{"entity": "researcher", "timestamp": "2026-08-20T20:37:12.263Z", "family": "Swanstrom", "given": "Ronald", "initials": "R", "orcid": "0000-0001-7777-0773", "affiliations": ["Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.", "Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/a267fa86094b4ddb9a965c9663ad1b60.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/a267fa86094b4ddb9a965c9663ad1b60"}}, "publications": [{"entity": "publication", "iuid": "cddad9583da743ca99f4f837e46f08d5", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/cddad9583da743ca99f4f837e46f08d5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/cddad9583da743ca99f4f837e46f08d5"}}, "title": "Cotranslational folding and maturation of HIV-1 protease.", "authors": [{"family": "Westerfield", "given": "Justin", "initials": "J", "orcid": "0000-0002-3937-5833", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/abd6b68fba914d529ef0ad62466a4ebc.json"}}, {"family": "Nicolaus", "given": "Felix", "initials": "F", "orcid": "0000-0001-9230-8544", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9f47078a41e242c98a1b2a3c2ad0ebe9.json"}}, {"family": "Swanstrom", "given": "Ronald", "initials": "R", "orcid": "0000-0001-7777-0773", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a267fa86094b4ddb9a965c9663ad1b60.json"}}, {"family": "von Heijne", "given": "Gunnar", "initials": "G", "orcid": "0000-0002-4490-8569", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/529a460e668a479ca7d9b9271375ef9f.json"}}], "type": "journal article", "published": "2025-08-27", "journal": {"title": "bioRxiv", "issn": "2692-8205", "issn-l": null}, "abstract": "HIV-1 particle assembly depends critically on multiple proteolytic cleavages of viral polyproteins by the viral protease, PR. PR is translated as part of the Gag-Pro-Pol polyprotein, which undergoes autoproteolysis to liberate active, dimeric PR during virus particle maturation. Gag-Pro-Pol is produced via an infrequent -1 frameshifting event in ribosomes translating full length genomic RNA as Gag mRNA. Here, we study the cotranslational folding and autoproteolytic processing of frameshifted transframe-protease-reverse transcriptase (TF-PR-RT) constructs by in vitro translation. We demonstrate partial cotranslational folding of ribosome-bound PR at its conserved \u03b1-helix near the C terminus. Unexpectedly, we find that the initial dimerization of TF-PR-RT involves ribosome-bound nascent chains that are then not further cleaved. Moreover, only ribosome-bound nascent chains are substrates for PR-catalyzed processing. These observations are consistent with a model for virion assembly in which dimerization of a subset of Pro-Pol precursors leads to cleavage of PR monomers that then carry out the bulk of the proteolytic processing needed for virion maturation and infectivity.", "doi": "10.1101/2025.08.27.672612", "pmid": "40909734", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12407942"}, {"db": "pii", "key": "2025.08.27.672612"}], "notes": [], "created": "2026-08-20T11:07:04.077Z", "modified": "2026-08-20T11:07:04.152Z"}]}