메뉴 건너뛰기




Volumn 310, Issue 2, 2003, Pages 310-318

Specific in vitro cleavage of Mason-Pfizer monkey virus capsid protein: Evidence for a potential role of retroviral protease in early stages of infection

Author keywords

HIV 1 capsid protein; HIV I protease; M PMV capsid nucleocapsid fusion protein; M PMV protease; Processing

Indexed keywords

PEPTIDE; PROTEINASE; VIRUS ENZYME; VIRUS PROTEIN; CAPSID PROTEIN; GAG PROTEIN;

EID: 0037664350     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0042-6822(03)00128-4     Document Type: Article
Times cited : (32)

References (49)
  • 1
    • 2642607039 scopus 로고    scopus 로고
    • A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 gag precursor is crucial for viral particle assembly
    • Accola, M.A., Höglund, S., Göttlinger, H.G., 1998. A putative α-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 gag precursor is crucial for viral particle assembly. J. Virol. 72, 2072-2078.
    • (1998) J. Virol. , vol.72 , pp. 2072-2078
    • Accola, M.A.1    Höglund, S.2    Göttlinger, H.G.3
  • 2
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type I capsid-p2 and a late assembly domain
    • Accola, M.A., Strack, B., Gottlinger, H.G., 2000. Efficient particle production by minimal gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type I capsid-p2 and a late assembly domain. J. Virol. 74, 5395-5402.
    • (2000) J. Virol. , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 3
    • 0030586691 scopus 로고    scopus 로고
    • Amino acid substitution in the CA protein of Moloney murine leukemia virus that block early events in infection
    • Alin, K., Goff, S.P., 1996. Amino acid substitution in the CA protein of Moloney murine leukemia virus that block early events in infection. Virology 222, 339-351.
    • (1996) Virology , vol.222 , pp. 339-351
    • Alin, K.1    Goff, S.P.2
  • 4
    • 0033106192 scopus 로고    scopus 로고
    • Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of H1V-I capsid protein (p24) complexed with a monoclonal antibody Fab
    • Berthet-Colominas, C., Novelli, A., Sibai, G., Mallet, F., Cusack, S., 1999. Head-to-tail dimers and interdomain flexibility revealed by the crystal structure of H1V-I capsid protein (p24) complexed with a monoclonal antibody Fab. EMBO J. 18, 1124-1136.
    • (1999) EMBO J. , vol.18 , pp. 1124-1136
    • Berthet-Colominas, C.1    Novelli, A.2    Sibai, G.3    Mallet, F.4    Cusack, S.5
  • 6
    • 0034954578 scopus 로고    scopus 로고
    • Second-site suppressors of Rous sarcoma vires CA mutations: Evidence for interdomain interactions
    • Bowzard, J.B., Wills, J.W., Craven, R.C., 2001. Second-site suppressors of Rous sarcoma vires CA mutations: evidence for interdomain interactions. J. Virol. 75, 6850-6856.
    • (2001) J. Virol. , vol.75 , pp. 6850-6856
    • Bowzard, J.B.1    Wills, J.W.2    Craven, R.C.3
  • 7
    • 0022642297 scopus 로고
    • Polypeptides of Mason-Pfizer monkey virus
    • Bradac, J., Hunter, E., 1986a. Polypeptides of Mason-Pfizer monkey virus. Virology 150, 491-502.
    • (1986) Virology , vol.150 , pp. 491-502
    • Bradac, J.1    Hunter, E.2
  • 8
    • 0022636806 scopus 로고
    • Short communications. Polypeptides of Mason-Pfizer monkey virus. Ill. Translational order of proteins on the gag and env gene specified precursor polypeptides
    • Bradac, J.A., Hunter, E., 1986b. Short communications. Polypeptides of Mason-Pfizer monkey virus. Ill. Translational order of proteins on the gag and env gene specified precursor polypeptides. Virology 150, 503-508.
    • (1986) Virology , vol.150 , pp. 503-508
    • Bradac, J.A.1    Hunter, E.2
  • 9
    • 0034751087 scopus 로고    scopus 로고
    • Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants
    • Cairns, T.M., Craven, R.C., 2001. Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants. J. Virol. 75, 242-250.
    • (2001) J. Virol. , vol.75 , pp. 242-250
    • Cairns, T.M.1    Craven, R.C.2
  • 10
    • 0034681298 scopus 로고    scopus 로고
    • Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses
    • Campos-Otivas, R., Newman, J.L., Summers, M.F., 2000. Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J. Mol. Biol. 296, 633-649.
    • (2000) J. Mol. Biol. , vol.296 , pp. 633-649
    • Campos-Otivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 11
    • 0032190245 scopus 로고    scopus 로고
    • Solution structures of human immunodeficiency virus type 1 (HIV-1) and Moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy
    • Clish, C.B., Peyton, D.H., Barklis, E., 1998. Solution structures of human immunodeficiency virus type 1 (HIV-1) and Moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy. Eur. J. Biochem. 257, 69-77.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 69-77
    • Clish, C.B.1    Peyton, D.H.2    Barklis, E.3
  • 12
    • 0035793720 scopus 로고    scopus 로고
    • Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
    • Comilescu, C.C., Bouamr, F., Yao, X., Carter, C., Tjandra, N., 2001. Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein. J. Mol. Biol. 306, 783-797.
    • (2001) J. Mol. Biol. , vol.306 , pp. 783-797
    • Cornilescu, C.C.1    Bouamr, F.2    Yao, X.3    Carter, C.4    Tjandra, N.5
  • 13
    • 0027236919 scopus 로고
    • Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag protein
    • Craven, R.C., Leure-duPree, A.E., Erdie, C.R., Wilson, C.B., Wills, J.W., 1993. Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag protein. J. Virol. 67, 6246-6252.
    • (1993) J. Virol. , vol.67 , pp. 6246-6252
    • Craven, R.C.1    Leure-duPree, A.E.2    Erdie, C.R.3    Wilson, C.B.4    Wills, J.W.5
  • 14
    • 0029015825 scopus 로고
    • Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein
    • Craven, R.C., Leure-duPree, A.E., Weldon Jr., R.A., Wills, J.W., 1995. Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein. J. Virol. 69, 4213-4227.
    • (1995) J. Virol. , vol.69 , pp. 4213-4227
    • Craven, R.C.1    Leure-duPree, A.E.2    Weldon Jr., R.A.3    Wills, J.W.4
  • 15
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman, T., Bukovsky, A., Ohagen, A., Hoglung, S., Gottlinger, H.G., 1994. Functional domains of the capsid protein of human immunodeficiency virus type 1. J. Virol. 68, 8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglung, S.4    Gottlinger, H.G.5
  • 16
    • 0025010060 scopus 로고
    • Expression in Escherichia coli and purification of human immunodeficiency virus type I capsid protein (p24)
    • Ehrlich, L.S., Krausslich, H.G., Wimmer, E., Carter, C.A., 1990. Expression in Escherichia coli and purification of human immunodeficiency virus type I capsid protein (p24). AIDS Res. Hum. Retroviruses 6, 1169-1175.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 1169-1175
    • Ehrlich, L.S.1    Krausslich, H.G.2    Wimmer, E.3    Carter, C.A.4
  • 17
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey, B.M., von Schwedler, U., Sundquist, W.I., Aiken, Ch., 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76, 5667-5677.
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, Ch.4
  • 19
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti, R.K., Lee, B.M., Walker, J., Summers, M.F., Yoo, S., Sundquist, W.I., 1996. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 273, 231-235.
    • (1996) Science , vol.273 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5    Sundquist, W.I.6
  • 20
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Göttlinger, H.G., Sodroski, J.G., Haseltine, W.A., 1989. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 86, 5781-578.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5578
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 23
    • 0022239332 scopus 로고
    • Purification and N-terminal amino acid sequence comparisons of structural proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus
    • Henderson, L.E., Sowder, R., Smythers, G., Benveniste, R.E., Oroszlan, S., 1985. Purification and N-terminal amino acid sequence comparisons of structural proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus. J. Virol. 55, 778-787.
    • (1985) J. Virol. , vol.55 , pp. 778-787
    • Henderson, L.E.1    Sowder, R.2    Smythers, G.3    Benveniste, R.E.4    Oroszlan, S.5
  • 24
    • 0023152815 scopus 로고
    • Chemical and immunological characterization of equine infectious anemia virus gag-encoded proteins
    • Henderson, L.E., Sowder, R.C., Smythers, G.W., Oroszlan, S., 1987. Chemical and immunological characterization of equine infectious anemia virus gag-encoded proteins. J. Virol. 61, 1116-1124.
    • (1987) J. Virol. , vol.61 , pp. 1116-1124
    • Henderson, L.E.1    Sowder, R.C.2    Smythers, G.W.3    Oroszlan, S.4
  • 26
    • 0033548068 scopus 로고    scopus 로고
    • Model for lentivirus capsid core assembly based on crystal dimers of E1AV p26
    • Jin, Z., Jin, L., Peterson, D.L, Lawson, C.L., 1999. Model for lentivirus capsid core assembly based on crystal dimers of E1AV p26. J. Mol. Biol. 286, 83-93.
    • (1999) J. Mol. Biol. , vol.286 , pp. 83-93
    • Jin, Z.1    Jin, L.2    Peterson, D.L.3    Lawson, C.L.4
  • 27
    • 0032781006 scopus 로고    scopus 로고
    • Solution structure of the capsid protein from the human T-cell leukemia virus type-I
    • Khorasanizadeh, S., Campos-Olivas, R., Summers, MF., 1999. Solution structure of the capsid protein from the human T-cell leukemia virus type-I. J. Mol. Biol. 291, 491-505.
    • (1999) J. Mol. Biol. , vol.291 , pp. 491-505
    • Khorasanizadeh, S.1    Campos-Olivas, R.2    Summers, M.F.3
  • 29
    • 0034605035 scopus 로고    scopus 로고
    • Analysis of Qa1b peptide binding specificity and the capacity of CD94/NKG2A to discriminate between Qa-1-peptide complexes
    • Kraft, J.R., Vance, R.E., Pohl, J., Martin, A.M., Raulet, D.H., Jensen, P.E., 2000. Analysis of Qa1b peptide binding specificity and the capacity of CD94/NKG2A to discriminate between Qa-1-peptide complexes. J. Exp. Med. 192, 613-624.
    • (2000) J. Exp. Med. , vol.192 , pp. 613-624
    • Kraft, J.R.1    Vance, R.E.2    Pohl, J.3    Martin, A.M.4    Raulet, D.H.5    Jensen, P.E.6
  • 30
    • 0029013585 scopus 로고
    • The spacer peptide between human immunodeficiency vires capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity
    • Krausslich, H.-G., Facke, M., Heuser, A.M., Konvalinka, J., Zentgraf., H., 1995. The spacer peptide between human immunodeficiency vires capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity. J. Virol. 69, 3407-3419.
    • (1995) J. Virol. , vol.69 , pp. 3407-3419
    • Krausslich, H.-G.1    Facke, M.2    Heuser, A.M.3    Konvalinka, J.4    Zentgraf, H.5
  • 31
    • 0035807841 scopus 로고    scopus 로고
    • Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro
    • Parker, S.D., Hunter, E., 2001. Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro. Microbiology 98, 14631-14636.
    • (2001) Microbiology , vol.98 , pp. 14631-14636
    • Parker, S.D.1    Hunter, E.2
  • 32
    • 0029166751 scopus 로고
    • Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses
    • Pepinsky, R.B., Papayannopoulos, I.A., Chow, E.P., Krishna, N.K., Craven, R.C., Vogt, V.M., 1995. Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses. J. Virol. 69, 6430-6438.
    • (1995) J. Virol. , vol.69 , pp. 6430-6438
    • Pepinsky, R.B.1    Papayannopoulos, I.A.2    Chow, E.P.3    Krishna, N.K.4    Craven, R.C.5    Vogt, V.M.6
  • 33
    • 0027971621 scopus 로고
    • The p2 domain of human immunodeficiency virus type I Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
    • Pettit, S.C., Moody, M.D., Wehbie, R.S., Kaplan, A.H., Nantermet, P.V., Klein, C.A., Swanstrom, R., 1994. The p2 domain of human immunodeficiency virus type I Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J. Virol. 68, 8017-8027.
    • (1994) J. Virol. , vol.68 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Wehbie, R.S.3    Kaplan, A.H.4    Nantermet, P.V.5    Klein, C.A.6    Swanstrom, R.7
  • 35
    • 0028873674 scopus 로고
    • Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: Effects on viral particle assembly, release, and infectivity
    • Reicin, A.S., Paik, S., Berkowitz, R.D., Luban, J., Lowy, I., Goff, S., 1995. Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on viral particle assembly, release, and infectivity. J. Virol. 69, 642-650.
    • (1995) J. Virol. , vol.69 , pp. 642-650
    • Reicin, A.S.1    Paik, S.2    Berkowitz, R.D.3    Luban, J.4    Lowy, I.5    Goff, S.6
  • 36
    • 0034805366 scopus 로고    scopus 로고
    • Comparison of classical and affinity purification techniques of Mason-Pfizer monkey virus capsid protein: The alteration of the product by an affinity tag
    • Rumlová, M., Benediková, J., Cubinková, R., Pichová, I., Ruml, T., 2001. Comparison of classical and affinity purification techniques of Mason-Pfizer monkey virus capsid protein: the alteration of the product by an affinity tag. Prot. Expr. Purif. 23, 75-83.
    • (2001) Prot. Expr. Purif. , vol.23 , pp. 75-83
    • Rumlová, M.1    Benediková, J.2    Cubinková, R.3    Pichová, I.4    Ruml, T.5
  • 38
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. 1. Papain
    • Schechter, 1., Berger, A., 1967. On the size of the active site in proteases. 1. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 39
    • 0034856077 scopus 로고    scopus 로고
    • Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type I RNA dimer maturation
    • Shehu-Xhilaga, M., Kraeusslich, H.-G., Pettit, S., Swanstrom, R., Lee, J.Y., Marshall, J.A., Crowe, S.M., Mak, J., 2001. Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type I RNA dimer maturation. J. Virol. 75, 9156-9164.
    • (2001) J. Virol. , vol.75 , pp. 9156-9164
    • Shehu-Xhilaga, M.1    Kraeusslich, H.-G.2    Pettit, S.3    Swanstrom, R.4    Lee, J.Y.5    Marshall, J.A.6    Crowe, S.M.7    Mak, J.8
  • 40
    • 0022530849 scopus 로고
    • Nucleotide-sequence of Mason-Pfizer monkey virus - An immunosuppressive D-type retrovirus
    • Sonigo, P., Barker, C., Hunter, E., Wainhobson, S., 1986. Nucleotide-sequence of Mason-Pfizer monkey virus - an immunosuppressive D-type retrovirus. Cell 45, 375-385.
    • (1986) Cell , vol.45 , pp. 375-385
    • Sonigo, P.1    Barker, C.2    Hunter, E.3    Wainhobson, S.4
  • 41
    • 0026465274 scopus 로고
    • Mutational analysis of the major homology region of Mason-Pfizer monkey virus by use of saturation mutagenesis
    • Strambio-de-Castillia, C., Hunter, E., 1992. Mutational analysis of the major homology region of Mason-Pfizer monkey virus by use of saturation mutagenesis. J. Virol. 66, 7021-7032.
    • (1992) J. Virol. , vol.66 , pp. 7021-7032
    • Strambio-de-Castillia, C.1    Hunter, E.2
  • 42
    • 0027944219 scopus 로고
    • Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor polypeptide
    • Tobin, G.J., Sowder, R.C., Fabris, D., Hu, M.Y., Battles, J.K., Fenselau, C., Henderson, L.E., Gonda, M.A., 1994. Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor polypeptide. J. Virol. 68, 7620-7627.
    • (1994) J. Virol. , vol.68 , pp. 7620-7627
    • Tobin, G.J.1    Sowder, R.C.2    Fabris, D.3    Hu, M.Y.4    Battles, J.K.5    Fenselau, C.6    Henderson, L.E.7    Gonda, M.A.8
  • 43
    • 0030815316 scopus 로고    scopus 로고
    • HIV-1 protease does not play a critical role in the early stages of HIV-1 infection
    • Uchida, H., Maeda, Y., Mitsuya, H., 1997. HIV-1 protease does not play a critical role in the early stages of HIV-1 infection. Antiviral Res. 36, 107-113.
    • (1997) Antiviral Res. , vol.36 , pp. 107-113
    • Uchida, H.1    Maeda, Y.2    Mitsuya, H.3
  • 45
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers, K., Rutter, G., Kottler, H., Tessmer, U., Hohenberg, H., Krausslich, H-G., 1998. Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J. Virol. 72, 2846-2854.
    • (1998) J. Virol. , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Krausslich, H.-G.6
  • 46
    • 0025728301 scopus 로고
    • Form, function and use of retroviral gag proteins
    • Wills, J.W., Craven, R.C., 1991. Form, function and use of retroviral gag proteins. AIDS 5, 639-65.
    • (1991) AIDS , vol.5 , pp. 639-665
    • Wills, J.W.1    Craven, R.C.2
  • 48
    • 0034968789 scopus 로고    scopus 로고
    • Proper processing of avian sarcoma/leukosis virus capsid proteins is required for infectivity
    • Xiang, Y, Thorick, R, Vana, ML, Craven, R, Leis, J., 2001. Proper processing of avian sarcoma/leukosis virus capsid proteins is required for infectivity. J. Virol. 75, 6016-21.
    • (2001) J. Virol. , vol.75 , pp. 6016-6021
    • Xiang, Y.1    Thorick, R.2    Vana, M.L.3    Craven, R.4    Leis, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.