Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses
Abstract
The matrix protein performs similar roles in all retroviruses, initially directing membrane localization of the assembling viral particle and subsequently forming a stable structural shell associated with the inner surface of the mature viral membrane. Although conserved structural elements are likely to perform these functions in all retroviral matrix proteins, invariant motifs are not evident at the primary sequence level and three-dimensional structures have been available for only the primate lentiviral matrix proteins. We have therefore used NMR spectroscopy to determine the structure of the matrix protein from human T-cell leukemia virus type II (HTLV-II), a member of the human oncovirus subclass of retroviruses. A total of 577 distance restraints were used to build 20 refined models that superimpose with an rmsd of 0.71 A for the backbone atoms of the structured regions. The globular HTLV-II matrix structure is composed of four alpha-helices and a 3(10) helix. Exposed basic residues near the C terminus of helix II form a putative membrane binding surface which could act in concert with the N-terminal myristoyl group to anchor the protein on the viral membrane surface. Clear structural similarities between the HTLV-II and HIV-1 matrix proteins suggest that the topology and exposed cationic membrane binding surface are likely to be conserved features of retroviral matrix proteins.
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Many other retroviruses, including SIV, EIAV, HTLV-2, BLV, and MPMV, exhibit MA trimers despite their highly varied sequences.
“Many other retroviruses, including SIV, EIAV, HTLV-2, BLV, and MPMV, exhibit MA trimers despite their highly varied sequences.”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Christensen et al. 1996
Mutations in the trimer interface, at least in MPMV, compromise CA assembly.
“Mutations in the trimer interface, at least in the case of MPMV, have been shown to compromise CA assembly”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Christensen et al. 1996
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HIV-1 Gag proteins: diverse functions in the virus life cycle
Freed, E. O. (1998) · Virology · doi:10.1006/viro.1998.9398 · Cited by 717 · see citing works
Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5 · see citing works
“Mutations in the trimer interface, at least in the case of MPMV, have been shown to compromise CA assembly (Rhee and Hunter 1991 , Rao et al. 1995 , Christensen et al. 1996 , Matthews et al. 1996 , Conte et al. 1997 ).”
- Authors
- Christensen, A. M., Massiah, M. A., Turner, B. G., Sundquist, W. I., & Summers, M. F.
- Affiliations
- University of Maryland, Baltimore (US)
- Corresponding author
- Sundquist, Wesley I.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1996-12
- Volume
- 264
- Issue
- 5
- Pages
- 1117-1131
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1993573856
- Cited by
- 59
- References
- 11
- Citations by year
- 2025: 2 · 2024: 1 · 2021: 3 · 2020: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 3
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI037524, AI30917)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Keywords
- HTLV-II, matrix protein, three-dimensional structure, HIV-1 matrix protein, myristoylation, alpha-helix, 310-helix, structural conservation, viral assembly
- MeSH terms
- Amino Acid Sequence, Escherichia coli, Humans, Models, Molecular, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Protein Conformation, Recombinant Proteins, Retroviridae, Species Specificity, Viral Matrix Proteins, Human T-lymphotropic virus 2, Human T-lymphotropic virus 1, HIV-1, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Structure, Tertiary
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