{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ao Y"],"funding":["National Institute of Allergy and Infectious Diseases","Gilead Research Scholars Program","amfAR","Vaccine Research Center","American Foundation for Aging Research","NIAID NIH HHS","National Institutes of Health","Engineering Research Centers","National Institute of General Medical Sciences","Gilead Sciences","NIGMS NIH HHS","Division of Intramural Research"],"pagination":["487-501.e7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10960674"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(3)"],"pubmed_abstract":["Structural dynamics of human immunodeficiency virus 1 (HIV-1) envelope (Env) glycoprotein mediate cell entry and facilitate immune evasion. Single-molecule FRET using peptides for Env labeling revealed structural dynamics of Env, but peptide use risks potential effects on structural integrity/dynamics. While incorporating noncanonical amino acids (ncAAs) into Env by amber stop-codon suppression, followed by click chemistry, offers a minimally invasive approach, this has proved to be technically challenging for HIV-1. Here, we develope an intact amber-free HIV-1 system that overcomes hurdles of preexisting viral amber codons. We achieved dual-ncAA incorporation into Env on amber-free virions, enabling single-molecule Förster resonance energy transfer (smFRET) studies of click-labeled Env th"],"journal":["Cell chemical biology"],"pubmed_title":["Bioorthogonal click labeling of an amber-free HIV-1 provirus for in-virus single molecule imaging."],"pmcid":["PMC10960674"],"funding_grant_id":["R01 AI129862","R01 AI181600","U54 AI170752","R35 GM147423","R56 AI170101","R37 AI150560","R35GM147423","R01 AI150560"],"pubmed_authors":["Arthos J","Han Y","Qin W","Haque MA","Lemke EA","Li W","Mothes W","Lu M","Katte R","Melikyan GB","Ao Y","Zhong G","Grover JR","Gifford L","Sauve S","Ghimire D","Zhang B","Kwong PD","Bhattacharjee R","Moradi M"],"additional_accession":[]},"is_claimable":false,"name":"Bioorthogonal click labeling of an amber-free HIV-1 provirus for in-virus single molecule imaging.","description":"Structural dynamics of human immunodeficiency virus 1 (HIV-1) envelope (Env) glycoprotein mediate cell entry and facilitate immune evasion. Single-molecule FRET using peptides for Env labeling revealed structural dynamics of Env, but peptide use risks potential effects on structural integrity/dynamics. While incorporating noncanonical amino acids (ncAAs) into Env by amber stop-codon suppression, followed by click chemistry, offers a minimally invasive approach, this has proved to be technically challenging for HIV-1. Here, we develope an intact amber-free HIV-1 system that overcomes hurdles of preexisting viral amber codons. We achieved dual-ncAA incorporation into Env on amber-free virions, enabling single-molecule Förster resonance energy transfer (smFRET) studies of click-labeled Env th","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-01T19:04:27.466Z","creation":"2025-04-04T03:03:45.199Z"},"accession":"S-EPMC10960674","cross_references":{"pubmed":["38232732"],"doi":["10.1016/j.chembiol.2023.12.017"]}}