Investigating the intercellular spreading properties of the foamy virus Gag protein
Small regions called protein transduction domains (PTDs), identified in cellular and viral proteins, have been reported to efficiently cross biological membranes. Here we show that the structural Gag protein of the prototypic foamy virus (PFV) is apparently able to move from cell to cell and to tran...
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Published in | PloS one Vol. 7; no. 2; p. e31108 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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29.02.2012
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Abstract | Small regions called protein transduction domains (PTDs), identified in cellular and viral proteins, have been reported to efficiently cross biological membranes. Here we show that the structural Gag protein of the prototypic foamy virus (PFV) is apparently able to move from cell to cell and to transport the green fluorescent protein (GFP) from few transfected cells to the nuclei of the entire monolayer. Deletion studies showed that this property lies within the second glycine/arginine (GRII) box in the C-terminus of the protein. We also found that uptake and nuclear accumulation of Gag GRII expressed as GFP-fusion protein in recipient cells was observed only following methanol fixation, but never in living cells or when cells were fixed with glutaraldehyde or treated with trichloroacetic acid prior to methanol fixation. Absence of intercellular spreading in vivo was further confirmed using a sensitive luciferase activity assay based on transactivation of the PFV long terminal repeats. Thus, we conclude that intercellular spreading of PFV Gag represents an artificial diffusion event occurring during cell fixation, followed by nuclear retention mediated by the chromatin-binding sequence within the Gag GRII box. In light of these results, we advise caution before defining a peptide as PTD on the basis of intercellular spreading observed by fluorescence microscopy. |
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AbstractList | Small regions called protein transduction domains (PTDs), identified in cellular and viral proteins, have been reported to efficiently cross biological membranes. Here we show that the structural Gag protein of the prototypic foamy virus (PFV) is apparently able to move from cell to cell and to transport the green fluorescent protein (GFP) from few transfected cells to the nuclei of the entire monolayer. Deletion studies showed that this property lies within the second glycine/arginine (GRII) box in the C-terminus of the protein. We also found that uptake and nuclear accumulation of Gag GRII expressed as GFP-fusion protein in recipient cells was observed only following methanol fixation, but never in living cells or when cells were fixed with glutaraldehyde or treated with trichloroacetic acid prior to methanol fixation. Absence of intercellular spreading in vivo was further confirmed using a sensitive luciferase activity assay based on transactivation of the PFV long terminal repeats. Thus, we conclude that intercellular spreading of PFV Gag represents an artificial diffusion event occurring during cell fixation, followed by nuclear retention mediated by the chromatin-binding sequence within the Gag GRII box. In light of these results, we advise caution before defining a peptide as PTD on the basis of intercellular spreading observed by fluorescence microscopy. Small regions called protein transduction domains (PTDs), identified in cellular and viral proteins, have been reported to efficiently cross biological membranes. Here we show that the structural Gag protein of the prototypic foamy virus (PFV) is apparently able to move from cell to cell and to transport the green fluorescent protein (GFP) from few transfected cells to the nuclei of the entire monolayer. Deletion studies showed that this property lies within the second glycine/arginine (GRII) box in the C-terminus of the protein. We also found that uptake and nuclear accumulation of Gag GRII expressed as GFP-fusion protein in recipient cells was observed only following methanol fixation, but never in living cells or when cells were fixed with glutaraldehyde or treated with trichloroacetic acid prior to methanol fixation. Absence of intercellular spreading in vivo was further confirmed using a sensitive luciferase activity assay based on transactivation of the PFV long terminal repeats. Thus, we conclude that intercellular spreading of PFV Gag represents an artificial diffusion event occurring during cell fixation, followed by nuclear retention mediated by the chromatin-binding sequence within the Gag GRII box. In light of these results, we advise caution before defining a peptide as PTD on the basis of intercellular spreading observed by fluorescence microscopy. |
Audience | Academic |
Author | Saïb, Ali Zamborlini, Alessia Bittoun, Patricia Tobaly-Tapiero, Joelle |
AuthorAffiliation | 2 Conservatoire National des Arts et Métiers, Paris, France 1 Institut Universitaire d'Hématologie, CNRS UMR7212-Inserm U944-Université Paris Diderot-Paris7, Paris, France Queensland Institute of Medical Research, Australia |
AuthorAffiliation_xml | – name: 2 Conservatoire National des Arts et Métiers, Paris, France – name: 1 Institut Universitaire d'Hématologie, CNRS UMR7212-Inserm U944-Université Paris Diderot-Paris7, Paris, France – name: Queensland Institute of Medical Research, Australia |
Author_xml | – sequence: 1 givenname: Joelle surname: Tobaly-Tapiero fullname: Tobaly-Tapiero, Joelle organization: Institut Universitaire d'Hématologie, CNRS UMR7212-Inserm U944-Université Paris Diderot-Paris7, Paris, France – sequence: 2 givenname: Alessia surname: Zamborlini fullname: Zamborlini, Alessia – sequence: 3 givenname: Patricia surname: Bittoun fullname: Bittoun, Patricia – sequence: 4 givenname: Ali surname: Saïb fullname: Saïb, Ali |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22393357$$D View this record in MEDLINE/PubMed |
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Copyright | COPYRIGHT 2012 Public Library of Science 2012 Tobaly-Tapiero et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Tobaly-Tapiero et al. 2012 |
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Notes | Conceived and designed the experiments: JTT AS. Performed the experiments: JTT PB. Analyzed the data: AZ AS. Contributed reagents/materials/analysis tools: JTT PB. Wrote the paper: AZ AS. |
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SubjectTerms | Animals Arginine Biological membranes Biological Transport Biology C-Terminus Cell division Chlorocebus aethiops Chromatin Clonal deletion COS Cells Cytoplasm Cytoplasm - metabolism Diffusion Fixation Fluorescence Fluorescence microscopy Fusion protein Gag protein Gene Deletion Gene Products, gag - metabolism Glutaral - chemistry Glutaraldehyde Glycine Green fluorescent protein Green Fluorescent Proteins - metabolism Herpes viruses Infections Investigations Luciferase Membranes Methanol Methanol - chemistry Microscopy Microscopy, Fluorescence - methods Models, Biological Monomolecular films Nuclei Nuclei (cytology) Open Reading Frames Peptides Plasmids - metabolism Protein Structure, Tertiary Protein transport Proteins Spreading Spumavirus - metabolism Transfection Trichloroacetic acid Viral proteins Viruses |
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Title | Investigating the intercellular spreading properties of the foamy virus Gag protein |
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