ArticlePloS one2011
A SNAP-tagged derivative of HIV-1--a versatile tool to study virus-cell interactions.
Article in PloS one, 2011. 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, 43 citations in OpenAlex.
- Advancements and Practical Considerations for Biophysical Research: Navigating the Challenges and Future of Super-resolution Microscopy.Chemical & biomedical imaging · 2024Review
- Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking.Viruses · 2022Article
- Towards a Quantitative Single Particle Characterization by Super Resolution Microscopy: From Virus Structures to Antivirals Design.Frontiers in bioengineering and biotechnology · 2021Review
- Single-Virus Tracking: From Imaging Methodologies to Virological Applications.Chemical reviews · 2020Review
- Super-resolution fluorescence microscopy studies of human immunodeficiency virus.Retrovirology · 2018Review
- New Routes and Opportunities for Modular Construction of Particulate Vaccines: Stick, Click, and Glue.Frontiers in immunology · 2018Review
- SNAP-tagged Chikungunya Virus Replicons Improve Visualisation of Non-Structural Protein 3 by Fluorescence Microscopy.Scientific reports · 2017Article
- Synchronized HIV assembly by tunable PIPeLife · 2017Article
- Article
- Where in the Cell Are You? Probing HIV-1 Host Interactions through Advanced Imaging Techniques.Viruses · 2016Review
- Visualizing the Behavior of HIV-Infected T Cells In Vivo Using Multiphoton Intravital Microscopy.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Antigenic properties of the human immunodeficiency virus envelope glycoprotein gp120 on virions bound to target cells.PLoS pathogens · 2015Article
- Super-resolution imaging of ESCRT-proteins at HIV-1 assembly sites.PLoS pathogens · 2015Article
- HIV virions as nanoscopic test tubes for probing oligomerization of the integrase enzyme.ACS nano · 2014Article
- Clustering and mobility of HIV-1 Env at viral assembly sites predict its propensity to induce cell-cell fusion.Journal of virology · 2013Article
- Super-resolution microscopy reveals specific recruitment of HIV-1 envelope proteins to viral assembly sites dependent on the envelope C-terminal tail.PLoS pathogens · 2013Article
- Single-molecule coordinate-based analysis of the morphology of HIV-1 assembly sites with near-molecular spatial resolution.Histochemistry and cell biology · 2013Article
- Detection of viral RNA by fluorescence in situ hybridization (FISH).Journal of visualized experiments : JoVE · 2012Article
- HIV taken by STORM: super-resolution fluorescence microscopy of a viral infection.Virology journal · 2012Article
- Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fluorescently labeled human immunodeficiency virus (HIV) derivatives, combined with the use of advanced fluorescence microscopy techniques, allow the direct visualization of dynamic events and individual steps in the viral life cycle. HIV proteins tagged with fluorescent proteins (FPs) have been successfully used for live-cell imaging analyses of HIV-cell interactions. However, FPs display limitations with respect to their physicochemical properties, and their maturation kinetics. Furthermore, several independent FP-tagged constructs have to be cloned and characterized in order to obtain spectral variations suitable for multi-color imaging setups. In contrast, the so-called SNAP-tag represents a genetically encoded non-fluorescent tag which mediates specific covalent coupling to fluorescent substrate molecules in a self-labeling reaction. Fusion of the SNAP-tag to the protein of interest allows specific labeling of the fusion protein with a variety of synthetic dyes, thereby offering enhanced flexibility for fluorescence imaging approaches.Here we describe the construction and characterization of the HIV derivative HIV(SNAP), which carries the SNAP-tag as an additional domain within the viral structural polyprotein Gag. Introduction of the tag close to the C-terminus of the matrix domain of Gag did not interfere with particle assembly, release or proteolytic virus maturation. The modified virions were infectious and could be propagated in tissue culture, albeit with reduced replication capacity. Insertion of the SNAP domain within Gag allowed specific staining of the viral polyprotein in the context of virus producing cells using a SNAP reactive dye as well as the visualization of individual virions and viral budding sites by stochastic optical reconstruction microscopy. Thus, HIV(SNAP) represents a versatile tool which expands the possibilities for the analysis of HIV-cell interactions using live cell imaging and sub-diffraction fluorescence microscopy.
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