메뉴 건너뛰기




Volumn 7, Issue 11, 2015, Pages 5813-5830

Cleavage of the HPV16 minor capsid protein L2 during virion morphogenesis ablates the requirement for cellular furin during de novo infection

Author keywords

Furin; HPV16; Human papillomavirus (HPV); J0101; PACS

Indexed keywords

CAPSID PROTEIN; FURIN; PROPROTEIN CONVERTASE 1; L2 PROTEIN, HUMAN PAPILLOMAVIRUS TYPE 16; ONCOPROTEIN;

EID: 84946925895     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v7112910     Document Type: Article
Times cited : (19)

References (82)
  • 1
    • 0142125393 scopus 로고    scopus 로고
    • Natural history of anogenital human papillomavirus infection and neoplasia
    • [CrossRef] [PubMed]
    • Schiffman, M.; Kjaer, S.K. Natural history of anogenital human papillomavirus infection and neoplasia. J. Natl. Cancer Inst. Monogr. 2003, 31, 14-19. [CrossRef] [PubMed]
    • (2003) J. Natl. Cancer Inst. Monogr. , vol.31 , pp. 14-19
    • Schiffman, M.1    Kjaer, S.K.2
  • 2
    • 59349121140 scopus 로고    scopus 로고
    • Papillomaviruses in the causation of human cancers-A brief historical account
    • [CrossRef] [PubMed]
    • Zur Hausen, H. Papillomaviruses in the causation of human cancers-A brief historical account. Virology 2009, 384, 260-265. [CrossRef] [PubMed]
    • (2009) Virology , vol.384 , pp. 260-265
    • Zur Hausen, H.1
  • 3
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction
    • [CrossRef]
    • Baker, T.S.; Newcomb, W.W.; Olson, N.H.; Cowsert, L.M.; Olson, C.; Brown, J.C. Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction. Biophys. J. 1991, 60, 1445-1456. [CrossRef]
    • (1991) Biophys. J. , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 4
    • 0033696899 scopus 로고    scopus 로고
    • Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16
    • [CrossRef]
    • Chen, X.S.; Garcea, R.L.; Goldberg, I.; Casini, G.; Harrison, S.C. Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16. Mol. Cell 2000, 5, 557-567. [CrossRef]
    • (2000) Mol. Cell , vol.5 , pp. 557-567
    • Chen, X.S.1    Garcea, R.L.2    Goldberg, I.3    Casini, G.4    Harrison, S.C.5
  • 5
    • 34948862944 scopus 로고    scopus 로고
    • Surface-exposed amino acid residues of hpv16 L1 protein mediating interaction with cell surface heparan sulfate
    • [CrossRef] [PubMed]
    • Knappe, M.; Bodevin, S.; Selinka, H.C.; Spillmann, D.; Streeck, R.E.; Chen, X.S.; Lindahl, U.; Sapp, M. Surface-exposed amino acid residues of hpv16 L1 protein mediating interaction with cell surface heparan sulfate. J. Biol. Chem. 2007, 282, 27913-27922. [CrossRef] [PubMed]
    • (2007) J. Biol. Chem. , vol.282 , pp. 27913-27922
    • Knappe, M.1    Bodevin, S.2    Selinka, H.C.3    Spillmann, D.4    Streeck, R.E.5    Chen, X.S.6    Lindahl, U.7    Sapp, M.8
  • 6
    • 0029025421 scopus 로고
    • Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells
    • [PubMed]
    • Volpers, C.; Unckell, F.; Schirmacher, P.; Streeck, R.E.; Sapp, M. Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells. J. Virol. 1995, 69, 3258-3264. [PubMed]
    • (1995) J. Virol. , vol.69 , pp. 3258-3264
    • Volpers, C.1    Unckell, F.2    Schirmacher, P.3    Streeck, R.E.4    Sapp, M.5
  • 7
    • 0030931283 scopus 로고    scopus 로고
    • Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution
    • [CrossRef] [PubMed]
    • Trus, B.L.; Roden, R.B.; Greenstone, H.L.; Vrhel, M.; Schiller, J.T.; Booy, F.P. Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution. Nat. Struct. Biol. 1997, 4, 413-420. [CrossRef] [PubMed]
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 413-420
    • Trus, B.L.1    Roden, R.B.2    Greenstone, H.L.3    Vrhel, M.4    Schiller, J.T.5    Booy, F.P.6
  • 9
    • 84884353537 scopus 로고    scopus 로고
    • L2, the minor capsid protein of papillomavirus
    • [CrossRef] [PubMed]
    • Wang, J.W.; Roden, R.B. L2, the minor capsid protein of papillomavirus. Virology 2013, 445, 175-186. [CrossRef] [PubMed]
    • (2013) Virology , vol.445 , pp. 175-186
    • Wang, J.W.1    Roden, R.B.2
  • 10
    • 0029841214 scopus 로고    scopus 로고
    • In vitro generation and type-specific neutralization of a human papillomavirus type 16 virion pseudotype
    • [PubMed]
    • Roden, R.B.; Greenstone, H.L.; Kirnbauer, R.; Booy, F.P.; Jessie, J.; Lowy, D.R.; Schiller, J.T. In vitro generation and type-specific neutralization of a human papillomavirus type 16 virion pseudotype. J. Virol. 1996, 70, 5875-5883. [PubMed]
    • (1996) J. Virol. , vol.70 , pp. 5875-5883
    • Roden, R.B.1    Greenstone, H.L.2    Kirnbauer, R.3    Booy, F.P.4    Jessie, J.5    Lowy, D.R.6    Schiller, J.T.7
  • 11
    • 0032502751 scopus 로고    scopus 로고
    • Dna packaging by L1 and L2 capsid proteins of bovine papillomavirus type 1
    • [CrossRef] [PubMed]
    • Zhao, K.N.; Sun, X.Y.; Frazer, I.H.; Zhou, J. Dna packaging by L1 and L2 capsid proteins of bovine papillomavirus type 1. Virology 1998, 243, 482-491. [CrossRef] [PubMed]
    • (1998) Virology , vol.243 , pp. 482-491
    • Zhao, K.N.1    Sun, X.Y.2    Frazer, I.H.3    Zhou, J.4
  • 12
    • 25444497974 scopus 로고    scopus 로고
    • Human papillomavirus 16 minor capsid protein L2 helps capsomeres assemble independently of intercapsomeric disulfide bonding
    • [CrossRef] [PubMed]
    • Ishii, Y.; Ozaki, S.; Tanaka, K.; Kanda, T. Human papillomavirus 16 minor capsid protein L2 helps capsomeres assemble independently of intercapsomeric disulfide bonding. Virus Genes 2005, 31, 321-328. [CrossRef] [PubMed]
    • (2005) Virus Genes , vol.31 , pp. 321-328
    • Ishii, Y.1    Ozaki, S.2    Tanaka, K.3    Kanda, T.4
  • 13
    • 84867846134 scopus 로고    scopus 로고
    • Host-cell factors involved in papillomavirus entry
    • [CrossRef] [PubMed]
    • Florin, L.; Sapp, M.; Spoden, G.A. Host-cell factors involved in papillomavirus entry. Med. Microbiol. Immunol. 2012, 201, 437-448. [CrossRef] [PubMed]
    • (2012) Med. Microbiol. Immunol. , vol.201 , pp. 437-448
    • Florin, L.1    Sapp, M.2    Spoden, G.A.3
  • 14
    • 0035130055 scopus 로고    scopus 로고
    • Human papillomavirus type 16 minor capsid protein L2 N-terminal region containing a common neutralization epitope binds to the cell surface and enters the cytoplasm
    • [PubMed]
    • Kawana, Y.; Kawana, K.; Yoshikawa, H.; Taketani, Y.; Yoshiike, K.; Kanda, T. Human papillomavirus type 16 minor capsid protein L2 N-terminal region containing a common neutralization epitope binds to the cell surface and enters the cytoplasm. J. Virol. 2001, 75, 2331-2336. [PubMed]
    • (2001) J. Virol. , vol.75 , pp. 2331-2336
    • Kawana, Y.1    Kawana, K.2    Yoshikawa, H.3    Taketani, Y.4    Yoshiike, K.5    Kanda, T.6
  • 15
    • 0037333367 scopus 로고    scopus 로고
    • Cell surface-binding motifs of L2 that facilitate papillomavirus infection
    • [CrossRef]
    • Yang, R.; Day, P.M.; Yutzy, W.H.T.; Lin, K.Y.; Hung, C.F.; Roden, R.B. Cell surface-binding motifs of L2 that facilitate papillomavirus infection. J. Virol. 2003, 77, 3531-3541. [CrossRef]
    • (2003) J. Virol. , vol.77 , pp. 3531-3541
    • Yang, R.1    Day, P.M.2    Yutzy, W.H.T.3    Lin, K.Y.4    Hung, C.F.5    Roden, R.B.6
  • 16
  • 17
    • 0032486389 scopus 로고    scopus 로고
    • A surface immunodeterminant of human papillomavirus type 16 minor capsid protein L2
    • [CrossRef] [PubMed]
    • Kawana, K.; Matsumoto, K.; Yoshikawa, H.; Taketani, Y.; Kawana, T.; Yoshiike, K.; Kanda, T. A surface immunodeterminant of human papillomavirus type 16 minor capsid protein L2. Virology 1998, 245, 353-359. [CrossRef] [PubMed]
    • (1998) Virology , vol.245 , pp. 353-359
    • Kawana, K.1    Matsumoto, K.2    Yoshikawa, H.3    Taketani, Y.4    Kawana, T.5    Yoshiike, K.6    Kanda, T.7
  • 18
    • 70049114748 scopus 로고    scopus 로고
    • Target cell cyclophilins facilitate human papillomavirus type 16 infection
    • [CrossRef] [PubMed]
    • Bienkowska-Haba, M.; Patel, H.D.; Sapp, M. Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog. 2009, 5, e1000524. [CrossRef] [PubMed]
    • (2009) PLoS Pathog. , vol.5
    • Bienkowska-Haba, M.1    Patel, H.D.2    Sapp, M.3
  • 19
    • 84856808484 scopus 로고    scopus 로고
    • Human papillomavirus L2 facilitates viral escape from late endosomes via sorting nexin 17
    • [CrossRef] [PubMed]
    • Bergant Marusic, M.; Ozbun, M.A.; Campos, S.K.; Myers, M.P.; Banks, L. Human papillomavirus L2 facilitates viral escape from late endosomes via sorting nexin 17. Traffic 2012, 13, 455-467. [CrossRef] [PubMed]
    • (2012) Traffic , vol.13 , pp. 455-467
    • Bergant Marusic, M.1    Ozbun, M.A.2    Campos, S.K.3    Myers, M.P.4    Banks, L.5
  • 20
    • 18744365783 scopus 로고    scopus 로고
    • Interaction of tsnare syntaxin 18 with the papillomavirus minor capsid protein mediates infection
    • [CrossRef] [PubMed]
    • Bossis, I.; Roden, R.B.; Gambhira, R.; Yang, R.; Tagaya, M.; Howley, P.M.; Meneses, P.I. Interaction of tsnare syntaxin 18 with the papillomavirus minor capsid protein mediates infection. J. Virol. 2005, 79, 6723-6731. [CrossRef] [PubMed]
    • (2005) J. Virol. , vol.79 , pp. 6723-6731
    • Bossis, I.1    Roden, R.B.2    Gambhira, R.3    Yang, R.4    Tagaya, M.5    Howley, P.M.6    Meneses, P.I.7
  • 21
    • 0038485582 scopus 로고    scopus 로고
    • Interaction of L2 with β-actin directs intracellular transport of papillomavirus and infection
    • [CrossRef] [PubMed]
    • Yang, R.; Yutzy, W.H.T.; Viscidi, R.P.; Roden, R.B. Interaction of L2 with β-actin directs intracellular transport of papillomavirus and infection. J. Biol. Chem. 2003, 278, 12546-12553. [CrossRef] [PubMed]
    • (2003) J. Biol. Chem. , vol.278 , pp. 12546-12553
    • Yang, R.1    Yutzy, W.H.T.2    Viscidi, R.P.3    Roden, R.B.4
  • 22
    • 33745251121 scopus 로고    scopus 로고
    • Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2
    • [CrossRef] [PubMed]
    • Florin, L.; Becker, K.A.; Lambert, C.; Nowak, T.; Sapp, C.; Strand, D.; Streeck, R.E.; Sapp, M. Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2. J. Virol. 2006, 80, 6691-6696. [CrossRef] [PubMed]
    • (2006) J. Virol. , vol.80 , pp. 6691-6696
    • Florin, L.1    Becker, K.A.2    Lambert, C.3    Nowak, T.4    Sapp, C.5    Strand, D.6    Streeck, R.E.7    Sapp, M.8
  • 23
    • 0031984638 scopus 로고    scopus 로고
    • The papillomavirus minor capsid protein, L2, induces localization of the major capsid protein, L1, and the viral transcription/replication protein, E2, to PML oncogenic domains
    • [PubMed]
    • Day, P.M.; Roden, R.B.; Lowy, D.R.; Schiller, J.T. The papillomavirus minor capsid protein, L2, induces localization of the major capsid protein, L1, and the viral transcription/replication protein, E2, to PML oncogenic domains. J. Virol. 1998, 72, 142-150. [PubMed]
    • (1998) J. Virol. , vol.72 , pp. 142-150
    • Day, P.M.1    Roden, R.B.2    Lowy, D.R.3    Schiller, J.T.4
  • 24
    • 70449109171 scopus 로고    scopus 로고
    • Nuclear location of minor capsid protein L2 is required for expression of a reporter plasmid packaged in HPV51 pseudovirions
    • [CrossRef] [PubMed]
    • Kondo, K.; Ishii, Y.; Mori, S.; Shimabukuro, S.; Yoshikawa, H.; Kanda, T. Nuclear location of minor capsid protein L2 is required for expression of a reporter plasmid packaged in HPV51 pseudovirions. Virology 2009, 394, 259-265. [CrossRef] [PubMed]
    • (2009) Virology , vol.394 , pp. 259-265
    • Kondo, K.1    Ishii, Y.2    Mori, S.3    Shimabukuro, S.4    Yoshikawa, H.5    Kanda, T.6
  • 25
    • 31944439998 scopus 로고    scopus 로고
    • Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection
    • [CrossRef] [PubMed]
    • Richards, R.M.; Lowy, D.R.; Schiller, J.T.; Day, P.M. Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection. Proc. Natl. Acad. Sci. USA 2006, 103, 1522-1527. [CrossRef] [PubMed]
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1522-1527
    • Richards, R.M.1    Lowy, D.R.2    Schiller, J.T.3    Day, P.M.4
  • 26
    • 73949127173 scopus 로고    scopus 로고
    • The initial steps leading to papillomavirus infection occur on the basement membrane prior to cell surface binding
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 28
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • [PubMed]
    • Stadler, K.; Allison, S.L.; Schalich, J.; Heinz, F.X. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 1997, 71, 8475-8481. [PubMed]
    • (1997) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 29
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins
    • [CrossRef] [PubMed]
    • Nakayama, K. Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 1997, 327(Pt. 3), 625-635. [CrossRef] [PubMed]
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 30
    • 0027298474 scopus 로고
    • Protease-dependent virus tropism and pathogenicity
    • [CrossRef]
    • Nagai, Y. Protease-dependent virus tropism and pathogenicity. Trends Microbiol. 1993, 1, 81-87. [CrossRef]
    • (1993) Trends Microbiol. , vol.1 , pp. 81-87
    • Nagai, Y.1
  • 32
    • 0346688642 scopus 로고    scopus 로고
    • Efficient intracellular assembly of papillomaviral vectors
    • [CrossRef] [PubMed]
    • Buck, C.B.; Pastrana, D.V.; Lowy, D.R.; Schiller, J.T. Efficient intracellular assembly of papillomaviral vectors. J. Virol. 2004, 78, 751-757. [CrossRef] [PubMed]
    • (2004) J. Virol. , vol.78 , pp. 751-757
    • Buck, C.B.1    Pastrana, D.V.2    Lowy, D.R.3    Schiller, J.T.4
  • 33
    • 84878199077 scopus 로고    scopus 로고
    • The evolving field of human papillomavirus receptor research: A review of binding and entry
    • [CrossRef] [PubMed]
    • Raff, A.B.; Woodham, A.W.; Raff, L.M.; Skeate, J.G.; Yan, L.; da Silva, D.M.; Schelhaas, M.; Kast, W.M. The evolving field of human papillomavirus receptor research: A review of binding and entry. J. Virol. 2013, 87, 6062-6072. [CrossRef] [PubMed]
    • (2013) J. Virol. , vol.87 , pp. 6062-6072
    • Raff, A.B.1    Woodham, A.W.2    Raff, L.M.3    Skeate, J.G.4    Yan, L.5    da Silva, D.M.6    Schelhaas, M.7    Kast, W.M.8
  • 34
    • 0037347091 scopus 로고    scopus 로고
    • Papillomaviruses infect cells via a clathrin-dependent pathway
    • [CrossRef]
    • Day, P.M.; Lowy, D.R.; Schiller, J.T. Papillomaviruses infect cells via a clathrin-dependent pathway. Virology 2003, 307, 1-11. [CrossRef]
    • (2003) Virology , vol.307 , pp. 1-11
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 35
    • 1642452616 scopus 로고    scopus 로고
    • Differential antibody responses to a distinct region of human papillomavirus minor capsid proteins
    • [PubMed]
    • Embers, M.E.; Budgeon, L.R.; Culp, T.D.; Reed, C.A.; Pickel, M.D.; Christensen, N.D. Differential antibody responses to a distinct region of human papillomavirus minor capsid proteins. Vaccine 2004, 22, 670-680. [PubMed]
    • (2004) Vaccine , vol.22 , pp. 670-680
    • Embers, M.E.1    Budgeon, L.R.2    Culp, T.D.3    Reed, C.A.4    Pickel, M.D.5    Christensen, N.D.6
  • 38
    • 0027050013 scopus 로고
    • Papillomavirus L1 major capsid protein self-assembles into virus-like particles that are highly immunogenic
    • [PubMed]
    • Kirnbauer, R.; Booy, F.; Cheng, N.; Lowy, D.R.; Schiller, J.T. Papillomavirus L1 major capsid protein self-assembles into virus-like particles that are highly immunogenic. Proc. Natl. Acad. Sci. USA 1992, 89, 12180-12184. [PubMed]
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12180-12184
    • Kirnbauer, R.1    Booy, F.2    Cheng, N.3    Lowy, D.R.4    Schiller, J.T.5
  • 39
    • 84941039850 scopus 로고    scopus 로고
    • Papillomavirus infectious pathways: A comparison of systems
    • [CrossRef] [PubMed]
    • Biryukov, J.; Meyers, C. Papillomavirus infectious pathways: A comparison of systems. Viruses 2015, 7, 4303-4325. [CrossRef] [PubMed]
    • (2015) Viruses , vol.7 , pp. 4303-4325
    • Biryukov, J.1    Meyers, C.2
  • 40
    • 70349750271 scopus 로고    scopus 로고
    • Tissue-spanning redox gradient-dependent assembly of native human papillomavirus type 16 virions
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 41
    • 79960449881 scopus 로고    scopus 로고
    • Differentiation-dependent interpentameric disulfide bond stabilizes native human papillomavirus type 16
    • [CrossRef] [PubMed]
    • Conway, M.J.; Cruz, L.; Alam, S.; Christensen, N.D.; Meyers, C. Differentiation-dependent interpentameric disulfide bond stabilizes native human papillomavirus type 16. PLoS ONE 2011, 6, e22427. [CrossRef] [PubMed]
    • (2011) PLoS ONE , vol.6
    • Conway, M.J.1    Cruz, L.2    Alam, S.3    Christensen, N.D.4    Meyers, C.5
  • 43
    • 71149108255 scopus 로고    scopus 로고
    • Inducible heat shock protein 70 enhances HPV31 viral genome replication and virion production during the differentiation-dependent life cycle in human keratinocytes
    • [CrossRef] [PubMed]
    • Song, H.; Moseley, P.L.; Lowe, S.L.; Ozbun, M.A. Inducible heat shock protein 70 enhances HPV31 viral genome replication and virion production during the differentiation-dependent life cycle in human keratinocytes. Virus Res. 2010, 147, 113-122. [CrossRef] [PubMed]
    • (2010) Virus Res. , vol.147 , pp. 113-122
    • Song, H.1    Moseley, P.L.2    Lowe, S.L.3    Ozbun, M.A.4
  • 44
    • 0042337379 scopus 로고    scopus 로고
    • Chaperone-mediated in vitro assembly of polyomavirus capsids
    • [PubMed]
    • Chromy, L.R.; Pipas, J.M.; Garcea, R.L. Chaperone-mediated in vitro assembly of polyomavirus capsids. Proc. Natl. Acad. Sci. USA 2003, 100, 10477-10482. [PubMed]
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10477-10482
    • Chromy, L.R.1    Pipas, J.M.2    Garcea, R.L.3
  • 45
    • 33646444561 scopus 로고    scopus 로고
    • Chaperone-mediated in vitro disassembly of polyoma- and papillomaviruses
    • [CrossRef] [PubMed]
    • Chromy, L.R.; Oltman, A.; Estes, P.A.; Garcea, R.L. Chaperone-mediated in vitro disassembly of polyoma- and papillomaviruses. J. Virol. 2006, 80, 5086-5091. [CrossRef] [PubMed]
    • (2006) J. Virol. , vol.80 , pp. 5086-5091
    • Chromy, L.R.1    Oltman, A.2    Estes, P.A.3    Garcea, R.L.4
  • 46
    • 79951560833 scopus 로고    scopus 로고
    • Cross-neutralization potential of native human papillomavirus N-terminal L2 epitopes
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2011) PLoS ONE , vol.6
    • Conway, M.J.1    Cruz, L.2    Alam, S.3    Christensen, N.D.4    Meyers, C.5
  • 47
    • 42449153250 scopus 로고    scopus 로고
    • Mechanisms of human papillomavirus type 16 neutralization by L2 cross-neutralizing and L1 type-specific antibodies
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (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
  • 48
    • 84879831306 scopus 로고    scopus 로고
    • Differential dependence on host cell glycosaminoglycans for infection of epithelial cells by high-risk HPV types
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2013) PLoS ONE , vol.8
    • Cruz, L.1    Meyers, C.2
  • 49
    • 84930935143 scopus 로고    scopus 로고
    • Human papillomavirus species-specific interaction with the basement membrane-resident non-heparan sulfate receptor
    • [CrossRef] [PubMed]
    • Richards, K.F.; Mukherjee, S.; Bienkowska-Haba, M.; Pang, J.; Sapp, M. Human papillomavirus species-specific interaction with the basement membrane-resident non-heparan sulfate receptor. Viruses 2014, 6, 4856-4879. [CrossRef] [PubMed]
    • (2014) Viruses , vol.6 , pp. 4856-4879
    • Richards, K.F.1    Mukherjee, S.2    Bienkowska-Haba, M.3    Pang, J.4    Sapp, M.5
  • 50
    • 57349115458 scopus 로고    scopus 로고
    • Heparan sulfate-independent cell binding and infection with furin-precleaved papillomavirus capsids
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (2008) J. Virol. , vol.82 , pp. 12565-12568
    • Day, P.M.1    Lowy, D.R.2    Schiller, J.T.3
  • 52
    • 0030245737 scopus 로고    scopus 로고
    • Surface conformational and linear epitopes on HPV-16 and HPV-18 L1 virus-like particles as defined by monoclonal antibodies
    • [CrossRef] [PubMed]
    • Christensen, N.D.; Dillner, J.; Eklund, C.; Carter, J.J.; Wipf, G.C.; Reed, C.A.; Cladel, N.M.; Galloway, D.A. Surface conformational and linear epitopes on HPV-16 and HPV-18 L1 virus-like particles as defined by monoclonal antibodies. Virology 1996, 223, 174-184. [CrossRef] [PubMed]
    • (1996) Virology , vol.223 , pp. 174-184
    • Christensen, N.D.1    Dillner, J.2    Eklund, C.3    Carter, J.J.4    Wipf, G.C.5    Reed, C.A.6    Cladel, N.M.7    Galloway, D.A.8
  • 53
    • 1642446613 scopus 로고    scopus 로고
    • Reactivity of human sera in a sensitive, high-throughput pseudovirus-based papillomavirus neutralization assay for HPV16 and HPV18
    • [CrossRef] [PubMed]
    • Pastrana, D.V.; Buck, C.B.; Pang, Y.Y.; Thompson, C.D.; Castle, P.E.; FitzGerald, P.C.; Kruger Kjaer, S.; Lowy, D.R.; Schiller, J.T. Reactivity of human sera in a sensitive, high-throughput pseudovirus-based papillomavirus neutralization assay for HPV16 and HPV18. Virology 2004, 321, 205-216. [CrossRef] [PubMed]
    • (2004) Virology , vol.321 , pp. 205-216
    • Pastrana, D.V.1    Buck, C.B.2    Pang, Y.Y.3    Thompson, C.D.4    Castle, P.E.5    FitzGerald, P.C.6    Kruger Kjaer, S.7    Lowy, D.R.8    Schiller, J.T.9
  • 54
    • 0032560449 scopus 로고    scopus 로고
    • Alpha1-antitrypsin portland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent
    • [CrossRef] [PubMed]
    • Jean, F.; Stella, K.; Thomas, L.; Liu, G.; Xiang, Y.; Reason, A.J.; Thomas, G. Alpha1-antitrypsin portland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent. Proc. Natl. Acad. Sci. USA 1998, 95, 7293-7298. [CrossRef] [PubMed]
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7293-7298
    • Jean, F.1    Stella, K.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Reason, A.J.6    Thomas, G.7
  • 55
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • [PubMed]
    • 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. [PubMed]
    • (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
  • 56
    • 0034998031 scopus 로고    scopus 로고
    • Proprotein convertase expression and localization in epidermis: Evidence for multiple roles and substrates
    • [CrossRef] [PubMed]
    • Pearton, D.J.; Nirunsuksiri,W.; Rehemtulla, A.; Lewis, S.P.; Presland, R.B.; Dale, B.A. Proprotein convertase expression and localization in epidermis: Evidence for multiple roles and substrates. Exp. Dermatol. 2001, 10, 193-203. [CrossRef] [PubMed]
    • (2001) Exp. Dermatol. , vol.10 , pp. 193-203
    • Pearton, D.J.1    Nirunsuksiri, W.2    Rehemtulla, A.3    Lewis, S.P.4    Presland, R.B.5    Dale, B.A.6
  • 58
    • 0023201247 scopus 로고
    • Identification of proteins encoded by the L1 and L2 open reading frames of human papillomavirus 1a
    • [PubMed]
    • 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. [PubMed]
    • (1987) J. Virol. , vol.61 , pp. 2793-2799
    • Doorbar, J.1    Gallimore, P.H.2
  • 59
    • 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. General Virol. 1989, 70, 1133-1140.
    • (1989) J. General Virol. , vol.70 , pp. 1133-1140
    • Jin, X.W.1    Cowsert, L.M.2    Pilacinski, W.P.3    Jenson, A.B.4
  • 60
    • 0023032821 scopus 로고
    • The L2 open reading frame of human papillomavirus type 1a encodes a minor structural protein carrying type-specific antigens
    • [PubMed]
    • 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. [PubMed]
    • (1986) J. Virol. , vol.60 , pp. 813-816
    • Komly, C.A.1    Breitburd, F.2    Croissant, O.3    Streeck, R.E.4
  • 61
    • 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
    • [CrossRef] [PubMed]
    • 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. General Virol. 1990, 71, 2725-2729. [CrossRef] [PubMed]
    • (1990) J. General Virol. , vol.71 , pp. 2725-2729
    • Rose, R.C.1    Bonnez, W.2    Strike, D.G.3    Reichman, R.C.4
  • 62
    • 0043169726 scopus 로고    scopus 로고
    • Human papillomavirus type 45 propagation, infection, and neutralization
    • [CrossRef]
    • McLaughlin-Drubin, M.E.; Wilson, S.; Mullikin, B.; Suzich, J.; Meyers, C. Human papillomavirus type 45 propagation, infection, and neutralization. Virology 2003, 312, 1-7. [CrossRef]
    • (2003) Virology , vol.312 , pp. 1-7
    • McLaughlin-Drubin, M.E.1    Wilson, S.2    Mullikin, B.3    Suzich, J.4    Meyers, C.5
  • 63
    • 0030820343 scopus 로고    scopus 로고
    • Synthesis of infectious human papillomavirus type 18 in differentiating epithelium transfected with viral dna
    • [PubMed]
    • Meyers, C.; Mayer, T.J.; Ozbun, M.A. Synthesis of infectious human papillomavirus type 18 in differentiating epithelium transfected with viral dna. J. Virol. 1997, 71, 7381-7386. [PubMed]
    • (1997) J. Virol. , vol.71 , pp. 7381-7386
    • Meyers, C.1    Mayer, T.J.2    Ozbun, M.A.3
  • 64
    • 0026671476 scopus 로고
    • Biosynthesis of human papillomavirus from a continuous cell line upon epithelial differentiation
    • [CrossRef] [PubMed]
    • 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. [CrossRef] [PubMed]
    • (1992) Science , vol.257 , pp. 971-973
    • Meyers, C.1    Frattini, M.G.2    Hudson, J.B.3    Laimins, L.A.4
  • 67
    • 0029901601 scopus 로고    scopus 로고
    • Ceramides are transported through the golgi apparatus in human keratinocytes in vitro
    • [CrossRef] [PubMed]
    • Madison, K.C.; Howard, E.J. Ceramides are transported through the golgi apparatus in human keratinocytes in vitro. J. Investig. Dermatol. 1996, 106, 1030-1035. [CrossRef] [PubMed]
    • (1996) J. Investig. Dermatol. , vol.106 , pp. 1030-1035
    • Madison, K.C.1    Howard, E.J.2
  • 68
    • 0035264543 scopus 로고    scopus 로고
    • Transmission of human papillomavirus type 11 infection by desquamated cornified cells
    • [CrossRef] [PubMed]
    • Bryan, J.T.; Brown, D.R. Transmission of human papillomavirus type 11 infection by desquamated cornified cells. Virology 2001, 281, 35-42. [CrossRef] [PubMed]
    • (2001) Virology , vol.281 , pp. 35-42
    • Bryan, J.T.1    Brown, D.R.2
  • 69
    • 60449098831 scopus 로고    scopus 로고
    • Insights into the role and function of L2, the minor capsid protein of papillomaviruses
    • [CrossRef] [PubMed]
    • Pereira, R.; Hitzeroth, I.I.; Rybicki, E.P. Insights into the role and function of L2, the minor capsid protein of papillomaviruses. Arch. Virol. 2009, 154, 187-197. [CrossRef] [PubMed]
    • (2009) Arch. Virol. , vol.154 , pp. 187-197
    • Pereira, R.1    Hitzeroth, I.I.2    Rybicki, E.P.3
  • 70
    • 0028120905 scopus 로고
    • Interaction of human papillomavirus (HPV) type 16 capsid proteins with HPV DNA requires an intact L2 N-terminal sequence
    • [PubMed]
    • Zhou, J.; Sun, X.Y.; Louis, K.; Frazer, I.H. Interaction of human papillomavirus (HPV) type 16 capsid proteins with HPV DNA requires an intact L2 N-terminal sequence. J. Virol. 1994, 68, 619-625. [PubMed]
    • (1994) J. Virol. , vol.68 , pp. 619-625
    • Zhou, J.1    Sun, X.Y.2    Louis, K.3    Frazer, I.H.4
  • 71
    • 33748499815 scopus 로고    scopus 로고
    • Keratinocyte-secreted laminin 5 can function as a transient receptor for human papillomaviruses by binding virions and transferring them to adjacent cells
    • [CrossRef] [PubMed]
    • Culp, T.D.; Budgeon, L.R.; Marinkovich, M.P.; Meneguzzi, G.; Christensen, N.D. Keratinocyte-secreted laminin 5 can function as a transient receptor for human papillomaviruses by binding virions and transferring them to adjacent cells. J. Virol. 2006, 80, 8940-8950. [CrossRef] [PubMed]
    • (2006) J. Virol. , vol.80 , pp. 8940-8950
    • Culp, T.D.1    Budgeon, L.R.2    Marinkovich, M.P.3    Meneguzzi, G.4    Christensen, N.D.5
  • 72
    • 84885419211 scopus 로고    scopus 로고
    • Heparin increases the infectivity of human papillomavirus type 16 independent of cell surface proteoglycans and induces L1 epitope exposure
    • [CrossRef] [PubMed]
    • Cerqueira, C.; Liu, Y.; Kuhling, L.; Chai, W.; Hafezi, W.; van Kuppevelt, T.H.; Kuhn, J.E.; Feizi, T.; Schelhaas, M. Heparin increases the infectivity of human papillomavirus type 16 independent of cell surface proteoglycans and induces L1 epitope exposure. Cell. Microbiol. 2013. [CrossRef] [PubMed]
    • (2013) Cell. Microbiol.
    • Cerqueira, C.1    Liu, Y.2    Kuhling, L.3    Chai, W.4    Hafezi, W.5    van Kuppevelt, T.H.6    Kuhn, J.E.7    Feizi, T.8    Schelhaas, M.9
  • 73
    • 71949096137 scopus 로고    scopus 로고
    • Viral entry mechanisms: Human papillomavirus and a long journey from extracellular matrix to the nucleus
    • [CrossRef] [PubMed]
    • Sapp, M.; Bienkowska-Haba, M. Viral entry mechanisms: Human papillomavirus and a long journey from extracellular matrix to the nucleus. Febs. J. 2009, 276, 7206-7216. [CrossRef] [PubMed]
    • (2009) Febs. J. , vol.276 , pp. 7206-7216
    • Sapp, M.1    Bienkowska-Haba, M.2
  • 74
    • 84880351887 scopus 로고    scopus 로고
    • Human papillomavirus types 16, 18, and 31 share similar endocytic requirements for entry
    • [CrossRef] [PubMed]
    • Spoden, G.; Kuhling, L.; Cordes, N.; Frenzel, B.; Sapp, M.; Boller, K.; Florin, L.; Schelhaas, M. Human papillomavirus types 16, 18, and 31 share similar endocytic requirements for entry. J. Virol. 2013, 87, 7765-7773. [CrossRef] [PubMed]
    • (2013) J. Virol. , vol.87 , pp. 7765-7773
    • Spoden, G.1    Kuhling, L.2    Cordes, N.3    Frenzel, B.4    Sapp, M.5    Boller, K.6    Florin, L.7    Schelhaas, M.8
  • 75
    • 84861207605 scopus 로고    scopus 로고
    • Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis
    • [CrossRef] [PubMed]
    • Schelhaas, M.; Shah, B.; Holzer, M.; Blattmann, P.; Kuhling, L.; Day, P.M.; Schiller, J.T.; Helenius, A. Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis. PLoS Pathog. 2012, 8, e1002657. [CrossRef] [PubMed]
    • (2012) PLoS Pathog. , vol.8
    • Schelhaas, M.1    Shah, B.2    Holzer, M.3    Blattmann, P.4    Kuhling, L.5    Day, P.M.6    Schiller, J.T.7    Helenius, A.8
  • 76
    • 52649120857 scopus 로고    scopus 로고
    • Caveolin-1-dependent infectious entry of human papillomavirus type 31 in human keratinocytes proceeds to the endosomal pathway for ph-dependent uncoating
    • [PubMed]
    • Smith, J.L.; Campos, S.K.; Wandinger-Ness, A.; Ozbun, M.A. Caveolin-1-dependent infectious entry of human papillomavirus type 31 in human keratinocytes proceeds to the endosomal pathway for ph-dependent uncoating. J. Virol. 2008, 82, 9505-9512. [PubMed]
    • (2008) J. Virol. , vol.82 , pp. 9505-9512
    • Smith, J.L.1    Campos, S.K.2    Wandinger-Ness, A.3    Ozbun, M.A.4
  • 77
    • 0037334521 scopus 로고    scopus 로고
    • Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells
    • [CrossRef] [PubMed]
    • Bousarghin, L.; Touze, A.; Sizaret, P.Y.; Coursaget, P. Human papillomavirus types 16, 31, and 58 use different endocytosis pathways to enter cells. J. Virol. 2003, 77, 3846-3850. [CrossRef] [PubMed]
    • (2003) J. Virol. , vol.77 , pp. 3846-3850
    • Bousarghin, L.1    Touze, A.2    Sizaret, P.Y.3    Coursaget, P.4
  • 78
    • 33847685344 scopus 로고    scopus 로고
    • Mechanisms regulating expression of the HPV 31 L1 and L2 capsid proteins and pseudovirion entry
    • [CrossRef] [PubMed]
    • Hindmarsh, P.L.; Laimins, L.A. Mechanisms regulating expression of the HPV 31 L1 and L2 capsid proteins and pseudovirion entry. Virol. J. 2007, 4, 19. [CrossRef] [PubMed]
    • (2007) Virol. J. , vol.4 , pp. 19
    • Hindmarsh, P.L.1    Laimins, L.A.2
  • 79
    • 84860891623 scopus 로고    scopus 로고
    • Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections
    • [PubMed]
    • 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. [PubMed]
    • (2012) PLoS Pathog. , vol.8
    • Surviladze, Z.1    Dziduszko, A.2    Ozbun, M.A.3
  • 80
    • 33644843775 scopus 로고    scopus 로고
    • Generation of HPV pseudovirions using transfection and their use in neutralization assays
    • [PubMed]
    • Buck, C.B.; Pastrana, D.V.; Lowy, D.R.; Schiller, J.T. Generation of HPV pseudovirions using transfection and their use in neutralization assays. Methods Mol. Med. 2005, 119, 445-462. [PubMed]
    • (2005) Methods Mol. Med. , vol.119 , pp. 445-462
    • Buck, C.B.1    Pastrana, D.V.2    Lowy, D.R.3    Schiller, J.T.4
  • 81
    • 0034850163 scopus 로고    scopus 로고
    • Enhancement of capsid gene expression: Preparing the human papillomavirus type 16 major structural gene L1 for DNA vaccination purposes
    • [CrossRef] [PubMed]
    • Leder, C.; Kleinschmidt, J.A.;Wiethe, C.; Muller, M. Enhancement of capsid gene expression: Preparing the human papillomavirus type 16 major structural gene L1 for DNA vaccination purposes. J. Virol. 2001, 75, 9201-9209. [CrossRef] [PubMed]
    • (2001) J. Virol. , vol.75 , pp. 9201-9209
    • Leder, C.1    Kleinschmidt, J.A.2    Wiethe, C.3    Muller, M.4
  • 82
    • 33750715451 scopus 로고    scopus 로고
    • Papillomavirus particles assembled in 293tt cells are infectious in vivo
    • [CrossRef] [PubMed]
    • Culp, T.D.; Cladel, N.M.; Balogh, K.K.; Budgeon, L.R.; Mejia, A.F.; Christensen, N.D. Papillomavirus particles assembled in 293tt cells are infectious in vivo. J. Virol. 2006, 80, 11381-11384. [CrossRef] [PubMed]
    • (2006) J. Virol. , vol.80 , pp. 11381-11384
    • Culp, T.D.1    Cladel, N.M.2    Balogh, K.K.3    Budgeon, L.R.4    Mejia, A.F.5    Christensen, N.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.