메뉴 건너뛰기




Volumn 318, Issue 2, 2004, Pages 534-541

The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles

Author keywords

Autoprocessing; Gag Pol; HIV PR

Indexed keywords

GAG PROTEIN; PROTEINASE; VIRUS DNA;

EID: 1242328733     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2003.08.043     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0029097067 scopus 로고
    • Potent inhibition of human immunodeficiency virus type 1 (HIV-1) replication by inducible expression of HIV-1 PR multimers
    • Arrigo S.J., Huffman K. Potent inhibition of human immunodeficiency virus type 1 (HIV-1) replication by inducible expression of HIV-1 PR multimers. J. Virol. 69:1995;5988-5994.
    • (1995) J. Virol. , vol.69 , pp. 5988-5994
    • Arrigo, S.J.1    Huffman, K.2
  • 2
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
    • Bennett R., Nelle T.D., Wills J.W. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins. J. Virol. 67:1993;6487-6498.
    • (1993) J. Virol. , vol.67 , pp. 6487-6498
    • Bennett, R.1    Nelle, T.D.2    Wills, J.W.3
  • 3
    • 0025985690 scopus 로고
    • Assembly and processing of avian retroviral gag polyproteins containing linked protease dimers
    • Burstein H., Bizub D., Skalka A.M. Assembly and processing of avian retroviral gag polyproteins containing linked protease dimers. J. Virol. 64:1991;6156-6172.
    • (1991) J. Virol. , vol.64 , pp. 6156-6172
    • Burstein, H.1    Bizub, D.2    Skalka, A.M.3
  • 6
    • 0032506207 scopus 로고    scopus 로고
    • HIV Gag proteins: Diverse functions in the virus life cycle
    • Freed E.O. HIV Gag proteins: diverse functions in the virus life cycle. Virology. 251:1998;1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 7
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristylation in morphogenesis and infectivity of human immunodeficiency virus 1
    • Gottlinger H.G., Sodroski J.G., Haseltine W.A. Role of capsid precursor processing and myristylation in morphogenesis and infectivity of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. U.S.A. 86:1989;5781-5785.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 8
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processing, and complete amino acid sequences
    • Henderson L.E., Bowers M.A., Sowder R.C. II, Serabyn S.A., Johnson D.G., Bess J.W. Jr., Arthur L.O., Bryant D.K., Fenselau C. Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processing, and complete amino acid sequences. J. Virol. 66:1992;1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder II, R.C.3    Serabyn, S.A.4    Johnson, D.G.5    Bess Jr., J.W.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 9
    • 0034947840 scopus 로고    scopus 로고
    • Gag-Pol supplied in trans is efficiently packaged and supports viral function in human immunodeficiency virus type 1
    • Hill M.K., Hooker C.W., Harrich D., Crowe S.M., Mak J. Gag-Pol supplied in trans is efficiently packaged and supports viral function in human immunodeficiency virus type 1. J. Virol. 75:2001;6835-6840.
    • (2001) J. Virol. , vol.75 , pp. 6835-6840
    • Hill, M.K.1    Hooker, C.W.2    Harrich, D.3    Crowe, S.M.4    Mak, J.5
  • 10
    • 0002168907 scopus 로고
    • Macromolecular interactions in the assembly of HIV and other retroviruses
    • Hunter E. Macromolecular interactions in the assembly of HIV and other retroviruses. Semin. Virol. 5:1994;71-83.
    • (1994) Semin. Virol. , vol.5 , pp. 71-83
    • Hunter, E.1
  • 12
    • 0027932364 scopus 로고
    • The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency
    • Kaplan A.H., Manchester M., Swanstorm M. The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency. J. Virol. 68:1994;6782-6786.
    • (1994) J. Virol. , vol.68 , pp. 6782-6786
    • Kaplan, A.H.1    Manchester, M.2    Swanstorm, M.3
  • 14
    • 0026322839 scopus 로고
    • Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity
    • Krausslich H.-G. Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity. Proc. Natl. Acad. Sci. U.S.A. 88:1991;3213-3217.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3213-3217
    • Krausslich, H.-G.1
  • 15
  • 17
    • 0023755462 scopus 로고
    • The gag gene products of human immunodeficiency virus type 1: Alignment within the gag open reading frame, identification of posttranslation modifications, and evidence for alternative gag precursors
    • Mervis R.J., Ahmad N., Lillehoj E.P., Raum M.G., Salazar F.H.R., Chan H.W., Venkatesan V. The gag gene products of human immunodeficiency virus type 1: alignment within the gag open reading frame, identification of posttranslation modifications, and evidence for alternative gag precursors. J. Virol. 62:1988;3993-4002.
    • (1988) J. Virol. , vol.62 , pp. 3993-4002
    • Mervis, R.J.1    Ahmad, N.2    Lillehoj, E.P.3    Raum, M.G.4    Salazar, F.H.R.5    Chan, H.W.6    Venkatesan, V.7
  • 18
    • 0025005828 scopus 로고
    • Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity
    • Page K.A., Landau N.R., Littman D.R. Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity. J. Virol. 64:1990;5270-5276.
    • (1990) J. Virol. , vol.64 , pp. 5270-5276
    • Page, K.A.1    Landau, N.R.2    Littman, D.R.3
  • 19
    • 0026018243 scopus 로고
    • Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production
    • Park J., Morrow C.D. Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production. J. Virol. 65:1991;5111-5117.
    • (1991) J. Virol. , vol.65 , pp. 5111-5117
    • Park, J.1    Morrow, C.D.2
  • 20
    • 0025286146 scopus 로고
    • Mutational analysis of a native substrate of the human immunodeficiency virus type 1 proteinase
    • Partin K., Krausslich H.G., Ehrlich L., Wimmer E., Carter C. Mutational analysis of a native substrate of the human immunodeficiency virus type 1 proteinase. J. Virol. 64:1990;3938-3947.
    • (1990) J. Virol. , vol.64 , pp. 3938-3947
    • Partin, K.1    Krausslich, H.G.2    Ehrlich, L.3    Wimmer, E.4    Carter, C.5
  • 21
    • 0025728270 scopus 로고
    • Deletion of sequences upstream of the proteinase improve the proteolytic processing of human immunodeficiency virus type 1
    • Partin K., Zybarth G., Ehrlich L., DeCrombrugghe M., Wimmer E., Carter C. Deletion of sequences upstream of the proteinase improve the proteolytic processing of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. U.S.A. 88:1991;4776-4780.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4776-4780
    • Partin, K.1    Zybarth, G.2    Ehrlich, L.3    Decrombrugghe, M.4    Wimmer, E.5    Carter, C.6
  • 22
    • 0024334170 scopus 로고
    • Role of human immunodeficiency virus type 1-specific protease in core particle maturation and viral infectivity
    • Peng C., Ho B.K., Chang T.W., Chang N.T. Role of human immunodeficiency virus type 1-specific protease in core particle maturation and viral infectivity. J. Virol. 63:1989;2550-2556.
    • (1989) J. Virol. , vol.63 , pp. 2550-2556
    • Peng, C.1    Ho, B.K.2    Chang, T.W.3    Chang, N.T.4
  • 23
    • 0037213627 scopus 로고    scopus 로고
    • The dimmer interfaces of protease and extra-protease domains influence the activation of protease and the stability of Gag-Pol cleavage
    • Pettit S.C., Gulnik S., Everitt L., Kaplan A.H. The dimmer interfaces of protease and extra-protease domains influence the activation of protease and the stability of Gag-Pol cleavage. J. Virol. 77:2003;366-374.
    • (2003) J. Virol. , vol.77 , pp. 366-374
    • Pettit, S.C.1    Gulnik, S.2    Everitt, L.3    Kaplan, A.H.4
  • 24
    • 0029978462 scopus 로고    scopus 로고
    • Extensive regions of pol are required for efficient human immunodeficiency virus polyprotein processing and particle maturation
    • Quillent C., Borman A.M., Paulous S., Dauguet C., Clavel F. Extensive regions of pol are required for efficient human immunodeficiency virus polyprotein processing and particle maturation. Virology. 219:1996;29-36.
    • (1996) Virology , vol.219 , pp. 29-36
    • Quillent, C.1    Borman, A.M.2    Paulous, S.3    Dauguet, C.4    Clavel, F.5
  • 25
    • 0028969065 scopus 로고
    • Defining the level of human immunodeficiency virus type 1 (HIV-1) protease activity required for HIV-1 particle maturation and infectivity
    • Rose J.R., Base L.M., Craik C.S. Defining the level of human immunodeficiency virus type 1 (HIV-1) protease activity required for HIV-1 particle maturation and infectivity. J. Virol. 69:1995;2751-2758.
    • (1995) J. Virol. , vol.69 , pp. 2751-2758
    • Rose, J.R.1    Base, L.M.2    Craik, C.S.3
  • 26
    • 0035138477 scopus 로고    scopus 로고
    • Maintenance of the Gag/Gag-Pol ration is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity
    • Shehu-Xhilaga M., Crowe S.M., Mak J. Maintenance of the Gag/Gag-Pol ration is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity. J. Virol. 75:2001;1834-1841.
    • (2001) J. Virol. , vol.75 , pp. 1834-1841
    • Shehu-Xhilaga, M.1    Crowe, S.M.2    Mak, J.3
  • 27
    • 2642680072 scopus 로고    scopus 로고
    • Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity
    • Tessmer U., Krausslich H.-K. Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity. J. Virol. 72:1998;3459-3463.
    • (1998) J. Virol. , vol.72 , pp. 3459-3463
    • Tessmer, U.1    Krausslich, H.-K.2
  • 28
    • 0027160015 scopus 로고
    • Assembly, processing, and infectivity of human immunodeficiency virus type 1 Gag mutants
    • Wang C.-T., Barklis E. Assembly, processing, and infectivity of human immunodeficiency virus type 1 Gag mutants. J. Virol. 67:1993;4264-4273.
    • (1993) J. Virol. , vol.67 , pp. 4264-4273
    • Wang, C.-T.1    Barklis, E.2
  • 29
    • 0031666030 scopus 로고    scopus 로고
    • Analysis of minimal human immunodeficiency virus type 1 gag coding sequences capable of virus-like particle assembly and release
    • Wang C.-T., Lai H.-Y., Li J.-J. Analysis of minimal human immunodeficiency virus type 1 gag coding sequences capable of virus-like particle assembly and release. J. Virol. 72:1998;7950-7959.
    • (1998) J. Virol. , vol.72 , pp. 7950-7959
    • Wang, C.-T.1    Lai, H.-Y.2    Li, J.-J.3
  • 30
    • 0034056030 scopus 로고    scopus 로고
    • Assembly and processing of human immunodeficiency virus gag mutants containing a partial replacement of the matrix domain by the viral protease domain
    • Wang C.-T., Chou Y.-C., Chiang C.-C. Assembly and processing of human immunodeficiency virus gag mutants containing a partial replacement of the matrix domain by the viral protease domain. J. Virol. 74:2000;3418-3422.
    • (2000) J. Virol. , vol.74 , pp. 3418-3422
    • Wang, C.-T.1    Chou, Y.-C.2    Chiang, C.-C.3
  • 31
    • 0027328715 scopus 로고
    • Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release
    • Weldon R.A., Wills J.W. Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release. J. Virol. 67:1993;5550-5561.
    • (1993) J. Virol. , vol.67 , pp. 5550-5561
    • Weldon, R.A.1    Wills, J.W.2
  • 32
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • Wills J.W., Craven R.C. Form, function, and use of retroviral gag proteins. AIDS. 5:1991;639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 33
    • 0031054525 scopus 로고    scopus 로고
    • Altered Rous sarcoma virus Gag polyprotein processing and its effects on particle formation
    • Xiang Y., Ridky T.W., Krishna N.K., Leis J. Altered Rous sarcoma virus Gag polyprotein processing and its effects on particle formation. J. Virol. 71:1997;2083-2091.
    • (1997) J. Virol. , vol.71 , pp. 2083-2091
    • Xiang, Y.1    Ridky, T.W.2    Krishna, N.K.3    Leis, J.4
  • 34
    • 0031910808 scopus 로고    scopus 로고
    • Analysis of the assembly functions of the human immunodeficiency virus type 1 gag protein nucleocapsid domain
    • Zhang Y., Qian H., Love Z., Barklis E. Analysis of the assembly functions of the human immunodeficiency virus type 1 gag protein nucleocapsid domain. J. Virol. 72:1998;1782-1789.
    • (1998) J. Virol. , vol.72 , pp. 1782-1789
    • Zhang, Y.1    Qian, H.2    Love, Z.3    Barklis, E.4
  • 35
    • 0029013602 scopus 로고
    • Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessing
    • Zybarth G., Carter C. Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessing. J. Virol. 69:1995;3878-3884.
    • (1995) J. Virol. , vol.69 , pp. 3878-3884
    • Zybarth, G.1    Carter, C.2
  • 36
    • 0027957918 scopus 로고
    • Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain
    • Zybarth G., Krausslich H.G., Partin K., Carter C. Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain. J. Virol. 68:1994;240-250.
    • (1994) J. Virol. , vol.68 , pp. 240-250
    • Zybarth, G.1    Krausslich, H.G.2    Partin, K.3    Carter, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.