Solution structure of the capsid protein from the human T-cell leukemia virus type-I

被引:83
作者
Khorasanizadeh, S
Campos-Olivas, R
Summers, MF [1 ]
机构
[1] Univ Maryland Baltimore Cty, Howard Hughes Med Inst, Baltimore, MD 21250 USA
[2] Univ Maryland Baltimore Cty, Dept Biochem & Chem, Baltimore, MD 21250 USA
关键词
HTLV-I; capsid protein; retrovirus; three-dimensional structure; heteronuclear NMR spectroscopy;
D O I
10.1006/jmbi.1999.2986
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The solution structure of the capsid protein (CA) from the human T-cell leukemia virus type one (HTLV-I), a retrovirus that causes T-cell leukemia and HTLV-I-associated myelopathy in humans, has been determined by NMR methods. The protein consists of independent N and C-terminal domains connected by a flexible linker. The domains are structurally similar to the N-terminal "core" and C-terminal "dimerization" domains, respectively, of the human immunodeficiency virus type one (HIV-1) and equine infectious anemia virus (EIAV) capsid proteins, although several important differences exist. In particular, hydrophobic residues near the major homology region are partially buried in HTLV-I CA, which is monomeric in solution, whereas analogous residues in HIV-1 and EIAV CA project from the C-terminal domain and promote dimerization: These differences in the structure and oligomerization state of the proteins appear to be related to, and possibly controlled by, the oxidation state of conserved cysteine residues, which are reduced in HTLV-I CA but form a disulfide bond in the HIV-1 and EIAV CA crystal structures. The results are consistent with an oxidative capsid assembly mechanism, in which CA oligomerization or maturation is triggered by disulfide bond formation as the budding virus enters the oxidizing environment of the bloodstream. (C) 1999 Academic Press.
引用
收藏
页码:491 / 505
页数:15
相关论文
共 76 条
  • [51] LINKER INSERTION MUTATIONS IN THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GAG GENE - EFFECTS ON VIRION PARTICLE ASSEMBLY, RELEASE, AND INFECTIVITY
    REICIN, AS
    PAIK, S
    BERKOWITZ, RD
    LUBAN, J
    LOWY, I
    GOFF, SP
    [J]. JOURNAL OF VIROLOGY, 1995, 69 (02) : 642 - 650
  • [52] RIDDLES PW, 1983, METHOD ENZYMOL, V91, P49
  • [53] CHARACTERIZATION OF HIV-1 P24 SELF-ASSOCIATION USING ANALYTICAL AFFINITY-CHROMATOGRAPHY
    ROSE, S
    HENSLEY, P
    OSHANNESSY, DJ
    CULP, J
    DEBOUCK, C
    CHAIKEN, I
    [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1992, 13 (02): : 112 - 119
  • [54] VIRAL CELL RECOGNITION AND ENTRY
    ROSSMANN, MG
    [J]. PROTEIN SCIENCE, 1994, 3 (10) : 1712 - 1725
  • [55] Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines
    Sapp, M
    Fligge, C
    Petzak, I
    Harris, JR
    Streeck, RE
    [J]. JOURNAL OF VIROLOGY, 1998, 72 (07) : 6186 - 6189
  • [56] IDENTIFICATION OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 GAG PROTEIN DOMAINS ESSENTIAL TO MEMBRANE-BINDING AND PARTICLE ASSEMBLY
    SPEARMAN, P
    WANG, JJ
    VANDERHEYDEN, N
    RATNER, L
    [J]. JOURNAL OF VIROLOGY, 1994, 68 (05) : 3232 - 3242
  • [57] STEWART SA, 1994, VIRUSES CANC, P167
  • [58] STUDIER FW, 1990, METHOD ENZYMOL, V185, P60
  • [59] FUNCTIONAL ASSOCIATION OF CYCLOPHILIN-A WITH HIV-1 VIRIONS
    THALI, M
    BUKOVSKY, A
    KONDO, E
    ROSENWIRTH, B
    WALSH, CT
    SODROSKI, J
    GOTTLINGER, HG
    [J]. NATURE, 1994, 372 (6504) : 363 - 365
  • [60] Structural biology of HIV
    Turner, BG
    Summers, MF
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (01) : 1 - 32