{"doi":"10.1073/pnas.1210903109","title":"Structural insight into HIV-1 capsid recognition by rhesus TRIM5α","abstract":"<jats:p>Tripartite motif protein isoform 5 alpha (TRIM5α) is a potent antiviral protein that restricts infection by HIV-1 and other retroviruses. TRIM5α recognizes the lattice of the retrovirus capsid through its B30.2 (PRY/SPRY) domain in a species-specific manner. Upon binding, TRIM5α induces premature disassembly of the viral capsid and activates the downstream innate immune response. We have determined the crystal structure of the rhesus TRIM5α PRY/SPRY domain that reveals essential features for capsid binding. Combined cryo-electron microscopy and biochemical data show that the monomeric rhesus TRIM5α PRY/SPRY, but not the human TRIM5α PRY/SPRY, can bind to HIV-1 capsid protein assemblies without causing disruption of the capsid. This suggests that the PRY/SPRY domain alone constitutes an important pattern-sensing component of TRIM5α that is capable of interacting with viral capsids of different curvatures. Our results provide molecular insights into the mechanisms of TRIM5α-mediated retroviral restriction.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2012,"id":678809,"datarank":0.6496100010429497,"base_score":4.330733340286331,"endowment":4.330733340286331,"self_citation_contribution":0.6496100010429497,"citation_network_contribution":0.0,"self_endowment_contribution":0.6496100010429497,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":75,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":886728,"name":"Xiaoyun Ji","orcid":"0000-0002-0801-8825","position":1,"is_corresponding":false},{"id":238471,"name":"Gongpu Zhao","orcid":"0000-0003-0330-1581","position":2,"is_corresponding":false},{"id":463230,"name":"Jiying Ning","orcid":"0000-0002-8244-7230","position":3,"is_corresponding":false},{"id":950097,"name":"Qi Zhao","orcid":"0000-0002-5267-8046","position":4,"is_corresponding":false},{"id":307290,"name":"Christopher Aiken","orcid":"0000-0002-2476-4078","position":5,"is_corresponding":false},{"id":141368,"name":"Angela M. 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We have determined the crystal structure of the rhesus TRIM5α PRY/SPRY domain that reveals essential features for capsid binding. Combined cryo-electron microscopy and biochemical data show that the monomeric rhesus TRIM5α PRY/SPRY, but not the human TRIM5α PRY/SPRY, can bind to HIV-1 capsid protein assemblies without causing disruption of the capsid. This suggests that the PRY/SPRY domain alone constitutes an important pattern-sensing component of TRIM5α that is capable of interacting with viral capsids of different curvatures. Our results provide molecular insights into the mechanisms of TRIM5α-mediated retroviral restriction.</jats:p>","is_dataset_classified":null,"base_score":4.330733340286331,"endowment":4.330733340286331,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23091002","pmcid":"PMC3494900","openalex_id":"https://openalex.org/W2085704334","authors":[],"funders":[{"funder_name":"NIAID NIH HHS","grant_id":"AI089401","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM085043","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"P50GM82251","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"R01 AI097064","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"P50 GM082251","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM085043","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"AI097064","title":null},{"funder_name":"NIAID NIH HHS","grant_id":"R01 AI089401","title":null}],"total_grants":8,"fwci":2.9846,"citation_percentile":0.91699905,"influential_citations":0,"citation_trend":[{"year":2013,"count":8},{"year":2014,"count":8},{"year":2015,"count":8},{"year":2016,"count":7},{"year":2017,"count":4},{"year":2018,"count":5},{"year":2019,"count":10},{"year":2020,"count":4},{"year":2021,"count":4},{"year":2022,"count":2},{"year":2023,"count":3},{"year":2024,"count":4},{"year":2025,"count":5},{"year":2026,"count":3}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://www.pnas.org/content/pnas/109/45/18372.full.pdf","host_type":"journal"},{"url":"https://www.pnas.org/content/pnas/109/45/18372.full.pdf","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.1210903109","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.1210903109","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23091002","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3494900","host_type":"repository"}],"fields_of_study":["HIV Research and Treatment","interferon and immune responses","RNA and protein synthesis mechanisms"],"mesh_terms":["Amino Acid Sequence","Animals","Capsid","Carrier Proteins","Humans","Macaca mulatta","Models, Molecular","Molecular Sequence Data","Protein Binding","Solutions","HIV-1","Conserved Sequence","Protein Structure, Tertiary","Crystallography, X-Ray","Evolution, Molecular","Protein Multimerization"],"keywords":["Capsid","Retrovirus","Biology","Viral protein","Plasma protein binding","Group-specific antigen","Gene isoform","Cell biology","Virology","Human immunodeficiency virus (HIV)","Virus","Genetics","Gene"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"emdb"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T11:29:41.345453Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}