ArticleACS chemical biology2012
Tyrosine cross-linking reveals interfacial dynamics in adeno-associated viral capsids during infection.
Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 29 citations in OpenAlex.
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- Engineered dityrosine-bonding of the RSV prefusion F protein imparts stability and potency advantages.Nature communications · 2024Article
- Multiparametric domain insertional profiling of adeno-associated virus VP1.Molecular therapy. Methods & clinical development · 2023Article
- Structure-guided AAV capsid evolution strategies for enhanced CNS gene delivery.Nature protocols · 2023Review
- Analysis of thermally driven structural changes, genome release, disassembly, and aggregation of recombinant AAV by CDMS.Molecular therapy. Methods & clinical development · 2022Article
- Assembly of Protein Cages for Drug Delivery.Pharmaceutics · 2022Review
- Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine.iScience · 2020Review
- The Golgi Calcium ATPase Pump Plays an Essential Role in Adeno-associated Virus Trafficking and Transduction.Journal of virology · 2020Article
- Physical, chemical, and synthetic virology: Reprogramming viruses as controllable nanodevices.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2019Review
- Microglia-specific targeting by novel capsid-modified AAV6 vectors.Molecular therapy. Methods & clinical development · 2016Article
- Structure of neurotropic adeno-associated virus AAVrh.8.Journal of structural biology · 2015Article
- Metal-binding and redox properties of substituted linear and cyclic ATCUN motifs.Journal of inorganic biochemistry · 2014Article
- Structure and dynamics of adeno-associated virus serotype 1 VP1-unique N-terminal domain and its role in capsid trafficking.Journal of virology · 2013Article
- Macrocyclization of the ATCUN motif controls metal binding and catalysis.Inorganic chemistry · 2013Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Viral capsid dynamics are often observed during infectious events such as cell surface attachment, entry and genome release. Structural analysis of adeno-associated virus (AAV), a helper-dependent parvovirus, revealed a cluster of surface-exposed tyrosine residues at the icosahedral two-fold symmetry axis. We exploited the latter observation to carry out selective oxidation of Tyr residues, which yielded cross-linked viral protein (VP) subunit dimers, effectively "stitching" together the AAV capsid two-fold interface. Characterization of different Tyr-to-Phe mutants confirmed that the formation of cross-linked VP dimers is mediated by dityrosine adducts and requires the Tyr704 residue, which crosses over from one neighboring VP subunit to the other. When compared to unmodified capsids, Tyr-cross-linked AAV displayed decreased transduction efficiency in cell culture. Surprisingly, further biochemical and quantitative microscopy studies revealed that restraining the two-fold interface hinders externalization of buried VP N-termini, which contain a phospholipase A2 domain and nuclear localization sequences critical for infection. These adverse effects caused by tyrosine oxidation support the notion that interfacial dynamics at the AAV capsid two-fold symmetry axis play a role in externalization of VP N-termini during infection.
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