| Author | Cortines, Juliana R. | |
| Author | Lima, Luís Mauricio T. R. | |
| Author | Mohana-Borges, Ronaldo | |
| Author | Millen, Thiago de A. | |
| Author | Gaspar, Luciane Pinto | |
| Author | Lanman, Jason K. | |
| Author | Prevelige Jr, Peter E. | |
| Author | Silva, Jerson L. | |
| Access date | 2024-06-20T17:25:32Z | |
| Available date | 2024-06-20T17:25:32Z | |
| Document date | 2015 | |
| Citation | CORTINES, Juliana R. et al. Structural insights into the stabilization of the human immunodeficiency virus type 1 capsid protein by the cyclophilin-binding domain and implications on the virus cycle. Biochimica et Biophysica Acta, v. 1854, n. 5, p. 341-348, May 2015. | en_US |
| ISSN | 1570-9639 | en_US |
| URI | https://www.arca.fiocruz.br/handle/icict/64587 | |
| Language | eng | en_US |
| Publisher | Elsevier | en_US |
| Rights | restricted access | |
| Title | Structural insights into the stabilization of the human immunodeficiency virus type 1 capsid protein by the cyclophilin-binding domain and implications on the virus cycle | en_US |
| Type | Article | |
| DOI | 10.1016/j.bbapap.2014.12.008 | |
| Abstract | During infection, human immunodeficiency virus type 1 (HIV-1) interacts with the cellular host factor cyclophilin A (CypA) through residues 85–93 of the N-terminal domain of HIV-1's capsid protein (CA). The role of the CA:CypA interaction is still unclear. Previous studies showed that a CypA-binding loop mutant, Δ87–97, has increased ability to assemble in vitro. We used this mutant to infer whether the CypA-binding region has an overall effect on CA stability, as measured by pressure and chemical perturbation. We built a SAXS-based envelope model for the dimer of both WT and Δ87–97. A new conformational arrangement of the dimers is described, showing the structural plasticity that CA can adopt. In protein folding studies, the deletion of the loop drastically reduces CA stability, as assayed by high hydrostatic pressure and urea. We hypothesize that the deletion promotes a rearrangement of helix 4, which may enhance the heterotypic interaction between the N- and C-terminal domains of CA dimers. In addition, we propose that the cyclophilin-binding loop may modulate capsid assembly during infection, either in the cytoplasm or near the nucleus by binding to the nuclear protein Nup385. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica. Instituto Nacional de Biologia Estrutural e Bioimagem. Rio de Janeiro, RJ, Brasil / Universidade Federal Do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Departamento de Virologia. Rio de Janeiro, RJ, Brasil. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Escola de farmácia. Rio de Janeiro, RJ, Brasil. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Rio de Janeiro, RJ, Brasil. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica. Instituto Nacional de Biologia Estrutural e Bioimagem. Rio de Janeiro, RJ, Brasil. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica. Instituto Nacional de Biologia Estrutural e Bioimagem. Rio de Janeiro, RJ, Brasil / Fundação Oswaldo Cruz. Instituto de Tecnologia em Imunobiológicos (Bio-Manguinhos). Rio de Janeiro, RJ, Brasil. | en_US |
| Affilliation | University of Alabama at Birmingham. Department of Microbiology. Birmingham, AL, USA. | en_US |
| Affilliation | University of Alabama at Birmingham. Department of Microbiology. Birmingham, AL, USA. | en_US |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica. Instituto Nacional de Biologia Estrutural e Bioimagem. Rio de Janeiro, RJ, Brasil. | en_US |
| Subject | Human immunodeficiency virus | en_US |
| Subject | Capsid protein | en_US |
| Subject | Cyclophilin | en_US |
| Subject | High hydrostatic pressure | en_US |
| Subject | SAXS | en_US |
| Embargo date | 2030-12-31 | |
