메뉴 건너뛰기




Volumn 81, Issue 17, 2007, Pages 9396-9407

Structural features of the scaffold interaction domain at the N terminus of the major capsid protein (VP5) of herpes simplex virus type 1

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CAPSID PROTEIN; DOUBLE STRANDED DNA; PROLINE; PROTEIN VP5; UNCLASSIFIED DRUG; VALINE;

EID: 34548175920     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00986-07     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 0041347832 scopus 로고    scopus 로고
    • Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics
    • Baker, M. L., W. Jiang, B. R. Bowman, Z. H. Zhou, F. A. Quiocho, F. J. Rixon, and W. Chlu. 2003. Architecture of the herpes simplex virus major capsid protein derived from structural bioinformatics. J. Mol. Biol. 331:447-456.
    • (2003) J. Mol. Biol , vol.331 , pp. 447-456
    • Baker, M.L.1    Jiang, W.2    Bowman, B.R.3    Zhou, Z.H.4    Quiocho, F.A.5    Rixon, F.J.6    Chlu, W.7
  • 2
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker, M. L., W. Jiang, F. J. Rixon, and W. Chiu. 2005. Common ancestry of herpesviruses and tailed DNA bacteriophages. J. Virol. 79:14967-14970.
    • (2005) J. Virol , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 3
    • 0029843595 scopus 로고    scopus 로고
    • Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursor
    • Beaudet-Miller, M., R. Zhang, J. Durkin, W. Gibson, A. D. Kwong, and Z. Hong. 1996. Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursor. J. Virol. 70:8081-8088.
    • (1996) J. Virol , vol.70 , pp. 8081-8088
    • Beaudet-Miller, M.1    Zhang, R.2    Durkin, J.3    Gibson, W.4    Kwong, A.D.5    Hong, Z.6
  • 6
    • 0027511720 scopus 로고
    • Mutations in herpes simplex virus type 1 genes encoding VPS and VP23 abrogate capsid formation and cleavage of replicated DNA
    • Desai, P., N. A. DeLuca, J. C. Glorioso, and S. Person. 1993. Mutations in herpes simplex virus type 1 genes encoding VPS and VP23 abrogate capsid formation and cleavage of replicated DNA. J. Virol. 67:1357-1364.
    • (1993) J. Virol , vol.67 , pp. 1357-1364
    • Desai, P.1    DeLuca, N.A.2    Glorioso, J.C.3    Person, S.4
  • 7
    • 17344386043 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 VP26 is not essential for replication in cell culture but influences production of infectious virus in the nervous system of infected mice
    • Desai, P., N. A. DeLuca, and S. Person. 1998. Herpes simplex virus type 1 VP26 is not essential for replication in cell culture but influences production of infectious virus in the nervous system of infected mice. Virology 247:115-124.
    • (1998) Virology , vol.247 , pp. 115-124
    • Desai, P.1    DeLuca, N.A.2    Person, S.3
  • 8
    • 0028145083 scopus 로고
    • A genetic selection method for the transfer of HSV-1 glycoprotein B mutations from plasmid to the viral genome: Preliminary characterization of transdominance and entry kinetics of mutant viruses
    • Desai, P., F. L. Homa, S. Person, and J. C. Glorioso. 1994. A genetic selection method for the transfer of HSV-1 glycoprotein B mutations from plasmid to the viral genome: preliminary characterization of transdominance and entry kinetics of mutant viruses. Virology 204:312-322.
    • (1994) Virology , vol.204 , pp. 312-322
    • Desai, P.1    Homa, F.L.2    Person, S.3    Glorioso, J.C.4
  • 9
    • 0029892968 scopus 로고    scopus 로고
    • Molecular interactions between the HSV-1 capsid proteins as measured by the yeast two-hybrid system
    • Desai, P., and S. Person. 1996. Molecular interactions between the HSV-1 capsid proteins as measured by the yeast two-hybrid system. Virology 220:516-521.
    • (1996) Virology , vol.220 , pp. 516-521
    • Desai, P.1    Person, S.2
  • 10
    • 0033198645 scopus 로고    scopus 로고
    • Second site mutations in the N-terminus of the major capsid protein (VPS) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1
    • Desai, P., and S. Person. 1999. Second site mutations in the N-terminus of the major capsid protein (VPS) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1. Virology 261:357-366.
    • (1999) Virology , vol.261 , pp. 357-366
    • Desai, P.1    Person, S.2
  • 11
    • 0028067308 scopus 로고
    • The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame
    • Desai, P., S. C. Watkins, and S. Person. 1994. The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frame. J. Virol. 68:5365-5374.
    • (1994) J. Virol , vol.68 , pp. 5365-5374
    • Desai, P.1    Watkins, S.C.2    Person, S.3
  • 12
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 13
    • 0015427631 scopus 로고
    • Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2
    • Gibson, W., and B. Roizman. 1972. Proteins specified by herpes simplex virus. 8. Characterization and composition of multiple capsid forms of subtypes 1 and 2. J. Virol. 10:1044-1052.
    • (1972) J. Virol , vol.10 , pp. 1044-1052
    • Gibson, W.1    Roizman, B.2
  • 14
    • 0029921211 scopus 로고    scopus 로고
    • Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: Leucine 66 to proline and leucine 91 to proline
    • Gray, T. M., E. J. Arnoys, S. Blankespoor, T. Born, R. Jagar, R. Everman, D. Plowman, A. Stair, and D. Zhang. 1996. Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. Protein Sci. 5:742-751.
    • (1996) Protein Sci , vol.5 , pp. 742-751
    • Gray, T.M.1    Arnoys, E.J.2    Blankespoor, S.3    Born, T.4    Jagar, R.5    Everman, R.6    Plowman, D.7    Stair, A.8    Zhang, D.9
  • 15
    • 0027467164 scopus 로고
    • Disruption of endoplasmic reticulum to Golgi transport leads to the accumulation of large aggregates containing beta-COP in pancreatic acinar cells
    • Hendricks, L. C., M. McCaffery, G. E. Palade, and M. G. Farquhar. 1993. Disruption of endoplasmic reticulum to Golgi transport leads to the accumulation of large aggregates containing beta-COP in pancreatic acinar cells. Mol. Biol. Cell 4:413-424.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 413-424
    • Hendricks, L.C.1    McCaffery, M.2    Palade, G.E.3    Farquhar, M.G.4
  • 16
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
    • Heymann, J. B., N. Cheng, W. W. Newcomb, B. L. Trus, J. C. Brown, and A. C. Steven. 2003. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat. Struct. Biol. 10:334-341.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 17
    • 0029655959 scopus 로고    scopus 로고
    • Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein
    • Hong, Z., M. Beaudet-Miller, J. Durkin, R. Zhang, and A. D. Kwong. 1996. Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein. J. Virol. 70:533-540.
    • (1996) J. Virol , vol.70 , pp. 533-540
    • Hong, Z.1    Beaudet-Miller, M.2    Durkin, J.3    Zhang, R.4    Kwong, A.D.5
  • 18
    • 0029007025 scopus 로고
    • The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold
    • Kennard, J., F. J. Rixon, I. M. McDougall, J. D. Tatman, and V. G. Preston. 1995. The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold. J. Gen. Virol. 76:1611-1621.
    • (1995) J. Gen. Virol , vol.76 , pp. 1611-1621
    • Kennard, J.1    Rixon, F.J.2    McDougall, I.M.3    Tatman, J.D.4    Preston, V.G.5
  • 19
    • 0029015830 scopus 로고
    • The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids
    • Matusick-Kumar, L., W. W. Newcomb, J. C. Brown, P. J. McCann III, W. Hurlburt, S. P. Weinheimer, and M. Gao. 1995. The C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsids. J. Virol. 69:4347-4356.
    • (1995) J. Virol , vol.69 , pp. 4347-4356
    • Matusick-Kumar, L.1    Newcomb, W.W.2    Brown, J.C.3    McCann III, P.J.4    Hurlburt, W.5    Weinheimer, S.P.6    Gao, M.7
  • 20
    • 0030298322 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: Characterization of intermediates observed during cell-free capsid formation
    • Newcomb, W. W., F. L. Homa, D. R. Thomsen, F. P. Booy, B. L. Trus, A. C. Steven, J. V. Spencer, and J. C. Brown. 1996. Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation. J. Mol. Biol. 263:432-446.
    • (1996) J. Mol. Biol , vol.263 , pp. 432-446
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Booy, F.P.4    Trus, B.L.5    Steven, A.C.6    Spencer, J.V.7    Brown, J.C.8
  • 21
    • 0028210056 scopus 로고
    • Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a
    • Nicholson, P., C. Addison, A. M. Cross, J. Kennard, V. G. Preston, and F. J. Rixon. 1994. Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a. J. Gen. Virol. 75:1091-1099.
    • (1994) J. Gen. Virol , vol.75 , pp. 1091-1099
    • Nicholson, P.1    Addison, C.2    Cross, A.M.3    Kennard, J.4    Preston, V.G.5    Rixon, F.J.6
  • 22
    • 0031026433 scopus 로고    scopus 로고
    • Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: Critical role of the C terminus
    • Oien, N. L., D. R. Thomsen, M. W. Wathen, W. W. Newcomb, J. C. Brown, and F. L. Homa. 1997. Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminus. J. Virol. 71:1281-1291.
    • (1997) J. Virol , vol.71 , pp. 1281-1291
    • Oien, N.L.1    Thomsen, D.R.2    Wathen, M.W.3    Newcomb, W.W.4    Brown, J.C.5    Homa, F.L.6
  • 23
    • 0032029782 scopus 로고    scopus 로고
    • Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C)
    • Person, S., and P. Desai. 1998. Capsids are formed in a mutant virus blocked at the maturation site of the UL26 and UL26.5 open reading frames of herpes simplex virus type 1 but are not formed in a null mutant of UL38 (VP19C). Virology 242:193-203.
    • (1998) Virology , vol.242 , pp. 193-203
    • Person, S.1    Desai, P.2
  • 25
    • 0344118125 scopus 로고    scopus 로고
    • Thermodynamic effects of replacements of Pro residues in helix interiors of maltose-binding protein
    • Prajapati, R. S., G. M. Lingaraju, K. Bacchawat, A. Surolia, and R. Varadarajan. 2003. Thermodynamic effects of replacements of Pro residues in helix interiors of maltose-binding protein. Proteins 53:863-871.
    • (2003) Proteins , vol.53 , pp. 863-871
    • Prajapati, R.S.1    Lingaraju, G.M.2    Bacchawat, K.3    Surolia, A.4    Varadarajan, R.5
  • 26
    • 0001315638 scopus 로고
    • Structure and assembly of herpesviruses
    • Rixon, F. J. 1993. Structure and assembly of herpesviruses. Semin. Virology. 4:135-144.
    • (1993) Semin. Virology , vol.4 , pp. 135-144
    • Rixon, F.J.1
  • 27
    • 0029840591 scopus 로고    scopus 로고
    • Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins
    • Rixon, F. J., C. Addison, A. McGregor, S. J. Macnab, P. Nicholson, V. G. Preston, and J. D. Tatman. 1996. Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins. J. Gen. Virol. 77:2251-2260.
    • (1996) J. Gen. Virol , vol.77 , pp. 2251-2260
    • Rixon, F.J.1    Addison, C.2    McGregor, A.3    Macnab, S.J.4    Nicholson, P.5    Preston, V.G.6    Tatman, J.D.7
  • 28
    • 0000595684 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley ed, 3rd ed. Lippincott-Raven, Philadelphia, PA
    • Roizman, B., and A. Sears. 1996. Herpes simplex viruses and their replication, p. 2223-2295. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven, Philadelphia, PA.
    • (1996) Fields virology , pp. 2223-2295
    • Roizman, B.1    Sears, A.2
  • 29
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 31
    • 0021112868 scopus 로고
    • Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure
    • Sweet, R. M., and D. Eisenberg. 1983. Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. J. Mol. Biol. 171:479-488.
    • (1983) J. Mol. Biol , vol.171 , pp. 479-488
    • Sweet, R.M.1    Eisenberg, D.2
  • 32
    • 0028256487 scopus 로고
    • Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses
    • Tatman, J. D., V. G. Preston, P. Nicholson, R. M. Elliott, and F. J. Rixon. 1994. Assembly of herpes simplex virus type 1 capsids using a panel of recombinant baculoviruses. J. Gen. Virol. 75:1101-1113.
    • (1994) J. Gen. Virol , vol.75 , pp. 1101-1113
    • Tatman, J.D.1    Preston, V.G.2    Nicholson, P.3    Elliott, R.M.4    Rixon, F.J.5
  • 33
    • 0029019922 scopus 로고
    • Assembly of the herpes simplex virus capsid: Requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes
    • Thomsen, D. R., W. W. Newcomb, J. C. Brown, and F. L. Homa. 1995. Assembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes. J. Virol. 69:3690-3703.
    • (1995) J. Virol , vol.69 , pp. 3690-3703
    • Thomsen, D.R.1    Newcomb, W.W.2    Brown, J.C.3    Homa, F.L.4
  • 34
    • 0028345731 scopus 로고
    • Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins
    • Thomsen, D. R., L. L. Roof, and F. L. Homa. 1994. Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins. J. Virol. 68:2442-2457.
    • (1994) J. Virol , vol.68 , pp. 2442-2457
    • Thomsen, D.R.1    Roof, L.L.2    Homa, F.L.3
  • 35
    • 0029908793 scopus 로고    scopus 로고
    • The herpes simplex virus procapsid: Structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
    • Trus, B. L., F. P. Booy, W. W. Newcomb, J. C. Brown, F. L. Homa, D. R. Thomsen, and A. C. Steven. 1996. The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 263:447-462.
    • (1996) J. Mol. Biol , vol.263 , pp. 447-462
    • Trus, B.L.1    Booy, F.P.2    Newcomb, W.W.3    Brown, J.C.4    Homa, F.L.5    Thomsen, D.R.6    Steven, A.C.7
  • 36
    • 0037379174 scopus 로고    scopus 로고
    • Mutation of single hydrophobic residue 127, L35, F39, L58, L65, L67, or L71 in the N terminus of VP5 abolishes interaction with the scaffold protein and prevents closure of herpes simplex virus type 1 capsid shells
    • Walters, J. N., G. L. Sexton, J. M. McCaffery, and P. Desai. 2003. Mutation of single hydrophobic residue 127, L35, F39, L58, L65, L67, or L71 in the N terminus of VP5 abolishes interaction with the scaffold protein and prevents closure of herpes simplex virus type 1 capsid shells. J. Virol. 77:4043-4059.
    • (2003) J. Virol , vol.77 , pp. 4043-4059
    • Walters, J.N.1    Sexton, G.L.2    McCaffery, J.M.3    Desai, P.4
  • 37
    • 0034610231 scopus 로고    scopus 로고
    • Second-site mutations encoding residues 34 and 78 of the major capsid protein (VPS) of herpes simplex virus type 1 are important for overcoming a blocked maturation cleavage site of the capsid scaffold proteins
    • Warner, S. C., P. Desai, and S. Person. 2000. Second-site mutations encoding residues 34 and 78 of the major capsid protein (VPS) of herpes simplex virus type 1 are important for overcoming a blocked maturation cleavage site of the capsid scaffold proteins. Virology 278:217-226.
    • (2000) Virology , vol.278 , pp. 217-226
    • Warner, S.C.1    Desai, P.2    Person, S.3
  • 38
    • 0031060532 scopus 로고    scopus 로고
    • Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains
    • Wood, L. J., M. K. Baxter, S. M. Plafker, and W. Gibson. 1997. Human cytomegalovirus capsid assembly protein precursor (pUL80.5) interacts with itself and with the major capsid protein (pUL86) through two different domains. J. Virol. 71:179-190.
    • (1997) J. Virol , vol.71 , pp. 179-190
    • Wood, L.J.1    Baxter, M.K.2    Plafker, S.M.3    Gibson, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.