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Volumn 449, Issue , 2014, Pages 304-316

Preparation and properties of a papillomavirus infectious intermediate and its utility for neutralization studies

Author keywords

Carrageenan; Furin; Gamma secretase; Heparin; Human papillomavirus (HPV); Infectious intermediate; L2; Minor capsid protein; Neutralization; Papillomavirus

Indexed keywords

CAPSID PROTEIN; CAPSID PROTEIN L2; CARRAGEENAN; EPITOPE; FURIN; GAMMA SECRETASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84890725011     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2013.10.038     Document Type: Article
Times cited : (35)

References (57)
  • 1
    • 0031001304 scopus 로고    scopus 로고
    • Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage
    • Anderson E.D., VanSlyke J.K., Thulin C.D., Jean F., Thomas G. Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. EMBO J. 1997, 16:1508-1518.
    • (1997) EMBO J. , vol.16 , pp. 1508-1518
    • Anderson, E.D.1    VanSlyke, J.K.2    Thulin, C.D.3    Jean, F.4    Thomas, G.5
  • 2
    • 78650827011 scopus 로고    scopus 로고
    • Development and characterisation of an assay for furin activity
    • Bourne G.L., Grainger D.J. Development and characterisation of an assay for furin activity. J. Immunol. Methods 2011, 364:101-108.
    • (2011) J. Immunol. Methods , vol.364 , pp. 101-108
    • Bourne, G.L.1    Grainger, D.J.2
  • 4
    • 0346688642 scopus 로고    scopus 로고
    • Efficient intracellular assembly of papillomaviral vectors
    • Buck C.B., Pastrana D.V., Lowy D.R., Schiller J.T. Efficient intracellular assembly of papillomaviral vectors. J. Virol. 2004, 78:751-757.
    • (2004) J. Virol. , vol.78 , pp. 751-757
    • Buck, C.B.1    Pastrana, D.V.2    Lowy, D.R.3    Schiller, J.T.4
  • 7
    • 84858271333 scopus 로고    scopus 로고
    • The papillomavirus virion: a machine built to hide molecular Achilles' heels
    • Buck C.B., Trus B.L. The papillomavirus virion: a machine built to hide molecular Achilles' heels. Adv. Exp. Med. Biol. 2012, 726:403-422.
    • (2012) Adv. Exp. Med. Biol. , vol.726 , pp. 403-422
    • Buck, C.B.1    Trus, B.L.2
  • 8
    • 0025801048 scopus 로고
    • Expression of human papillomavirus proteins in yeast Saccharomyces cerevisiae
    • Carter J.J., Yaegashi N., Jenison S.A., Galloway D.A. Expression of human papillomavirus proteins in yeast Saccharomyces cerevisiae. Virology 1991, 182:513-521.
    • (1991) Virology , vol.182 , pp. 513-521
    • Carter, J.J.1    Yaegashi, N.2    Jenison, S.A.3    Galloway, D.A.4
  • 10
    • 0025755278 scopus 로고
    • The open reading frame L2 of cottontail rabbit papillomavirus contains antibody-inducing neutralizing epitopes
    • Christensen N.D., Kreider J.W., Kan N.C., DiAngelo S.L. The open reading frame L2 of cottontail rabbit papillomavirus contains antibody-inducing neutralizing epitopes. Virology 1991, 181:572-579.
    • (1991) Virology , vol.181 , pp. 572-579
    • Christensen, N.D.1    Kreider, J.W.2    Kan, N.C.3    DiAngelo, S.L.4
  • 11
    • 84881260776 scopus 로고    scopus 로고
    • Secondary infections, expanded tissue tropism, and evidence for malignant potential in immunocompromised mice infected with Mus musculus papillomavirus 1 DNA and virus
    • Cladel N.M., Budgeon L.R., Cooper T.K., Balogh K.K., Hu J., Christensen N.D. Secondary infections, expanded tissue tropism, and evidence for malignant potential in immunocompromised mice infected with Mus musculus papillomavirus 1 DNA and virus. J. Virol. 2013, 87:9391-9395.
    • (2013) J. Virol. , vol.87 , pp. 9391-9395
    • Cladel, N.M.1    Budgeon, L.R.2    Cooper, T.K.3    Balogh, K.K.4    Hu, J.5    Christensen, N.D.6
  • 12
    • 70349840682 scopus 로고    scopus 로고
    • Overlapping and independent structural roles for human papillomavirus type 16 L2 conserved cysteines
    • Conway M.J., Alam S., Christensen N.D., Meyers C. Overlapping and independent structural roles for human papillomavirus type 16 L2 conserved cysteines. Virology 2009, 393:295-303.
    • (2009) Virology , vol.393 , pp. 295-303
    • Conway, M.J.1    Alam, S.2    Christensen, N.D.3    Meyers, C.4
  • 13
    • 70349750271 scopus 로고    scopus 로고
    • Tissue-spanning redox gradient-dependent assembly of native human papillomavirus type 16 virions
    • Conway M.J., Alam S., Ryndock E.J., Cruz L., Christensen N.D., Roden R.B., Meyers C. Tissue-spanning redox gradient-dependent assembly of native human papillomavirus type 16 virions. J. Virol. 2009, 83:10515-10526.
    • (2009) J. Virol. , vol.83 , pp. 10515-10526
    • Conway, M.J.1    Alam, S.2    Ryndock, E.J.3    Cruz, L.4    Christensen, N.D.5    Roden, R.B.6    Meyers, C.7
  • 14
    • 79951560833 scopus 로고    scopus 로고
    • Cross-neutralization potential of native human papillomavirus N-terminal L2 epitopes
    • Conway M.J., Cruz L., Alam S., Christensen N.D., Meyers C. Cross-neutralization potential of native human papillomavirus N-terminal L2 epitopes. PloS One 2011, 6:e16405.
    • (2011) PloS One , vol.6
    • Conway, M.J.1    Cruz, L.2    Alam, S.3    Christensen, N.D.4    Meyers, C.5
  • 15
    • 84879831306 scopus 로고    scopus 로고
    • Differential dependence on host cell glycosaminoglycans for infection of epithelial cells by high-risk HPV types
    • Cruz L., Meyers C. Differential dependence on host cell glycosaminoglycans for infection of epithelial cells by high-risk HPV types. PloS One 2013, 8:e68379.
    • (2013) PloS One , vol.8
    • Cruz, L.1    Meyers, C.2
  • 17
    • 42449153250 scopus 로고    scopus 로고
    • Mechanisms of human papillomavirus type 16 neutralization by l2 cross-neutralizing and l1 type-specific antibodies
    • Day P.M., Gambhira R., Roden R.B., Lowy D.R., Schiller J.T. Mechanisms of human papillomavirus type 16 neutralization by l2 cross-neutralizing and l1 type-specific antibodies. J. Virol. 2008, 82:4638-4646.
    • (2008) J. Virol. , vol.82 , pp. 4638-4646
    • Day, P.M.1    Gambhira, R.2    Roden, R.B.3    Lowy, D.R.4    Schiller, J.T.5
  • 18
    • 57349115458 scopus 로고    scopus 로고
    • Heparan sulfate-independent cell binding and infection with furin-precleaved papillomavirus capsids
    • Day P.M., Lowy D.R., Schiller J.T. Heparan sulfate-independent cell binding and infection with furin-precleaved papillomavirus capsids. J. Virol. 2008, 82:12565-12568.
    • (2008) J. Virol. , vol.82 , pp. 12565-12568
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 19
    • 84863540390 scopus 로고    scopus 로고
    • A human papillomavirus (HPV) in vitro neutralization assay that recapitulates the in vitro process of infection provides a sensitive measure of HPV L2 infection-inhibiting antibodies
    • Day P.M., Pang Y.Y., Kines R.C., Thompson C.D., Lowy D.R., Schiller J.T. A human papillomavirus (HPV) in vitro neutralization assay that recapitulates the in vitro process of infection provides a sensitive measure of HPV L2 infection-inhibiting antibodies. Clin. Vaccine Immunol. 2012, 19:1075-1082.
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 1075-1082
    • Day, P.M.1    Pang, Y.Y.2    Kines, R.C.3    Thompson, C.D.4    Lowy, D.R.5    Schiller, J.T.6
  • 20
    • 84863540390 scopus 로고    scopus 로고
    • A human papillomavirus (HPV) in vitro neutralization assay that recapitulates the in vitro process of infection provides a sensitive measure of HPV L2 infection-inhibiting antibodies
    • Day P.M., Pang Y.Y.S., Kines R.C., Thompson C.D., Lowy D.R., Schiller J.T. A human papillomavirus (HPV) in vitro neutralization assay that recapitulates the in vitro process of infection provides a sensitive measure of HPV L2 infection-inhibiting antibodies. Clin. Vaccine Immunol. 2012, 19:1075-1082.
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 1075-1082
    • Day, P.M.1    Pang, Y.Y.S.2    Kines, R.C.3    Thompson, C.D.4    Lowy, D.R.5    Schiller, J.T.6
  • 22
    • 0023201247 scopus 로고
    • Identification of proteins encoded by the L1 and L2 open reading frames of human papillomavirus 1a
    • Doorbar J., Gallimore P.H. Identification of proteins encoded by the L1 and L2 open reading frames of human papillomavirus 1a. J. Virol. 1987, 61:2793-2799.
    • (1987) J. Virol. , vol.61 , pp. 2793-2799
    • Doorbar, J.1    Gallimore, P.H.2
  • 23
    • 0017259817 scopus 로고
    • Establishment of a human carcinoembryonic antigen-producing colon adenocarcinoma cell line
    • Drewinko B., Romsdahl M.M., Yang L.Y., Ahearn M.J., Trujillo J.M. Establishment of a human carcinoembryonic antigen-producing colon adenocarcinoma cell line. Cancer Res. 1976, 36:467-475.
    • (1976) Cancer Res. , vol.36 , pp. 467-475
    • Drewinko, B.1    Romsdahl, M.M.2    Yang, L.Y.3    Ahearn, M.J.4    Trujillo, J.M.5
  • 24
    • 2142854239 scopus 로고
    • Animal cell mutants defective in glycosaminoglycan biosynthesis
    • Esko J.D., Stewart T.E., Taylor W.H. Animal cell mutants defective in glycosaminoglycan biosynthesis. Proc. Natl. Acad. Sci. USA 1985, 82:3197-3201.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3197-3201
    • Esko, J.D.1    Stewart, T.E.2    Taylor, W.H.3
  • 26
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon V.M., Klimpel K.R., Arora N., Henderson M.A., Leppla S.H. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. 1995, 63:82-87.
    • (1995) Infect. Immun. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 27
    • 15244344245 scopus 로고    scopus 로고
    • The minor capsid protein L2 contributes to two steps in the human papillomavirus type 31 life cycle
    • Holmgren S.C., Patterson N.A., Ozbun M.A., Lambert P.F. The minor capsid protein L2 contributes to two steps in the human papillomavirus type 31 life cycle. J. Virol. 2005, 79:3938-3948.
    • (2005) J. Virol. , vol.79 , pp. 3938-3948
    • Holmgren, S.C.1    Patterson, N.A.2    Ozbun, M.A.3    Lambert, P.F.4
  • 28
    • 77957665372 scopus 로고    scopus 로고
    • Inhibition of gamma secretase blocks HPV infection
    • Huang H.S., Buck C.B., Lambert P.F. Inhibition of gamma secretase blocks HPV infection. Virology 2010, 407:391-396.
    • (2010) Virology , vol.407 , pp. 391-396
    • Huang, H.S.1    Buck, C.B.2    Lambert, P.F.3
  • 31
    • 0024546844 scopus 로고
    • Identification of L2 open reading frame gene products of bovine papillomavirus type 1 using monoclonal antibodies
    • Jin X.W., Cowsert L.M., Pilacinski W.P., Jenson A.B. Identification of L2 open reading frame gene products of bovine papillomavirus type 1 using monoclonal antibodies. J. Gen. Virol. 1989, 70(Pt 5):1133-1140.
    • (1989) J. Gen. Virol. , vol.70 , Issue.PART 5 , pp. 1133-1140
    • Jin, X.W.1    Cowsert, L.M.2    Pilacinski, W.P.3    Jenson, A.B.4
  • 32
    • 60049100934 scopus 로고    scopus 로고
    • Role of heparan sulfate in attachment to and infection of the murine female genital tract by human papillomavirus
    • Johnson K.M., Kines R.C., Roberts J.N., Lowy D.R., Schiller J.T., Day P.M. Role of heparan sulfate in attachment to and infection of the murine female genital tract by human papillomavirus. J. Virol. 2009, 83:2067-2074.
    • (2009) J. Virol. , vol.83 , pp. 2067-2074
    • Johnson, K.M.1    Kines, R.C.2    Roberts, J.N.3    Lowy, D.R.4    Schiller, J.T.5    Day, P.M.6
  • 34
    • 73949127173 scopus 로고    scopus 로고
    • The initial steps leading to papillomavirus infection occur on the basement membrane prior to cell surface binding
    • Kines R.C., Thompson C.D., Lowy D.R., Schiller J.T., Day P.M. The initial steps leading to papillomavirus infection occur on the basement membrane prior to cell surface binding. Proc. Natl. Acad. Sci. USA 2009, 106:20458-20463.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20458-20463
    • Kines, R.C.1    Thompson, C.D.2    Lowy, D.R.3    Schiller, J.T.4    Day, P.M.5
  • 35
    • 0023032821 scopus 로고
    • The L2 open reading frame of human papillomavirus type 1a encodes a minor structural protein carrying type-specific antigens
    • Komly C.A., Breitburd F., Croissant O., Streeck R.E. The L2 open reading frame of human papillomavirus type 1a encodes a minor structural protein carrying type-specific antigens. J. Virol. 1986, 60:813-816.
    • (1986) J. Virol. , vol.60 , pp. 813-816
    • Komly, C.A.1    Breitburd, F.2    Croissant, O.3    Streeck, R.E.4
  • 37
    • 0031579249 scopus 로고    scopus 로고
    • Sequence close to the N-terminus of L2 protein is displayed on the surface of bovine papillomavirus type 1 virions
    • Liu W.J., Gissmann L., Sun X.Y., Kanjanahaluethai A., Muller M., Doorbar J., Zhou J. Sequence close to the N-terminus of L2 protein is displayed on the surface of bovine papillomavirus type 1 virions. Virology 1997, 227:474-483.
    • (1997) Virology , vol.227 , pp. 474-483
    • Liu, W.J.1    Gissmann, L.2    Sun, X.Y.3    Kanjanahaluethai, A.4    Muller, M.5    Doorbar, J.6    Zhou, J.7
  • 38
    • 84866628242 scopus 로고    scopus 로고
    • Cross-protective efficacy of two human papillomavirus vaccines: a systematic review and meta-analysis
    • Malagon T., Drolet M., Boily M.C., Franco E.L., Jit M., Brisson J., Brisson M. Cross-protective efficacy of two human papillomavirus vaccines: a systematic review and meta-analysis. Lancet Infect. Dis. 2012, 12:781-789.
    • (2012) Lancet Infect. Dis. , vol.12 , pp. 781-789
    • Malagon, T.1    Drolet, M.2    Boily, M.C.3    Franco, E.L.4    Jit, M.5    Brisson, J.6    Brisson, M.7
  • 40
    • 1942489261 scopus 로고    scopus 로고
    • Propagation, infection, and neutralization of authentic HPV16 virus
    • McLaughlin-Drubin M.E., Christensen N.D., Meyers C. Propagation, infection, and neutralization of authentic HPV16 virus. Virology 2004, 322:213-219.
    • (2004) Virology , vol.322 , pp. 213-219
    • McLaughlin-Drubin, M.E.1    Christensen, N.D.2    Meyers, C.3
  • 41
    • 0026671476 scopus 로고
    • Biosynthesis of human papillomavirus from a continuous cell-line upon epithelial differentiation
    • Meyers C., Frattini M.G., Hudson J.B., Laimins L.A. Biosynthesis of human papillomavirus from a continuous cell-line upon epithelial differentiation. Science 1992, 257:971-973.
    • (1992) Science , vol.257 , pp. 971-973
    • Meyers, C.1    Frattini, M.G.2    Hudson, J.B.3    Laimins, L.A.4
  • 42
    • 33748761925 scopus 로고    scopus 로고
    • Chapter 2: The burden of HPV-related cancers
    • Parkin D.M., Bray F. Chapter 2: The burden of HPV-related cancers. Vaccine 2006, 24(Suppl. 3):S3/11-25.
    • (2006) Vaccine , vol.24 , Issue.SUPPL. 3
    • Parkin, D.M.1    Bray, F.2
  • 44
    • 21544435412 scopus 로고    scopus 로고
    • Production of infectious human papillomavirus independently of viral replication and epithelial cell differentiation
    • Pyeon D., Lambert P.F., Ahlquist P. Production of infectious human papillomavirus independently of viral replication and epithelial cell differentiation. Proc. Natl. Acad. Sci. USA 2005, 102:9311-9316.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9311-9316
    • Pyeon, D.1    Lambert, P.F.2    Ahlquist, P.3
  • 45
    • 84886879612 scopus 로고    scopus 로고
    • Multiple heparan sulfate binding site engagements are required for the infectious entry of human papillomavirus type 16
    • Richards K.F., Bienkowska-Haba M., Dasgupta J., Chen X.S., Sapp M. Multiple heparan sulfate binding site engagements are required for the infectious entry of human papillomavirus type 16. J. Virol. 2013, 87:11426-11437.
    • (2013) J. Virol. , vol.87 , pp. 11426-11437
    • Richards, K.F.1    Bienkowska-Haba, M.2    Dasgupta, J.3    Chen, X.S.4    Sapp, M.5
  • 46
    • 0024382871 scopus 로고
    • Identification and characterization of the BPV-2 L2 protein
    • Rippe R.A., Meinke W.J. Identification and characterization of the BPV-2 L2 protein. Virology 1989, 171:298-301.
    • (1989) Virology , vol.171 , pp. 298-301
    • Rippe, R.A.1    Meinke, W.J.2
  • 48
    • 0034630951 scopus 로고    scopus 로고
    • Minor capsid protein of human genital papillomaviruses contains subdominant, cross-neutralizing epitopes
    • Roden R.B., Yutzy W.H.4th, Fallon R., Inglis S., Lowy D.R., Schiller J.T. Minor capsid protein of human genital papillomaviruses contains subdominant, cross-neutralizing epitopes. Virology 2000, 270:254-257.
    • (2000) Virology , vol.270 , pp. 254-257
    • Roden, R.B.1    Yutzy IV, W.H.2    Fallon, R.3    Inglis, S.4    Lowy, D.R.5    Schiller, J.T.6
  • 49
    • 0025012317 scopus 로고
    • Expression of the full-length products of the human papillomavirus type 6b (HPV-6b) and HPV-11 L2 open reading frames by recombinant baculovirus, and antigenic comparisons with HPV-11 whole virus particles
    • Rose R.C., Bonnez W., Strike D.G., Reichman R.C. Expression of the full-length products of the human papillomavirus type 6b (HPV-6b) and HPV-11 L2 open reading frames by recombinant baculovirus, and antigenic comparisons with HPV-11 whole virus particles. J. Gen. Virol. 1990, 71(Pt 11):2725-2729.
    • (1990) J. Gen. Virol. , vol.71 , Issue.PART 11 , pp. 2725-2729
    • Rose, R.C.1    Bonnez, W.2    Strike, D.G.3    Reichman, R.C.4
  • 50
    • 70349299873 scopus 로고    scopus 로고
    • Chimeric L1-L2 virus-like particles as potential broad-spectrum human papillomavirus vaccines
    • Schellenbacher C., Roden R., Kirnbauer R. Chimeric L1-L2 virus-like particles as potential broad-spectrum human papillomavirus vaccines. J. Virol. 2009, 83:10085-10095.
    • (2009) J. Virol. , vol.83 , pp. 10085-10095
    • Schellenbacher, C.1    Roden, R.2    Kirnbauer, R.3
  • 51
    • 84860891623 scopus 로고    scopus 로고
    • Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections
    • Surviladze Z., Dziduszko A., Ozbun M.A. Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections. PLoS Pathog. 2012, 8:e1002519.
    • (2012) PLoS Pathog. , vol.8
    • Surviladze, Z.1    Dziduszko, A.2    Ozbun, M.A.3
  • 52
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: from protein traffic to embryogenesis and disease
    • Thomas G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev.Mol. Cell Biol. 2002, 3:753-766.
    • (2002) Nat. Rev.Mol. Cell Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 53
    • 80051770278 scopus 로고    scopus 로고
    • A pan-HPV vaccine based on bacteriophage PP7 VLPs displaying broadly cross-neutralizing epitopes from the HPV minor capsid protein, L2
    • Tumban E., Peabody J., Peabody D.S., Chackerian B. A pan-HPV vaccine based on bacteriophage PP7 VLPs displaying broadly cross-neutralizing epitopes from the HPV minor capsid protein, L2. PloS One 2011, 6:e23310.
    • (2011) PloS One , vol.6
    • Tumban, E.1    Peabody, J.2    Peabody, D.S.3    Chackerian, B.4
  • 54
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation
    • Vey M., Schafer W., Berghofer S., Klenk H.D., Garten W. Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation. J. Cell Biol. 1994, 127:1829-1842.
    • (1994) J. Cell Biol. , vol.127 , pp. 1829-1842
    • Vey, M.1    Schafer, W.2    Berghofer, S.3    Klenk, H.D.4    Garten, W.5
  • 56
    • 84890731895 scopus 로고    scopus 로고
    • The Fc Domain Plays an Important Role in Neutralization and Protection of Mice from Vaginal HPV16 Challenge by Monoclonal Antibody WW1
    • In: Proceedings of the 28th International Papillomavirus Meeting, Puerto Rico, November 2012, Abstract B06-086
    • Wu, W., Kwak, K., Jagu, S., Huh, W.K., Roden, R.B.S., 2012. The Fc Domain Plays an Important Role in Neutralization and Protection of Mice from Vaginal HPV16 Challenge by Monoclonal Antibody WW1. In: Proceedings of the 28th International Papillomavirus Meeting, Puerto Rico, November 2012, Abstract B06-086.
    • (2012)
    • Wu, W.1    Kwak, K.2    Jagu, S.3    Huh, W.K.4    Roden, R.B.S.5
  • 57
    • 0026343745 scopus 로고
    • Baculovirus expression of the human papillomavirus type 16 capsid proteins: detection of L1-L2 protein complexes
    • Xi S.Z., Banks L.M. Baculovirus expression of the human papillomavirus type 16 capsid proteins: detection of L1-L2 protein complexes. J. Gen. Virol. 1991, 72(Pt 12):2981-2988.
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 12 , pp. 2981-2988
    • Xi, S.Z.1    Banks, L.M.2


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