{"doi":"10.1016/j.jmb.2023.168323","title":"Structure of the Borrelia Bacteriophage φBB1 Procapsid","abstract":null,"journal":"Journal of Molecular Biology","year":2023,"id":656593,"datarank":0.3453877639491069,"base_score":2.302585092994046,"endowment":2.302585092994046,"self_citation_contribution":0.3453877639491069,"citation_network_contribution":0.0,"self_endowment_contribution":0.3453877639491069,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":9,"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":1713940,"name":"Tibor Füzik","orcid":null,"position":1,"is_corresponding":false},{"id":1713941,"name":"Kaspars Tārs","orcid":null,"position":2,"is_corresponding":false},{"id":1713939,"name":"Jānis Rūmnieks","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Structure of the Borrelia Bacteriophage φBB1 Procapsid","abstract":"Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all B. burgdorferi isolates carry a prophage φBB1 as resident circular plasmids. Like its host, the φBB1 phage is quite distinctive and shares little sequence similarity with other known bacteriophages. We expressed φBB1 head morphogenesis proteins in Escherichia coli which resulted in assembly of homogeneous prolate procapsid structures and used cryo-electron microscopy to determine the three-dimensional structure of these particles. The φBB1 procapsids consist of 415 copies of the major capsid protein and an equal combined number of three homologous capsid decoration proteins that form trimeric knobs on the outside of the particle. One of the end vertices of the particle is occupied by a portal assembled from twelve copies of the portal protein. The φBB1 scaffolding protein is entirely α-helical and has an elongated shape with a small globular domain in the middle. Within the tubular section of the procapsid, the internal scaffold is built of stacked rings, each composed of 32 scaffolding protein molecules, which run in opposite directions from both caps with a heterogeneous part in the middle. Inside the portal-containing cap, the scaffold is organized asymmetrically with ten scaffolding protein molecules bound to the portal. The φBB1 procapsid structure provides better insight into the vast structural diversity of bacteriophages and presents clues of how elongated bacteriophage particles might be assembled.","is_dataset_classified":null,"base_score":2.302585092994046,"endowment":2.302585092994046,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"37866476","pmcid":null,"openalex_id":"https://openalex.org/W4387826837","authors":[],"funders":[{"funder_name":"European Commission","grant_id":"2581","title":null},{"funder_name":"European Regional Development Fund","grant_id":"1.1.1.2/VIAA/4/20/704","title":null},{"funder_name":"European Commission","grant_id":"871037","title":"Infrastructure for transnational access and discovery in structural biology"},{"funder_name":"Horizon 2020 Framework Programme","grant_id":"","title":null}],"total_grants":4,"fwci":1.7277,"citation_percentile":0.83774875,"influential_citations":0,"citation_trend":[{"year":2023,"count":1},{"year":2024,"count":3},{"year":2025,"count":2},{"year":2026,"count":3}],"oa_status":"closed","license":"CC BY NC","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0022283623004345?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0022283623004345?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.jmb.2023.168323","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/37866476","host_type":"repository"},{"url":"http://dx.doi.org/10.1016/j.jmb.2023.168323","host_type":""}],"fields_of_study":["Bacteriophages and microbial interactions","Vector-borne infectious diseases","Toxin Mechanisms and Immunotoxins","0301 basic medicine","03 medical and health sciences","Bacteriophages","Borrelia","Capsid","Capsid Proteins","Cryoelectron Microscopy","Virus Assembly"],"mesh_terms":["Bacteriophages","Borrelia","Capsid","Virus Assembly","Cryoelectron Microscopy","Capsid Proteins"],"keywords":["Capsid","Scaffold protein","Bacteriophage","Biology","Filamentous bacteriophage","Protein structure","Biophysics","Cell biology","Escherichia coli","Genetics","Virus","Gene","Scaffold","Portal","virus assembly","Cryo-em","Borrelia","Cryoelectron Microscopy","Bacteriophages","Capsid Proteins"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-11T21:26:52.125542Z","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":[]}