Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein

Cornilescu, Claudia C.; Bouamr, Fadila; Yao, Xiaolan; Carter, C; Tjandra, Nico

doi:10.1006/jmbi.2000.4395

Cited by 57 publications

(49 citation statements)

References 48 publications

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“…in contrast to the WT protein, in which these residues do not exhibit exchange (8). Leu 55 did not exhibit exchange in either protein.…”

Section: Dynamics Studies Of the D54a Mutant Of Htlv-1 Capsid Proteinmentioning

confidence: 61%

“…The DNA fragment encoding the D54A mutant was cloned into the NdeI/SapI sites of the pTYB1 plasmid vector (New England BioLabs), as described previously (8,16). The recombinant plasmid was transformed into Escherichia coli ER2566 strain for protein expression, and the purified D54A mutant was obtained by the method described previously (8,16).…”

Section: Protein Expression Purification and Preparation Of Nmr Sammentioning

confidence: 99%

“…The recombinant plasmid was transformed into Escherichia coli ER2566 strain for protein expression, and the purified D54A mutant was obtained by the method described previously (8,16). The uniformly 15 N-and 15 N/ 13 C-labeled NMR samples (0.8 -1.0 mM protein concentration) were prepared in 250 l of 10 mM Tris acetate, 0.1 mM NaN 3 , pH 6.0, containing 92.5% H 2 O and 7.5% 2 H 2 O.…”

Section: Protein Expression Purification and Preparation Of Nmr Sammentioning

confidence: 99%

“…Our previous studies (8) indicated that, although the ␤-hairpins of both CAs make contact with the helical core through the conserved salt bridge, they adopt significantly different orientations relative to it. Subsequent NMR transverse relaxation T 1 and steady-state heteronuclear nuclear Overhauser effect (NOE) measurements (16) also showed the rigidity of this structural element with values virtually identical to the rest of the well structured protein backbone.…”

mentioning

confidence: 96%

“…The structure is highly conserved among retroviral CA proteins that have been examined (5)(6)(7)(8)(9)(10); mutations in the C-terminal domain of HIV-1 block CA protein dimerization and particle assembly (3,(11)(12)(13). Mutations in the N-terminal domain (NTD) of HIV-1 impair CA protein assembly to a significantly lesser extent, but the assembled particles are noninfectious (3,11,13,14).…”

mentioning

confidence: 99%

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Structural and Dynamics Studies of the D54A Mutant of Human T Cell Leukemia Virus-1 Capsid Protein

Bouamr

Cornilescu

Goff

et al. 2005

Journal of Biological Chemistry

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The human T cell leukemia virus and the human immunodeficiency virus share a highly conserved, predominantly helical two-domain mature capsid (CA) protein structure with an N-terminal ␤-hairpin. Despite overall structural similarity, differences exist in the backbone dynamic properties of the CA N-terminal domain. Since studies with other retroviruses suggest that the ␤-hairpin is critical for formation of a CA-CA interface, we investigated the functional role of the human T cell leukemia virus ␤-hairpin by disrupting the salt bridge between Pro 1 and Asp 54 that stabilizes the ␤-hairpin. NMR 15 N relaxation data were used to characterize the backbone dynamics of the D54A mutant in the context of the N-terminal domains, compared with the wildtype counterpart. Moreover, the effect of the mutation on proteolytic processing and release of virus-like particles (VLPs) from human cells in culture was determined. Conformational and dynamic changes resulting from the mutation were detected by NMR spectroscopy. The mutation also altered the conformation of mature CA in cells and VLPs, as reflected by differential antibody recognition of the wild-type and mutated CA proteins. In contrast, the mutation did not detectably affect antibody recognition of the CA protein precursor or release of VLPs assembled by the precursor, consistent with the fact that the hairpin cannot form in the precursor molecule. The particle morphology and size were not detectably affected. The results indicate that the ␤-hairpin contributes to the overall structure of the mature CA protein and suggest that differences in the backbone dynamics of the ␤-hairpin contribute to mature CA structure, possibly introducing flexibility into interface formation during proteolytic maturation.

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“…in contrast to the WT protein, in which these residues do not exhibit exchange (8). Leu 55 did not exhibit exchange in either protein.…”

Section: Dynamics Studies Of the D54a Mutant Of Htlv-1 Capsid Proteinmentioning

confidence: 61%

Section: Protein Expression Purification and Preparation Of Nmr Sammentioning

confidence: 99%

Section: Protein Expression Purification and Preparation Of Nmr Sammentioning

confidence: 99%

mentioning

confidence: 96%

mentioning

confidence: 99%

See 3 more Smart Citations

Structural and Dynamics Studies of the D54A Mutant of Human T Cell Leukemia Virus-1 Capsid Protein

Bouamr

Cornilescu

Goff

et al. 2005

Journal of Biological Chemistry

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The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

Kingston

Olson

Vogt

2001

Journal of Structural Biology

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The Retrovirus Capsid Core

Zhang

Mendonça

Mansky

2018

Subcellular Biochemistry

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The retrovirus capsid core is a metastable structure that disassembles during the early phase of viral infection after membrane fusion. The core is intact and permeable to essential nucleotides during reverse transcription, but it undergoes disassembly for nuclear entry and genome integration. Increasing or decreasing the stability of the capsid core has a substantial negative impact on virus infectivity, which makes the core an attractive anti-viral target. The retrovirus capsid core also encounters a variety of virus- and organism-specific host cellular factors that promote or restrict viral replication. This review describes the structural elements fundamental to the formation and stability of the capsid core. The physical and chemical properties of the capsid core that are critical to its functional role in reverse transcription and interaction with host cellular factors are highlighted to emphasize areas of current research.

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Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein

Cited by 57 publications

References 48 publications

Structural and Dynamics Studies of the D54A Mutant of Human T Cell Leukemia Virus-1 Capsid Protein

Structural and Dynamics Studies of the D54A Mutant of Human T Cell Leukemia Virus-1 Capsid Protein

The Organization of Mature Rous Sarcoma Virus as Studied by Cryoelectron Microscopy

The Retrovirus Capsid Core

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