The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Open accessAbstract
The HIV-1 capsid protein forms the conical core structure at the center of the mature virion. Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the enzyme into the virion. Cyclophilin A subsequently performs an essential function in HIV-1 replication, possibly helping to disassemble the capsid core upon infection. We report the 2.36 A crystal structure of the N-terminal domain of HIV-1 capsid (residues 1-151) in complex with human cyclophilin A. A single exposed capsid loop (residues 85-93) binds in the enzyme's active site, and Pro-90 adopts an unprecedented trans conformation. The structure suggests how cyclophilin A can act as a sequence-specific binding protein and a nonspecific prolyl isomerase. In the crystal lattice, capsid molecules assemble into continuous planar strips. Side by side association of these strips may allow capsid to form the surface of the viral core. Cyclophilin A could then function by weakening the association between capsid strips, thereby promoting disassembly of the viral core.
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“A beta-hairpin is formed by the N-terminal residues in mature-like CA, stabilized by a salt bridge between the N-terminal proline and a conserved aspartate in helix 3”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [72]
Citations
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“Cyclophilin A is (bonds) 5 0.005 Å; RMSD (angles) 5 1.38; there are no w,c angles required for the replication of group M human immunodeficiency in the forbidden range (Laskowski et al., 1993).”
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Cited by
Sorted by citations
Items 701–710 of 710
Mechanisms of HIV-1 assembly, release and maturation
Kleinpeter, A. B., & Freed, E. O. (2026) · Nature Reviews Microbiology · doi:10.1038/s41579-026-01327-6 · Cited by 2
“Although the CA-NTD also participates in interhexameric interactions at a threefold interface in the lattice 78 , it is dispensable for VLP assembly and release in certain experimental systems 80 .”
InfluentialHIV capsid inhibitors: Mechanisms, resistance, and therapeutic advances
Mahdi, M., Lakatos, B., Mótyán, J. A., Hoffka, G., & Tőzsér, J. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014361
“One of the functionally important sites is a surface loop of NTD (residues 87–92) [58], which was found to bind the host-derived cofactor peptidyl-prolyl isomerase cyclophilin A (CypA).”
Capsid-Targeting Biologic Achieves Broad HIV-1 Neutralization with a High Barrier to Resistance
Stel, F. M., Willems, E., van Nuenen, A. C., Boeser‐Nunnink, B., Geijtenbeek, T. B. H., & Kootstra, N. A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27156883
“For both breakthrough variant 4A and 4B there was a V83L amino acid change in the CA region, which is located at the end of helix 4 CA [19,42].”
CypA is a molecular barrier to HIV emergence from Eastern chimpanzeesPreprint
Young, M. J., Cotera, F., Gill, C. C. C., Lewis, J. A., Whitby, F. G., Abdellatif, A., Rocha, J. L., Singer, M., Nalls, M. A., Faghri, F., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.08.747897
“For both capsids, one interface shows no direct interaction between CypA and the 6,7 loop, consistent with previous structural data for HIV-1 capsid [35] (fig.”
Amano, M., Nakamura, T., Miyakawa, T., & Hirotomo, N. (2026) · Antiviral Research · doi:10.1016/j.antiviral.2026.106552
Percipalle, M., Thader, A., Hodirnau, V.-V., Dick, R. A., & Schur, F. K. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.16.759032
“The retroviral CA-NTD contributes stabilizing contacts in both immature and mature lattices, but also occupies a more exposed position and participates in interactions with cellular factors, as demonstrated for HIV-1 36,39–41 .”
Metadata
- Authors
- Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P.
- Affiliations
- University of Utah (US)
- Corresponding author
- Hill, Christopher P
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1996-12
- Volume
- 87
- Issue
- 7
- Pages
- 1285-1294
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2121753315
- Cited by
- 706
- References
- 59
- Citations by year
- 2026: 12 · 2025: 8 · 2024: 7 · 2023: 18 · 2022: 20 · 2021: 26 · 2020: 16 · 2019: 12 · 2018: 23 · 2017: 21 · 2016: 29 · 2015: 22 · 2014: 25 · 2013: 32 · 2012: 24
- FWCI
- 6.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- cyclophilin A, HIV-1 capsid, peptidyl-prolyl isomerase, protein-protein complex, capsid disassembly, viral core, capsid assembly, HIV-1 replication
- MeSH terms
- Amino Acid Isomerases, Capsid, Carrier Proteins, Humans, Models, Molecular, Protein Binding, Virion, HIV-1, Gene Products, gag, Protein Structure, Tertiary, Crystallography, X-Ray, Peptidylprolyl Isomerase
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