2024
Channel width modulates the permeability of DNA origami–based nuclear pore mimics
Feng Q, Saladin M, Wu C, Cao E, Zheng W, Zhang A, Bhardwaj P, Li X, Shen Q, Kapinos L, Kozai T, Mariappan M, Lusk C, Xiong Y, Lim R, Lin C. Channel width modulates the permeability of DNA origami–based nuclear pore mimics. Science Advances 2024, 10: eadq8773. PMID: 39536094, PMCID: PMC11559598, DOI: 10.1126/sciadv.adq8773.Peer-Reviewed Original ResearchMeSH KeywordsCapsidDNAHepatitis B virusHumansMembrane GlycoproteinsNanoporesNuclear PoreNuclear Pore Complex ProteinsPermeability
2023
The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen Q, Kumari S, Xu C, Jang S, Shi J, Burdick R, Levintov L, Xiong Q, Wu C, Devarkar S, Tian T, Tripler T, Hu Y, Yuan S, Temple J, Feng Q, Lusk C, Aiken C, Engelman A, Perilla J, Pathak V, Lin C, Xiong Y. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2202815120. PMID: 36943880, PMCID: PMC10068764, DOI: 10.1073/pnas.2202815120.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusCapsidCapsid ProteinsHIV InfectionsHIV SeropositivityHIV-1HumansNuclear PoreNuclear Pore Complex ProteinsConceptsHIV-1 capsidC-terminal tail regionTriple arginine motifNuclear pore complexPhenylalanine-glycine motifsBipartite motifNuclear importPore complexNuclear poresNuclear entryNup153Capsid latticeInteraction moduleProtein latticeCA assemblyCA hexamersIntact capsidsNucleoporinsHIV-1 coreMotifCapsidTail regionIntact formInfection studiesMechanistic evidenceModeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusCapsid ProteinsCell LineDNAHIV-1HumansNuclear PoreNuclear Pore Complex ProteinsConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes