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Super-Resolution Imaging of ESCRT-Proteins at HIV-1 Assembly Sites
Viruses hijack the cellular machinery to complete their life cycle. In the case of HIV-1, the endosomal sorting complex required for transport (ESCRT) is recruited by nascent viruses to release themselves from infected cells. Currently, there has been an intense amount of research on how the ESCRT machinery induces viral release. Using super-resolution imaging with endogenous ESCRT proteins or ESCRT proteins containing a small tag, we are able to provide insight into how ESCRT leads to budding of HIV-1. Super resolution imaging of the early ESCRT factors Tsg101 and ALIX, as well as later factors CHMP4B and CHMP2A, also showed condensed, circular structures with diameters of roughly 60 to 90 nm. The cluster sizes were significantly smaller than that of the HIV-1 bud and the distribution of cluster sizes that colocalized with nascent HIV-1 assembly sites were narrower than for non-colocalizing structures. This indicates that the point of interaction between the ESCRT machinery and the HIV-1 assembly site is in the bud neck.
Vyšlo v časopise: Super-Resolution Imaging of ESCRT-Proteins at HIV-1 Assembly Sites. PLoS Pathog 11(2): e32767. doi:10.1371/journal.ppat.1004677
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004677Souhrn
Viruses hijack the cellular machinery to complete their life cycle. In the case of HIV-1, the endosomal sorting complex required for transport (ESCRT) is recruited by nascent viruses to release themselves from infected cells. Currently, there has been an intense amount of research on how the ESCRT machinery induces viral release. Using super-resolution imaging with endogenous ESCRT proteins or ESCRT proteins containing a small tag, we are able to provide insight into how ESCRT leads to budding of HIV-1. Super resolution imaging of the early ESCRT factors Tsg101 and ALIX, as well as later factors CHMP4B and CHMP2A, also showed condensed, circular structures with diameters of roughly 60 to 90 nm. The cluster sizes were significantly smaller than that of the HIV-1 bud and the distribution of cluster sizes that colocalized with nascent HIV-1 assembly sites were narrower than for non-colocalizing structures. This indicates that the point of interaction between the ESCRT machinery and the HIV-1 assembly site is in the bud neck.
Zdroje
1. Sundquist WI, Kräusslich H-G (2012) HIV-1 Assembly, Budding, and Maturation. Cold Spring Harbor Perspectives in Medicine 2: a007823. doi: 10.1101/cshperspect.a007823 22762022
2. Ganser-Pornillos BK, Yeager M, Pornillos O (2012) Assembly and Architecture of HIV. Advances in Experimental Medicine and Biology 726 : 441–465. doi: 10.1007/978-1-4614-0980-9_20 22297526
3. Briggs JAG, Kräusslich H-G (2011) The Molecular Architecture of HIV. Journal of Molecular Biology 410 : 491–500. doi: 10.1016/j.jmb.2011.04.021 21762795
4. Votteler J, Sundquist WI (2013) Virus Budding and the ESCRT Pathway. Cell Host & Microbe 14 : 232–241. doi: 10.1016/j.fgb.2015.01.006 25626172
5. Weiss ER, Göttlinger HG (2011) The Role of Cellular Factors in Promoting HIV Budding. Journal of Molecular Biology 410 : 525–533. doi: 10.1016/j.jmb.2011.04.055 21762798
6. Martin-Serrano J, Neil SJD (2011) Host factors involved in retroviral budding and release. Nature Reviews Microbiology 9 : 519–531. doi: 10.1038/nrmicro2596 21677686
7. Hurley JH, Hanson PI (2010) Membrane budding and scission by the ESCRT machinery: it’s all in the neck. Nature Reviews Molecular Cell Biology 11 : 556–566. doi: 10.1038/nrm2937 20588296
8. Caballe A, Martin-Serrano J (2011) ESCRT Machinery and Cytokinesis: the Road to Daughter Cell Separation. Traffic 12 : 1318–1326. doi: 10.1111/j.1600-0854.2011.01244.x 21722282
9. McCullough J, Colf LA, Sundquist WI (2013) Membrane Fission Reactions of the Mammalian ESCRT Pathway. Annual Review of Biochemistry 82 : 663–692. doi: 10.1146/annurev-biochem-072909-101058 23527693
10. Teis D, Saksena S, Emr1 SD (2009) The ESCRT Machinery. Cell 137 : 182–183. doi: 10.1016/j.cell.2009.03.027 19345195
11. Schwedler UKv, Stuchell M, Müller B, Ward DM, Chung H-Y, et al. (2003) The Protein Network of HIV Budding. Cell 114 : 701–713. 14505570
12. Stuchell MD, Garrus JE, Müller B, Stray KM, Ghaffarian S, et al. (2004) The Human Endosomal Sorting Complex Required for Transport (ESCRT-I) and Its Role in HIV-1 Budding. The Journal of Biological Chemistry 279 : 36059–36071. 15218037
13. Jouvenet N, Zhadina M, Bieniasz PD, Simon SM (2011) Dynamics of ESCRT protein recruitment during retroviral assembly. Nature Cell Biology 13 : 394–401. doi: 10.1038/ncb2207 21394083
14. Morita E, Sandrin V, McCullough J, Katsuyama A, Hamilton IB, et al. (2011) ESCRT-III Protein Requirements for HIV-1 Budding. Cell Host & Microbe 9 : 235–242. doi: 10.1016/j.fgb.2015.01.006 25626172
15. Domenico ID, Ward DM, Langelier C, Vaughn MB, Nemeth E, et al. (2007) The Molecular Mechanism of Hepcidin-mediated Ferroportin Down-Regulation. Molecular Biology of the Cell 18 : 2569–2578. 17475779
16. Demirov DG, Orenstein JM, Freed EO (2002) The Late Domain of Human Immunodeficiency Virus Type 1 p6 Promotes Virus Release in a Cell Type-Dependent Manner. Journal of Virology 76 : 105–117. 11739676
17. Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (2003) AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding. Cell 114 : 689–699. 14505569
18. Martin-Serrano J, Zang T, Bieniasz PD (2003) Role of ESCRT-I in Retroviral Budding. Journal of Virology 77 : 4794–4804. 12663786
19. Garrus JE, Schwedler UKv, Pornillos OW, Morham SG, Zavitz KH, et al. (2001) Tsg101 and the Vacuolar Protein Sorting Pathway Are Essential for HIV-1 Budding. Cell 107 : 55–65. 11595185
20. Martin-Serrano J, Zang T, Bieniasz PD (2001) HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nature Medicine 7 : 1313–1319. 11726971
21. VerPlank L, Bouamr F, LaGrassa TJ, Agresta B, Kikonyogo A, et al. (2001) Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55Gag. PNAS 98 : 7724–7729. 11427703
22. Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD (2003) Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. PNAS 100 : 12414–12419. 14519844
23. Göttlinger HG, Dorfman T, Sodroski JG, Haseltine WA (1991) Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. PNAS 88 : 3195–3199. 2014240
24. Huang M, Orenstein JM, Martin MA, Freed EO (1995) p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. Jorunal of Virology 69 : 6810–6818 7474093
25. Fisher RD, Chung H-Y, Zhai Q, Robinson H, Sundquist WI, et al. (2007) Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding. Cell 128 : 841–852. 17350572
26. Fujii K, Munshi UM, Ablan SD, Demirov DG, Soheilian F, et al. (2009) Functional role of Alix in HIV-1 replication. Virology 391 : 284–292. doi: 10.1016/j.virol.2009.06.016 19596386
27. Munshi UM, Kim J, Nagashima K, Hurley JH, Freed EO (2007) An Alix Fragment Potently Inhibits HIV-1 Budding—CHARACTERIZATION OF BINDING TO RETROVIRAL YPXL LATE DOMAINS. The Journal of Biological Chemistry 282 : 3847–3855. 17158451
28. Usami Y, Popov S, Göttlinger HG (2007) Potent Rescue of Human Immunodeficiency Virus Type 1 Late Domain Mutants by ALIX/AIP1 Depends on Its CHMP4 Binding Site. Journal of Virology 81 : 6614–6622. 17428861
29. McCullough J, Fisher RD, Whitby FG, Sundquist WI, Hill CP (2008) ALIX-CHMP4 interactions in the human ESCRT pathway. PNAS 105 : 7687–7691. doi: 10.1073/pnas.0801567105 18511562
30. Pires R, Hartlieb B, Signor L, Schoehn G, Lata S, et al. (2009) A Crescent-Shaped ALIX Dimer Targets ESCRT-III CHMP4 Filaments. Structure 17 : 843–856. doi: 10.1016/j.str.2009.04.007 19523902
31. Guizetti J, Gerlich DW (2012) ESCRT-III polymers in membrane neck constriction. Trends in Cell Biology 22 : 133–140. doi: 10.1016/j.tcb.2011.11.007 22240455
32. Weissenhorn W, Göttlinger HG (2011) Essential Ingredients for HIV-1 Budding. Cell Host & Microbe 9 : 172–174. doi: 10.1016/j.fgb.2015.01.006 25626172
33. Hanson PI, Roth R, Lin Y, Heuser JE (2008) Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. JCB 180 : 389–402. doi: 10.1083/jcb.200707031 18209100
34. Saksena S, Wahlman J, Teis D, Johnson AE, Emr SD (2009) Functional Reconstitution of ESCRT-III Assembly and Disassembly. Cell 136 : 97–109. doi: 10.1016/j.cell.2008.11.013 19135892
35. Elia N, Sougrat R, Spurlin TA, Hurley JH, Lippincott-Schwartz J (2011) Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission. PNAS 108 : 4846–4851. doi: 10.1073/pnas.1102714108 21383202
36. Fabrikant G, Lata S, Riches JD, Briggs JAG, Weissenhorn W, et al. (2009) Computational Model of Membrane Fission Catalyzed by ESCRT-III. PLoS Computational Biology 5: e1000575. doi: 10.1371/journal.pcbi.1000575 19936052
37. Lata S, Schoehn G, Jain A, Pires R, Piehle J, et al. (2008) Helical Structures of ESCRT-III Are Disassembled by VPS4. Science 321 : 1354–1357. doi: 10.1126/science.1161070 18687924
38. Boura E, Różycki B, Chung HS, Herrick DZ, Canagarajah B, et al. (2012) Solution Structure of the ESCRT-I and -II Supercomplex: Implications for Membrane Budding and Scission. Structure 20 : 874–886. doi: 10.1016/j.str.2012.03.008 22579254
39. Bodon G, Chassefeyre R, Pernet-Gallay K, Martinelli N, Effantin G, et al. (2011) Charged Multivesicular Body Protein 2B (CHMP2B) of the Endosomal Sorting Complex Required for Transport-III (ESCRT-III) Polymerizes into Helical Structures Deforming the Plasma Membrane. The Journal of Biological Chemistry 286 : 40276–40286. doi: 10.1074/jbc.M111.283671 21926173
40. Cashikar AG, Shim S, Roth R, Maldazys MR, Heuser JE, et al. (2014) Structure of cellular ESCRT-III spirals and their relationship to HIV budding. eLife: e02184.
41. Dobro MJ, Samson RY, Yu Z, McCullough J, Ding HJ, et al. (2013) Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission. Mol Biol Cell 24 : 2319–2327. doi: 10.1091/mbc.E12-11-0785 23761076
42. Hanson PI, Shim S, Merrill SA (2009) Cell biology of the ESCRT machinery. Current Opinion in Cell Biology 21 : 568–574. doi: 10.1016/j.ceb.2009.06.002 19560911
43. Wollert T, Wunder C, Lippincott-Schwartz J, Hurley JH (2009) Membrane scission by the ESCRT-III complex. Nature 458 : 172–177. doi: 10.1038/nature07836 19234443
44. Wollert T, Hurley JH (2010) Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 464 : 864–869. doi: 10.1038/nature08849 20305637
45. Baumgärtel V, Ivanchenko S, Dupont A, Sergeev M, Wiseman PW, et al. (2011) Dynamics of HIV budding site interactions with an ESCRT component visualized in live-cells. Nature Cell Biology 13 : 469–474. doi: 10.1038/ncb2215 21394086
46. Wollert T, Hurley JH (2010) Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 464 : 864–869. doi: 10.1038/nature08849 20305637
47. Van Engelenburg SB, Shtengel G, Sengupta P, Waki K, Jarnik M, et al. (2014) Distribution of ESCRT machinery at HIV assembly sites reveals virus scaffolding of ESCRT subunits. Science 343 : 653–656. doi: 10.1126/science.1247786 24436186
48. Lampe M, Briggs JAG, Endress T, Glass B, Riegelsberger S, et al. (2007) Double-labelled HIV-1 particles for study of virus–cell interaction. Virology 360 : 92–104. 17097708
49. Ripley BD (1979) Tests of `Randomness' for Spatial Point Patterns. Journal of the Royal Statistical Society Series B (Methodological) 41 : 368–374.
50. Carlson L-A, Briggs JAG, Glass B, Riches JD, Simon MN, et al. (2008) Three-Dimensional Analysis of Budding Sites and Released Virus Suggests a Revised Model for HIV-1 Morphogenesis. Cell Host & Microbe 4 : 592–599. doi: 10.1016/j.fgb.2015.01.006 25626172
51. Carlson L-A, Marco Ad, Oberwinkler H, Habermann A, Briggs JAG, et al. (2010) Cryo Electron Tomography of Native HIV-1 Budding Sites. PLoS Pathogens 6: e1001173. doi: 10.1371/journal.ppat.1001173 21124872
52. Eckhardt M, Anders M, Muranyi W, Heilemann M, Krijnse-Locker J, et al. (2011) A SNAP-Tagged Derivative of HIV-1—A Versatile Tool to Study Virus-Cell Interactions. PLoS ONE 6: e22007. doi: 10.1371/journal.pone.0022007 21799764
53. Lehmann M, Rocha S, Mangeat B, Blanchet F, Uji-i H, et al. (2011) Quantitative Multicolor Super-Resolution Microscopy Reveals Tetherin HIV-1 Interaction. PLoS Pathogens 7: e1002456. doi: 10.1371/journal.ppat.1002456 22194693
54. Malkusch S, Muranyi W, Muller B, Krausslich HG, Heilemann M (2013) Single-molecule coordinate-based analysis of the morphology of HIV-1 assembly sites with near-molecular spatial resolution. Histochem Cell Biol 139 : 173–179. doi: 10.1007/s00418-012-1014-4 22910843
55. Kiskowski MA, Hancock JF, Kenworthy AK (2009) On the use of Ripley's K-function and its derivatives to analyze domain size. Biophys J 97 : 1095–1103. doi: 10.1016/j.bpj.2009.05.039 19686657
56. Lavallée C, Yao XJ, Ladha A, Göttlinger H, Haseltine WA, et al. (1994) Requirement of the Pr55gag precursor for incorporation of the Vpr product into human immunodeficiency virus type 1 viral particles. Jorunal of Virology 68 : 1926–1934. 8107252
57. Bachand F, Yao X-J, Hrimech M, Rougeau N, Cohen ÉA (1999) Incorporation of Vpr into Human Immunodeficiency Virus Type 1 Requires a Direct Interaction with the p6 Domain of the p55 Gag Precursor*. The Journal of Biological Chemistry 274 : 9083–9091. 10085158
58. Müller B, Tessmer U, Schubert U, Kräusslich H-G (2000) Human Immunodeficiency Virus Type 1 Vpr Protein Is Incorporated into the Virion in Significantly Smaller Amounts than Gag and Is Phosphorylated in Infected Cells. Journal of Virology 74 : 9727–9731. 11000245
59. Hermida-Matsumoto L, Resh MD (2000) Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J Virol 74 : 8670–8679. 10954568
60. Ku P-I, Bendjennat M, Ballew J, Landesman MB, Saffarian S (2014) ALIX Is Recruited Temporarily into HIV-1 Budding Sites at the End of Gag Assembly. PLoS ONE 9: e96950. doi: 10.1371/journal.pone.0096950 24834918
61. Welsch S, Habermann A, Jäger S, Müller B, Krijnse-Locker J, et al. (2006) Ultrastructural Analysis of ESCRT Proteins Suggests a Role for Endosome-Associated Tubular–Vesicular Membranes in ESCRT Function. Traffic 7 : 1551–1566. 17014699
62. Baietti MF, Zhang Z, Mortier E, Melchior A, Degeest G, et al. (2012) Syndecan–syntenin–ALIX regulates the biogenesis of exosomes. Nature Cell Biology 14 : 677–685. doi: 10.1038/ncb2502 22660413
63. Hurley JH, Odorizzi G (2012) Get on the exosome bus with ALIX. Nature Cell Biology 14 : 654–655. doi: 10.1038/ncb2530 22743708
64. Dussupt V, Javid MP, Abou-Jaoudé G, Jadwin JA, Cruz JdL, et al. (2009) The Nucleocapsid Region of HIV-1 Gag Cooperates with the PTAP and LYPXnL Late Domains to Recruit the Cellular Machinery Necessary for Viral Budding. PLoS Pathogens 5: e1000339. doi: 10.1371/journal.ppat.1000339 19282983
65. Zhai Q, Fisher RD, Chung H-Y, Myszka DG, Sundquist WI, et al. (2008) Structural and functional studies of ALIX interactions with YPXnL late domains of HIV-1 and EIAV. Nat Struct Mol Biol 15 : 43–49. 18066081
66. Popov S, Popova E, Inoue M, Göttlinger HG (2008) Human Immunodeficiency Virus Type 1 Gag Engages the Bro1 Domain of ALIX/AIP1 through the Nucleocapsid. Journal of Virology 82 : 1389–1398. 18032513
67. Chertova E, Chertov O, Coren LV, Roser JD, Trubey CM, et al. (2006) Proteomic and Biochemical Analysis of Purified Human Immunodeficiency Virus Type 1 Produced from Infected Monocyte-Derived Macrophages Jorunal of Virology 80 : 9039–9052. 16940516
68. Zhang F, Zang T, Wilson SJ, Johnson MC, Bieniasz PD (2011) Clathrin Facilitates the Morphogenesis of Retrovirus Particles PLoS Pathogens 7: e1002119. doi: 10.1371/journal.ppat.1002119 21738476
69. Zhou X, Si J, Corvera J, Gallick GE, Kuang J (2010) Decoding the intrinsic mechanism that prohibits ALIX interaction with ESCRT and viral proteins. Biochemical Journal 432 : 525–534. doi: 10.1042/BJ20100862 20929444
70. Zhou X, Pan S, Sun L, Corvera J, Lee Y-C, et al. (2009) The CHMP4b - and Src-docking sites in the Bro1 domain are autoinhibited in the native state of Alix. Biochemical Journal 418 : 277–284. doi: 10.1042/BJ20081388 19016654
71. Zhai Q, Landesman MB, Chung H-Y, Dierkers A, Jeffries CM, et al. (2011) Activation of the Retroviral Budding Factor ALIX. Jorunal of Virology 85 : 9222–9226. doi: 10.1128/JVI.02653-10 21715492
72. Effantin G, Dordor A, Sandrin V, Martinelli N, Sundquist WI, et al. (2013) ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cellular Microbiology 15 : 213–226. doi: 10.1111/cmi.12041 23051622
73. Bleck M, Itano MS, Johnson DS, Thomas VK, North AJ, et al. (2014) Temporal and spatial organization of ESCRT protein recruitment during HIV-1 budding. PNAS 111 : 12211–12216. doi: 10.1073/pnas.1321655111 25099357
74. Zamborlini A, Usami Y, Radoshitzky SR, Popova E, Palu G, et al. (2006) Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding. Proc Natl Acad Sci U S A 103 : 19140–19145. 17146056
75. Galbraith CG, Galbraith JA (2011) Super-resolution microscopy at a glance. J Cell Sci 124 : 1607–1611. doi: 10.1242/jcs.080085 21536831
76. Lelek M, Nunzio FD, Henriques R, Charneau P, Arhel N, et al. (2012) Superresolution imaging of HIV in infected cells with FlAsH-PALM. PNAS 109 : 8564–8569. doi: 10.1073/pnas.1013267109 22586087
77. Graf M, Bojak A, Deml L, Bieler K, Wolf H, et al. (2000) Concerted action of multiple cis-acting sequences is required for Rev dependence of late human immunodeficiency virus type 1 gene expression. J Virol 74 : 10822–10826. 11044131
78. Waldhuber MG, Bateson M, Tan J, Greenway AL, McPhee DA (2003) Studies with GFP-Vpr fusion proteins: induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization. Virology 313 : 91–104. 12951024
79. Usami Y, Popov S, Weiss ER, Vriesema-Magnuson C, Calistri A, et al. (2012) Regulation of CHMP4/ESCRT-III Function in Human Immunodeficiency Virus Type 1 Budding by CC2D1A. Journal of Virology 86 : 3746–3756. doi: 10.1128/JVI.06539-11 22258254
80. Dempsey GT, Vaughan JC, Chen KH, Bates M, Zhuang X (2011) Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging. Nature Methods 8 : 1027–1036. doi: 10.1038/nmeth.1768 22056676
81. Rust MJ, Bates M, Zhuang X (2006) Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nature Methods 3 : 793–795. 16896339
82. Bates M, Huang B, Dempsey GT, Zhuang X (2007) Multicolor Super-Resolution Imaging with Photo-Switchable Fluorescent Probes. Science 317 : 1749–1753. 17702910
83. Schindelin J, Arganda-Carreras I, Frise E, Kaynig V, Longair M, et al. (2012) Fiji: an open-source platform for biological-image analysis. Nature Methods 9 : 676–682. doi: 10.1038/nmeth.2019 22743772
84. Sternberg SR (1983) Biomedical Image Processing. Computer 16 : 22–34.
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