of recombinant vaccinia viruses on the basis of plaque formation Gene 158 1995 157 162
    • (1995) Gene , vol.158 , pp. 157-162
    • Blasco, R.1    Moss, B.2
  • 5
    • 34548161338 scopus 로고    scopus 로고
    • Characterization of chimpanzee/human monoclonal antibodies to vaccinia virus A33 glycoprotein and its variola virus homolog in vitro and in a vaccinia virus mouse protection model
    • Z. Chen, P. Earl, J. Americo, I. Damon, S.K. Smith, F. Yu, A. Sebrell, S. Emerson, G. Cohen, R.J. Eisenberg, and et al. Characterization of chimpanzee/human monoclonal antibodies to vaccinia virus A33 glycoprotein and its variola virus homolog in vitro and in a vaccinia virus mouse protection model J. Virol. 81 2007 8989 8995
    • (2007) J. Virol. , vol.81 , pp. 8989-8995
    • Chen, Z.1    Earl, P.2    Americo, J.3    Damon, I.4    Smith, S.K.5    Yu, F.6    Sebrell, A.7    Emerson, S.8    Cohen, G.9    Eisenberg, R.J.10
  • 6
  • 8
    • 67349125435 scopus 로고    scopus 로고
    • The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake
    • K.J. Cho, H.J. Shin, J.H. Lee, K.J. Kim, S.S. Park, Y. Lee, C. Lee, S.S. Park, and K.H. Kim The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake J. Mol. Biol. 390 2009 83 98
    • (2009) J. Mol. Biol. , vol.390 , pp. 83-98
    • Cho, K.J.1    Shin, H.J.2    Lee, J.H.3    Kim, K.J.4    Park, S.S.5    Lee, Y.6    Lee, C.7    Park, S.S.8    Kim, K.H.9
  • 9
    • 80455164859 scopus 로고    scopus 로고
    • Epstein-Barr virus: An important vaccine target for cancer prevention
    • J.I. Cohen, A.S. Fauci, H. Varmus, and G.J. Nabel Epstein-Barr virus: an important vaccine target for cancer prevention Sci. Transl. Med. 3 2011 107fs7
    • (2011) Sci. Transl. Med. , vol.3 , pp. 107fs7
    • Cohen, J.I.1    Fauci, A.S.2    Varmus, H.3    Nabel, G.J.4
  • 10
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: A structural view of the herpesvirus entry machinery
    • S.A. Connolly, J.O. Jackson, T.S. Jardetzky, and R. Longnecker Fusing structure and function: a structural view of the herpesvirus entry machinery Nat. Rev. Microbiol. 9 2011 369 381
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 13
    • 49749222804 scopus 로고
    • Virus Particles in Cultured Lymphoblasts from Burkitt's Lymphoma
    • M.A. Epstein, B.G. Achong, and Y.M. Barr Virus Particles in Cultured Lymphoblasts from Burkitt's Lymphoma Lancet 1 1964 702 703
    • (1964) Lancet , vol.1 , pp. 702-703
    • Epstein, M.A.1    Achong, B.G.2    Barr, Y.M.3
  • 14
    • 0022430250 scopus 로고
    • Protection of cottontop tamarins against Epstein-Barr virus-induced malignant lymphoma by a prototype subunit vaccine
    • M.A. Epstein, A.J. Morgan, S. Finerty, B.J. Randle, and J.K. Kirkwood Protection of cottontop tamarins against Epstein-Barr virus-induced malignant lymphoma by a prototype subunit vaccine Nature 318 1985 287 289
    • (1985) Nature , vol.318 , pp. 287-289
    • Epstein, M.A.1    Morgan, A.J.2    Finerty, S.3    Randle, B.J.4    Kirkwood, J.K.5
  • 16
    • 84883421928 scopus 로고    scopus 로고
    • Elicitation of HIV-1-neutralizing antibodies against the CD4-binding site
    • I.S. Georgiev, M. Gordon Joyce, T. Zhou, and P.D. Kwong Elicitation of HIV-1-neutralizing antibodies against the CD4-binding site Curr. Opin. HIV AIDS 8 2013 382 392
    • (2013) Curr. Opin. HIV AIDS , vol.8 , pp. 382-392
    • Georgiev, I.S.1    Gordon Joyce, M.2    Zhou, T.3    Kwong, P.D.4
  • 17
    • 0029188184 scopus 로고
    • First EBV vaccine trial in humans using recombinant vaccinia virus expressing the major membrane antigen
    • S.Y. Gu, T.M. Huang, L. Ruan, Y.H. Miao, H. Lu, C.M. Chu, M. Motz, and H. Wolf First EBV vaccine trial in humans using recombinant vaccinia virus expressing the major membrane antigen Dev. Biol. Stand. 84 1995 171 177
    • (1995) Dev. Biol. Stand. , vol.84 , pp. 171-177
    • Gu, S.Y.1    Huang, T.M.2    Ruan, L.3    Miao, Y.H.4    Lu, H.5    Chu, C.M.6    Motz, M.7    Wolf, H.8
  • 18
    • 0019223713 scopus 로고
    • Monoclonal antibody against a 250,000-dalton glycoprotein of Epstein-Barr virus identifies a membrane antigen and a neutralizing antigen
    • G.J. Hoffman, S.G. Lazarowitz, and S.D. Hayward Monoclonal antibody against a 250,000-dalton glycoprotein of Epstein-Barr virus identifies a membrane antigen and a neutralizing antigen Proc. Natl. Acad. Sci. USA 77 1980 2979 2983
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2979-2983
    • Hoffman, G.J.1    Lazarowitz, S.G.2    Hayward, S.D.3
  • 19
    • 84874061841 scopus 로고    scopus 로고
    • Re-engineering protein interfaces yields copper-inducible ferritin cage assembly
    • D.J. Huard, K.M. Kane, and F.A. Tezcan Re-engineering protein interfaces yields copper-inducible ferritin cage assembly Nat. Chem. Biol. 9 2013 169 176
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 169-176
    • Huard, D.J.1    Kane, K.M.2    Tezcan, F.A.3
  • 20
    • 34547110512 scopus 로고    scopus 로고
    • Epstein-Barr virus entry
    • L.M. Hutt-Fletcher Epstein-Barr virus entry J. Virol. 81 2007 7825 7832
    • (2007) J. Virol. , vol.81 , pp. 7825-7832
    • Hutt-Fletcher, L.M.1
  • 21
    • 84886287251 scopus 로고    scopus 로고
    • Engineering synthetic vaccines using cues from natural immunity
    • D.J. Irvine, M.A. Swartz, and G.L. Szeto Engineering synthetic vaccines using cues from natural immunity Nat. Mater. 12 2013 978 990
    • (2013) Nat. Mater. , vol.12 , pp. 978-990
    • Irvine, D.J.1    Swartz, M.A.2    Szeto, G.L.3
  • 22
    • 34547828802 scopus 로고    scopus 로고
    • Production of apoferritin-based bioinorganic hybrid nanoparticles by bacterial fermentation followed by self-assembly
    • A. Jääskeläinen, R.R. Harinen, U. Lamminmäki, T. Korpimäki, L.J. Pelliniemi, T. Soukka, and M. Virta Production of apoferritin-based bioinorganic hybrid nanoparticles by bacterial fermentation followed by self-assembly Small 3 2007 1362 1367
    • (2007) Small , vol.3 , pp. 1362-1367
    • Jääskeläinen, A.1    Harinen, R.R.2    Lamminmäki, U.3    Korpimäki, T.4    Pelliniemi, L.J.5    Soukka, T.6    Virta, M.7
  • 24
    • 84873855312 scopus 로고    scopus 로고
    • Outer domain of HIV-1 gp120: Antigenic optimization, structural malleability, and crystal structure with antibody VRC-PG04
    • M.G. Joyce, M. Kanekiyo, L. Xu, C. Biertümpfel, J.C. Boyington, S. Moquin, W. Shi, X. Wu, Y. Yang, Z.Y. Yang, and et al. Outer domain of HIV-1 gp120: antigenic optimization, structural malleability, and crystal structure with antibody VRC-PG04 J. Virol. 87 2013 2294 2306
    • (2013) J. Virol. , vol.87 , pp. 2294-2306
    • Joyce, M.G.1    Kanekiyo, M.2    Xu, L.3    Biertümpfel, C.4    Boyington, J.C.5    Moquin, S.6    Shi, W.7    Wu, X.8    Yang, Y.9    Yang, Z.Y.10
  • 25
    • 84867427047 scopus 로고    scopus 로고
    • Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA
    • J.P. Julien, P.S. Lee, and I.A. Wilson Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA Immunol. Rev. 250 2012 180 198
    • (2012) Immunol. Rev. , vol.250 , pp. 180-198
    • Julien, J.P.1    Lee, P.S.2    Wilson, I.A.3
  • 28
    • 84878472445 scopus 로고    scopus 로고
    • Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape
    • T. Krey, A. Meola, Z.Y. Keck, L. Damier-Piolle, S.K. Foung, and F.A. Rey Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape PLoS Pathog. 9 2013 e1003364
    • (2013) PLoS Pathog. , vol.9 , pp. e1003364
    • Krey, T.1    Meola, A.2    Keck, Z.Y.3    Damier-Piolle, L.4    Foung, S.K.5    Rey, F.A.6
  • 29
    • 84867641531 scopus 로고    scopus 로고
    • Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
    • P.S. Lee, R. Yoshida, D.C. Ekiert, N. Sakai, Y. Suzuki, A. Takada, and I.A. Wilson Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity Proc. Natl. Acad. Sci. USA 109 2012 17040 17045
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 17040-17045
    • Lee, P.S.1    Yoshida, R.2    Ekiert, D.C.3    Sakai, N.4    Suzuki, Y.5    Takada, A.6    Wilson, I.A.7
  • 31
    • 33746312043 scopus 로고    scopus 로고
    • Ferritin nanoparticle technology. A new platform for antigen presentation and vaccine development
    • C.Q. Li, E. Soistman, and D.C. Carter Ferritin nanoparticle technology. A new platform for antigen presentation and vaccine development Ind. Biotechnol. 2 2006 143 147
    • (2006) Ind. Biotechnol. , vol.2 , pp. 143-147
    • Li, C.Q.1    Soistman, E.2    Carter, D.C.3
  • 33
    • 0021357898 scopus 로고
    • A sensitive enzyme-linked immunosorbent assay (ELISA) against the major EBV-associated antigens. I. Correlation between ELISA and immunofluorescence titers using purified antigens
    • J. Luka, R.C. Chase, and G.R. Pearson A sensitive enzyme-linked immunosorbent assay (ELISA) against the major EBV-associated antigens. I. Correlation between ELISA and immunofluorescence titers using purified antigens J. Immunol. Methods 67 1984 145 156
    • (1984) J. Immunol. Methods , vol.67 , pp. 145-156
    • Luka, J.1    Chase, R.C.2    Pearson, G.R.3
  • 35
    • 84877015262 scopus 로고    scopus 로고
    • Mid Staffordshire inquiry. Too long, too late but Francis can still help make the NHS better
    • A. McLellan Mid Staffordshire inquiry. Too long, too late but Francis can still help make the NHS better Health Serv. J. 123 2013 3
    • (2013) Health Serv. J. , vol.123 , pp. 3
    • McLellan, A.1
  • 36
    • 0027126202 scopus 로고
    • Magnetoferritin: In vitro synthesis of a novel magnetic protein
    • F.C. Meldrum, B.R. Heywood, and S. Mann Magnetoferritin: in vitro synthesis of a novel magnetic protein Science 257 1992 522 523
    • (1992) Science , vol.257 , pp. 522-523
    • Meldrum, F.C.1    Heywood, B.R.2    Mann, S.3
  • 37
  • 40
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Y. Okuno, Y. Isegawa, F. Sasao, and S. Ueda A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains J. Virol. 67 1993 2552 2558
    • (1993) J. Virol. , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 41
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with x-ray crystallographic structures
    • M.G. Rossmann, R. Bernal, and S.V. Pletnev Combining electron microscopic with x-ray crystallographic structures J. Struct. Biol. 136 2001 190 200
    • (2001) J. Struct. Biol. , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 42
    • 68549139880 scopus 로고    scopus 로고
    • Human antibody titers to Epstein-Barr Virus (EBV) gp350 correlate with neutralization of infectivity better than antibody titers to EBV gp42 using a rapid flow cytometry-based EBV neutralization assay
    • J. Sashihara, P.D. Burbelo, B. Savoldo, T.C. Pierson, and J.I. Cohen Human antibody titers to Epstein-Barr Virus (EBV) gp350 correlate with neutralization of infectivity better than antibody titers to EBV gp42 using a rapid flow cytometry-based EBV neutralization assay Virology 391 2009 249 256
    • (2009) Virology , vol.391 , pp. 249-256
    • Sashihara, J.1    Burbelo, P.D.2    Savoldo, B.3    Pierson, T.C.4    Cohen, J.I.5
  • 43
    • 80055066029 scopus 로고    scopus 로고
    • Soluble rhesus lymphocryptovirus gp350 protects against infection and reduces viral loads in animals that become infected with virus after challenge
    • J. Sashihara, Y. Hoshino, J.J. Bowman, T. Krogmann, P.D. Burbelo, V.M. Coffield, K. Kamrud, and J.I. Cohen Soluble rhesus lymphocryptovirus gp350 protects against infection and reduces viral loads in animals that become infected with virus after challenge PLoS Pathog. 7 2011 e1002308
    • (2011) PLoS Pathog. , vol.7 , pp. e1002308
    • Sashihara, J.1    Hoshino, Y.2    Bowman, J.J.3    Krogmann, T.4    Burbelo, P.D.5    Coffield, V.M.6    Kamrud, K.7    Cohen, J.I.8
  • 45
    • 39149121505 scopus 로고    scopus 로고
    • Recombinant gp350 vaccine for infectious mononucleosis: A phase 2, randomized, double-blind, placebo-controlled trial to evaluate the safety, immunogenicity, and efficacy of an Epstein-Barr virus vaccine in healthy young adults
    • E.M. Sokal, K. Hoppenbrouwers, C. Vandermeulen, M. Moutschen, P. Léonard, A. Moreels, M. Haumont, A. Bollen, F. Smets, and M. Denis Recombinant gp350 vaccine for infectious mononucleosis: a phase 2, randomized, double-blind, placebo-controlled trial to evaluate the safety, immunogenicity, and efficacy of an Epstein-Barr virus vaccine in healthy young adults J. Infect. Dis. 196 2007 1749 1753
    • (2007) J. Infect. Dis. , vol.196 , pp. 1749-1753
    • Sokal, E.M.1    Hoppenbrouwers, K.2    Vandermeulen, C.3    Moutschen, M.4    Léonard, P.5    Moreels, A.6    Haumont, M.7    Bollen, A.8    Smets, F.9    Denis, M.10
  • 48
    • 0024266413 scopus 로고
    • Soluble gp350/220 and deletion mutant glycoproteins block Epstein-Barr virus adsorption to lymphocytes
    • J. Tanner, Y. Whang, J. Sample, A. Sears, and E. Kieff Soluble gp350/220 and deletion mutant glycoproteins block Epstein-Barr virus adsorption to lymphocytes J. Virol. 62 1988 4452 4464
    • (1988) J. Virol. , vol.62 , pp. 4452-4464
    • Tanner, J.1    Whang, Y.2    Sample, J.3    Sears, A.4    Kieff, E.5
  • 49
    • 0019203638 scopus 로고
    • Monoclonal antibodies against the major glycoprotein (gp350/220) of Epstein-Barr virus neutralize infectivity
    • D.A. Thorley-Lawson, and K. Geilinger Monoclonal antibodies against the major glycoprotein (gp350/220) of Epstein-Barr virus neutralize infectivity Proc. Natl. Acad. Sci. USA 77 1980 5307 5311
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5307-5311
    • Thorley-Lawson, D.A.1    Geilinger, K.2
  • 50
    • 0019990514 scopus 로고
    • Identification and isolation of the main component (gp350-gp220) of Epstein-Barr virus responsible for generating neutralizing antibodies in vivo
    • D.A. Thorley-Lawson, and C.A. Poodry Identification and isolation of the main component (gp350-gp220) of Epstein-Barr virus responsible for generating neutralizing antibodies in vivo J. Virol. 43 1982 730 736
    • (1982) J. Virol. , vol.43 , pp. 730-736
    • Thorley-Lawson, D.A.1    Poodry, C.A.2
  • 51
    • 0029040871 scopus 로고
    • High resolution crystal structures of amphibian red-cell L ferritin: Potential roles for structural plasticity and solvation in function
    • J. Trikha, E.C. Theil, and N.M. Allewell High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and solvation in function J. Mol. Biol. 248 1995 949 967
    • (1995) J. Mol. Biol. , vol.248 , pp. 949-967
    • Trikha, J.1    Theil, E.C.2    Allewell, N.M.3
  • 52
    • 0037349930 scopus 로고    scopus 로고
    • Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells
    • S.M. Tugizov, J.W. Berline, and J.M. Palefsky Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells Nat. Med. 9 2003 307 314
    • (2003) Nat. Med. , vol.9 , pp. 307-314
    • Tugizov, S.M.1    Berline, J.W.2    Palefsky, J.M.3
  • 53
    • 20144389700 scopus 로고    scopus 로고
    • Molecular and biological characterization of human monoclonal antibodies binding to the spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus
    • E.N. van den Brink, J. Ter Meulen, F. Cox, M.A. Jongeneelen, A. Thijsse, M. Throsby, W.E. Marissen, P.M. Rood, A.B. Bakker, H.R. Gelderblom, and et al. Molecular and biological characterization of human monoclonal antibodies binding to the spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus J. Virol. 79 2005 1635 1644
    • (2005) J. Virol. , vol.79 , pp. 1635-1644
    • Van Den Brink, E.N.1    Ter Meulen, J.2    Cox, F.3    Jongeneelen, M.A.4    Thijsse, A.5    Throsby, M.6    Marissen, W.E.7    Rood, P.M.8    Bakker, A.B.9    Gelderblom, H.R.10
  • 57
    • 55549083164 scopus 로고    scopus 로고
    • Molecular basis of the interaction between complement receptor type 2 (CR2/CD21) and Epstein-Barr virus glycoprotein gp350
    • K.A. Young, A.P. Herbert, P.N. Barlow, V.M. Holers, and J.P. Hannan Molecular basis of the interaction between complement receptor type 2 (CR2/CD21) and Epstein-Barr virus glycoprotein gp350 J. Virol. 82 2008 11217 11227
    • (2008) J. Virol. , vol.82 , pp. 11217-11227
    • Young, K.A.1    Herbert, A.P.2    Barlow, P.N.3    Holers, V.M.4    Hannan, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.