Skip to main content
SpringerLink
Log in
Book cover

The Future of HIV-1 Therapeutics pp 243–252Cite as

Illustrations of the HIV Life Cycle

Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY,volume 389)

Abstract

Illustrations of the HIV Life Cycle. The illustrations include proteins, nucleic acids and membranes; small molecules and water are omitted for clarity. Host cell molecules are shown in shades of blue and green and blood plasma proteins are shown in shades of tan and brown. HIV proteins are shown in red and magenta, HIV RNA is in yellow and HIV DNA is in yellow-green. The 3D model of the mature virion was generated using CellPACK by Graham Johnson

Illustrations of the major steps of HIV life cycle are presented that integrate information from structural and biophysical studies. The illustrations depict HIV and its interaction with its cellular host at a magnification that reveals all macromolecules. This report describes the sources of scientific support for the structures and processes shown in the illustrations.

Keywords

  • Nuclear Pore Complex
  • Primer Binding Site
  • Immature Virion
  • Myristoyl Group
  • Reverse Transcription Complex

These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

This is a preview of subscription content, access via your institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

References

  • Ambrose Z, Aiken C (2014) HIV-1 uncoating: connection to nuclear entry and regulation by host proteins. Virology 454–455:371–379. doi:10.1016/j.virol.2014.02.004, [pii] S0042-6822(14)00048-8

  • Balasubramaniam M, Freed EO (2011) New insights into HIV assembly and trafficking. Physiology (Bethesda) 26(4):236-251. doi:10.1152/physiol.00051.2010, [pii] 26/4/236

  • Bell NM, Lever AM 2013 HIV Gag polyprotein: processing and early viral particle assembly. Trends Microbiol 21(3):136–144. doi:10.1016/j.tim.2012.11.006, [pii] S0966-842X(12)00212-0

  • Brierley I, Dos Ramos FJ (2006) Programmed ribosomal frameshifting in HIV-1 and the SARS-CoV. Virus Res 119 (1):29-42. doi:10.1016/j.virusres.2005.10.008, [pii] S0168-1702(05)00321-7

  • Briggs JA, Krausslich HG (2011) The molecular architecture of HIV. J Mol Biol 410 (4):491–500. doi:10.1016/j.jmb.2011.04.021, [pii] S0022-2836(11)00436-0

  • Briggs JA, Simon MN, Gross I, Krausslich HG, Fuller SD, Vogt VM, Johnson MC (2004) The stoichiometry of Gag protein in HIV-1. Nat Struct Mol Biol 11 (7):672–675. doi:10.1038/nsmb785, [pii] nsmb785

  • Checkley MA, Luttge BG, Freed EO (2011) HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J Mol Biol 410 (4):582–608. doi:10.1016/j.jmb.2011.04.042, [pii] S0022-2836(11)00471-2

  • Chojnacki J, Staudt T, Glass B, Bingen P, Engelhardt J, Anders M, Schneider J, Muller B, Hell SW, Krausslich HG (2012) Maturation-dependent HIV-1 surface protein redistribution revealed by fluorescence nanoscopy. Science 338 (6106):524–528. doi:10.1126/science.1226359, [pii] 338/6106/524

  • Datta SA, Curtis JE, Ratcliff W, Clark PK, Crist RM, Lebowitz J, Krueger S, Rein A (2007) Conformation of the HIV-1 Gag protein in solution. J Mol Biol 365 (3):812–824. doi:10.1016/j.jmb.2006.10.073, [pii] S0022-2836(06)01453-7

  • de Marco A, Muller B, Glass B, Riches JD, Krausslich HG, Briggs JA (2010) Structural analysis of HIV-1 maturation using cryo-electron tomography. PLoS Pathog 6(11):e1001215. doi:10.1371/journal.ppat.1001215

    CrossRef  PubMed Central  PubMed  Google Scholar 

  • Di Nunzio F (2013) New insights in the role of nucleoporins: a bridge leading to concerted steps from HIV-1 nuclear entry until integration. Virus Res 178 (2):187–196. doi:10.1016/j.virusres.2013.09.003, [pii] S0168-1702(13)00295-5

  • Diribarne G, Bensaude O (2009) 7SK RNA, a non-coding RNA regulating P-TEFb, a general transcription factor. RNA Biol 6 (2):122–128, [pii] 8115

    Google Scholar 

  • Engelman A, Cherepanov P (2012) The structural biology of HIV-1: mechanistic and therapeutic insights. Nat Rev Microbiol 10 (4):279–290. doi:10.1038/nrmicro2747, [pii] nrmicro2747

  • Fassati A (2012) Multiple roles of the capsid protein in the early steps of HIV-1 infection. Virus Res 170 (1–2):15–24. doi:10.1016/j.virusres.2012.09.012, [pii] S0168-1702(12)00365-6

  • Fernandes J, Jayaraman B, Frankel A (2012) The HIV-1 Rev response element: an RNA scaffold that directs the cooperative assembly of a homo-oligomeric ribonucleoprotein complex. RNA Biol 9 (1):6–11. doi:10.4161/rna.9.1.18178, [pii] 18178

  • Fisher RJ, Rein A, Fivash M, Urbaneja MA, Casas-Finet JR, Medaglia M, Henderson LE (1998) Sequence-specific binding of human immunodeficiency virus type 1 nucleocapsid protein to short oligonucleotides. J Virol 72(3):1902–1909

    PubMed Central  CAS  PubMed  Google Scholar 

  • Ganser-Pornillos BK, Yeager M, Pornillos O (2012) Assembly and architecture of HIV. Adv Exp Med Biol 726:441–465. doi:10.1007/978-1-4614-0980-9_20

    CrossRef  CAS  PubMed  Google Scholar 

  • Ganser-Pornillos BK, Yeager M, Sundquist WI (2008) The structural biology of HIV assembly. Curr Opin Struct Biol 18 (2):203–217. doi:10.1016/j.sbi.2008.02.001, [pii] S0959-440X(08)00028-6

  • Gaudin R, de Alencar BC, Arhel N, Benaroch P (2013) HIV trafficking in host cells: motors wanted! Trends Cell Biol 23 (12):652–662. doi:10.1016/j.tcb.2013.09.004, [pii] S0962-8924(13)00156-6

  • Goodsell DS (2009) The machinery of life, 2nd edn. Springer, New York

    CrossRef  Google Scholar 

  • Goodsell DS (2011) Eukaryotic cell panorama. Biochem Mol Biol Educ 39(2):91–101. doi:10.1002/bmb.20494

    CrossRef  CAS  PubMed  Google Scholar 

  • Goodsell DS (2012) Illustrating the machinery of life: viruses. Biochem Mol Biol Educ 40(5):291–296. doi:10.1002/bmb.20636

    CrossRef  CAS  PubMed  Google Scholar 

  • Henne WM, Buchkovich NJ, Emr SD (2011) The ESCRT pathway. Dev Cell 21 (1):77–91. doi:10.1016/j.devcel.2011.05.015, [pii] S1534-5807(11)00207-3

  • Herschhorn A, Hizi A (2010) Retroviral reverse transcriptases. Cell Mol Life Sci 67(16):2717–2747. doi:10.1007/s00018-010-0346-2

    CrossRef  CAS  PubMed  Google Scholar 

  • Hughes SH (2014) Reverse transcription of retroviruses and LTR retrotransposons. Microbiol Spectr 2(5):MDNA3-0027–2014

    Google Scholar 

  • Hurley JH, Hanson PI (2010) Membrane budding and scission by the ESCRT machinery: it’s all in the neck. Nat Rev Mol Cell Biol 11 (8):556–566. doi:10.1038/nrm2937, [pii] nrm2937

  • Ivanchenko S, Godinez WJ, Lampe M, Krausslich HG, Eils R, Rohr K, Brauchle C, Muller B, Lamb DC (2009) Dynamics of HIV-1 assembly and release. PLoS Pathog 5(11):e1000652. doi:10.1371/journal.ppat.1000652

    CrossRef  PubMed Central  PubMed  Google Scholar 

  • Johnson GT, Autin L, Al-Alusi M, Goodsell DS, Sanner MF, Olson AJ (2015) cellPACK: a virtual mesoscope to model and visualize structural systems biology. Nat Methods 12 (1):85–91. doi:10.1038/nmeth.3204, [pii] nmeth.3204

  • Johnson GT, Goodsell DS, Autin L, Forli S, Sanner MF, Olson AJ (2014) 3D molecular models of whole HIV-1 virions generated with cellPACK. Faraday Discuss 169:23–44. doi:10.1039/c4fd00017j

    CrossRef  CAS  PubMed  Google Scholar 

  • Julien JP, Lee PS, Wilson IA (2012) Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA. Immunol Rev 250(1):180–198. doi:10.1111/imr.12005

    CrossRef  PubMed Central  PubMed  Google Scholar 

  • Karn J, Stoltzfus CM (2012) Transcriptional and posttranscriptional regulation of HIV-1 gene expression. Cold Spring Harb Perspect Med 2 (2):a006916. doi:10.1101/cshperspect.a006916, [pii] a006916

  • Klasse PJ (2012) The molecular basis of HIV entry. Cell Microbiol 14(8):1183–1192. doi:10.1111/j.1462-5822.2012.01812.x

    CrossRef  PubMed Central  CAS  PubMed  Google Scholar 

  • Krishnan L, Engelman A (2012) Retroviral integrase proteins and HIV-1 DNA integration. J Biol Chem 287 (49):40858–40866. doi:10.1074/jbc.R112.397760, [pii] R112.397760

  • Lim RY, Aebi U, Fahrenkrog B (2008) Towards reconciling structure and function in the nuclear pore complex. Histochem Cell Biol 129(2):105–116. doi:10.1007/s00418-007-0371-x

    CrossRef  PubMed Central  CAS  PubMed  Google Scholar 

  • Maertens GN, Hare S, Cherepanov P (2010) The mechanism of retroviral integration from X-ray structures of its key intermediates. Nature 468 (7321):326–329. doi:10.1038/nature09517, [pii] nature09517

  • Maillot B, Levy N, Eiler S, Crucifix C, Granger F, Richert L, Didier P, Godet J, Pradeau-Aubreton K, Emiliani S, Nazabal A, Lesbats P, Parissi V, Mely Y, Moras D, Schultz P, Ruff M (2013) Structural and functional role of INI1 and LEDGF in the HIV-1 preintegration complex. PLoS ONE 8 (4):e60734. doi:10.1371/journal.pone.0060734, [pii] PONE-D-12-31606

  • Mangus DA, Evans MC, Jacobson A (2003) Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol 4(7):223. doi:10.1186/gb-2003-4-7-223

    CrossRef  PubMed Central  PubMed  Google Scholar 

  • McCullough J, Colf LA, Sundquist WI (2013) Membrane fission reactions of the mammalian ESCRT pathway. Annu Rev Biochem 82:663–692. doi:10.1146/annurev-biochem-072909-101058

    CrossRef  PubMed Central  CAS  PubMed  Google Scholar 

  • Michel F, Crucifix C, Granger F, Eiler S, Mouscadet JF, Korolev S, Agapkina J, Ziganshin R, Gottikh M, Nazabal A, Emiliani S, Benarous R, Moras D, Schultz P, Ruff M (2009) Structural basis for HIV-1 DNA integration in the human genome, role of the LEDGF/P75 cofactor. EMBO J 28 (7):980–991. doi:10.1038/emboj.2009.41, [pii] emboj200941

  • Muller B, Tessmer U, Schubert U, Krausslich HG (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. J Virol 74(20):9727–9731

    CrossRef  PubMed Central  CAS  PubMed  Google Scholar 

  • O’Carroll IP, Soheilian F, Kamata A, Nagashima K, Rein A (2013) Elements in HIV-1 Gag contributing to virus particle assembly. Virus Res 171 (2):341–345. doi:10.1016/j.virusres.2012.10.016, [pii] S0168-1702(12)00405-4

  • Onafuwa-Nuga AA, Telesnitsky A, King SR (2006) 7SL RNA, but not the 54-kd signal recognition particle protein, is an abundant component of both infectious HIV-1 and minimal virus-like particles. RNA 12 (4):542–546. doi:10.1261/rna.2306306, [pii] rna.2306306

  • Ott DE (2008) Cellular proteins detected in HIV-1. Rev Med Virol 18(3):159–175. doi:10.1002/rmv.570

    CrossRef  CAS  PubMed  Google Scholar 

  • Ott M, Geyer M, Zhou Q (2011) The control of HIV transcription: keeping RNA polymerase II on track. Cell Host Microbe 10 (5):426–435. doi:10.1016/j.chom.2011.11.002, [pii] S1931-3128(11)00336-2

  • Pettit SC, Simsic J, Loeb DD, Everitt L, Hutchison CA 3rd, Swanstrom R (1991) Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid. J Biol Chem 266(22):14539–14547

    CAS  PubMed  Google Scholar 

  • Popowicz GM, Schleicher M, Noegel AA, Holak TA (2006) Filamins: promiscuous organizers of the cytoskeleton. Trends Biochem Sci 31 (7):411–419. doi:10.1016/j.tibs.2006.05.006, [pii] S0968-0004(06)00140-X

  • Ratner L, Haseltine W, Patarca R, Livak KJ, Starcich B, Josephs SF, Doran ER, Rafalski JA, Whitehorn EA, Baumeister K et al (1985) Complete nucleotide sequence of the AIDS virus. HTLV-III. Nature 313(6000):277–284

    CrossRef  CAS  Google Scholar 

  • Rocha-Perugini V, Gordon-Alonso M, Sanchez-Madrid F (2014) PIP2: choreographer of actin-adaptor proteins in the HIV-1 dance. Trends Microbiol 22 (7):379–388. doi:10.1016/j.tim.2014.03.009, [pii] S0966-842X(14)00071-7

  • Saad JS, Miller J, Tai J, Kim A, Ghanam RH, Summers MF (2006) Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc Natl Acad Sci U S A 103 (30):11364–11369. doi:10.1073/pnas.0602818103, [pii] 0602818103

  • Schweitzer CJ, Jagadish T, Haverland N, Ciborowski P, Belshan M (2013) Proteomic analysis of early HIV-1 nucleoprotein complexes. J Proteome Res 12(2):559–572. doi:10.1021/pr300869h

    CrossRef  PubMed Central  CAS  PubMed  Google Scholar 

  • Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136 (4):731–745. doi:10.1016/j.cell.2009.01.042, [pii] S0092-8674(09)00090-7

  • Sundquist WI, Krausslich HG (2012) HIV-1 assembly, budding, and maturation. Cold Spring Harb Perspect Med 2 (7):a006924. doi:10.1101/cshperspect.a006924, [pii] a006924

  • Tang C, Louis JM, Aniana A, Suh JY, Clore GM (2008) Visualizing transient events in amino-terminal autoprocessing of HIV-1 protease. Nature 455 (7213):693–696. doi:10.1038/nature07342, [pii] nature07342

  • Votteler J, Sundquist WI (2013) Virus budding and the ESCRT pathway. Cell Host Microbe 14 (3):232–241. doi:10.1016/j.chom.2013.08.012, [pii] S1931-3128(13)00294-1

  • Waheed AA, Freed EO (2012) HIV type 1 Gag as a target for antiviral therapy. AIDS Res Hum Retroviruses 28(1):54–75. doi:10.1089/AID.2011.0230

    CrossRef  PubMed Central  CAS  PubMed  Google Scholar 

  • Warrilow D, Tachedjian G, Harrich D (2009) Maturation of the HIV reverse transcription complex: putting the jigsaw together. Rev Med Virol 19(6):324–337. doi:10.1002/rmv.627

    CrossRef  CAS  PubMed  Google Scholar 

  • Wright ER, Schooler JB, Ding HJ, Kieffer C, Fillmore C, Sundquist WI, Jensen GJ (2007) Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J 26 (8):2218–2226. doi:10.1038/sj.emboj.7601664, [pii] 7601664

  • Yazaki K, Yoshida T, Wakiyama M, Miura K (2000) Polysomes of eukaryotic cells observed by electron microscopy. J Electron Microsc (Tokyo) 49(5):663–668

    CrossRef  CAS  Google Scholar 

  • Zhu P, Liu J, Bess J Jr, Chertova E, Lifson JD, Grise H, Ofek GA, Taylor KA, Roux KH (2006) Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441 (7095):847–852. doi:10.1038/nature04817, [pii] nature04817

Download references

Acknowledgments

This work was supported by NIH (P50GM-103368) to the HIV Interaction and Viral Evolution Center. I thank Stephen Hughes, John Coffin, Stefan Sarafianos, Alan Engelman and Arthur Olson for insightful discussions.

Author information

Authors and Affiliations

  1. Department of Integrative Structural and Computational Biology and RCSB Protein Data Bank, The Scripps Research Institute, La Jolla, 92037, CA, USA

    David S. Goodsell

Authors
  1. David S. Goodsell
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to David S. Goodsell .

Editor information

Editors and Affiliations

  1. Departments of Molecular and Experimental Medicine and Immunology and Microbial Science (MEM 131), The Scripps Research Institute, La Jolla, California, USA

    Bruce E. Torbett

  2. Department of Integrative Structural and Computational Biology, and RCSB Protein Data Bank, The Scripps Research Institute, La Jolla, California, USA

    David S. Goodsell

  3. Department of Pathology, University of California, San Diego, La Jolla, California, USA

    Douglas D. Richman

Rights and permissions

Reprints and Permissions

Copyright information

© 2015 Springer International Publishing Switzerland

About this chapter

Cite this chapter

Goodsell, D.S. (2015). Illustrations of the HIV Life Cycle. In: Torbett, B., Goodsell, D., Richman, D. (eds) The Future of HIV-1 Therapeutics. Current Topics in Microbiology and Immunology, vol 389. Springer, Cham. https://doi.org/10.1007/82_2015_437

Download citation

search

Navigation