Generating Vectors for the Lattice Structures of Tubular and Conical Viral Capsids
Farrah Sadre-Marandi; Jiangguo Liu; Simon Tavener; Chaoping Chen
Molecular Based Mathematical Biology (2014)
- Volume: 2, Issue: 1
- ISSN: 2299-3266
Access Full Article
topAbstract
topHow to cite
topFarrah Sadre-Marandi, et al. "Generating Vectors for the Lattice Structures of Tubular and Conical Viral Capsids." Molecular Based Mathematical Biology 2.1 (2014): null. <http://eudml.org/doc/268690>.
@article{FarrahSadre2014,
abstract = {Retrovirus capsid is a fullerene-like lattice consisting of capsid protein hexamers and pentamers. Mathematical models for the lattice structure help understand the underlying biological mechanisms in the formation of viral capsids. It is known that viral capsids could be categorized into three major types: icosahedron, tube, and cone. While the model for icosahedral capsids is established and well-received, models for tubular and conical capsids need further investigation. This paper proposes new models for the tubular and conical capsids based on an extension of the Capser-Klug quasi-equivalence theory. In particular, two and three generating vectors are used to characterize respectively the lattice structures of tubular and conical capsids. Comparison with published HIV-1 data demonstrates a good agreement of our modeling results with experimental data.},
author = {Farrah Sadre-Marandi, Jiangguo Liu, Simon Tavener, Chaoping Chen},
journal = {Molecular Based Mathematical Biology},
keywords = {CA protein; capsid; cone; hexamer; HIV-1; icosahedron; pentamer; tube},
language = {eng},
number = {1},
pages = {null},
title = {Generating Vectors for the Lattice Structures of Tubular and Conical Viral Capsids},
url = {http://eudml.org/doc/268690},
volume = {2},
year = {2014},
}
TY - JOUR
AU - Farrah Sadre-Marandi
AU - Jiangguo Liu
AU - Simon Tavener
AU - Chaoping Chen
TI - Generating Vectors for the Lattice Structures of Tubular and Conical Viral Capsids
JO - Molecular Based Mathematical Biology
PY - 2014
VL - 2
IS - 1
SP - null
AB - Retrovirus capsid is a fullerene-like lattice consisting of capsid protein hexamers and pentamers. Mathematical models for the lattice structure help understand the underlying biological mechanisms in the formation of viral capsids. It is known that viral capsids could be categorized into three major types: icosahedron, tube, and cone. While the model for icosahedral capsids is established and well-received, models for tubular and conical capsids need further investigation. This paper proposes new models for the tubular and conical capsids based on an extension of the Capser-Klug quasi-equivalence theory. In particular, two and three generating vectors are used to characterize respectively the lattice structures of tubular and conical capsids. Comparison with published HIV-1 data demonstrates a good agreement of our modeling results with experimental data.
LA - eng
KW - CA protein; capsid; cone; hexamer; HIV-1; icosahedron; pentamer; tube
UR - http://eudml.org/doc/268690
ER -
References
top- [1] J. Benjamin, B.K. Ganser-Pornillos,W.F. Tivol,W.I. Sundquist, and G.J. Jensen, Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography. J. Mol. Biol. 346(2005), 577–588.
- [2] J. Briggs, K. Grünewald, B. Glass, F. Förster, H-G. Kräusslich, and S.D. Fuller, The mechanism of HIV-1 core assembly: Insights from three-dimensional reconstructions of authentic virions. Structure 14(2006), 15–20.
- [3] J. Briggs and H. Krausslich, The molecular architecture of HIV. J. Mol. Biol. 410(2011), 491–500.
- [4] J. Briggs, T. Wilk, R. Welker, H-G. Kräusslich, and S.D. Fuller, Structural organization of authentic, mature HIV-1 virions and cores. EMBO 22(2003), 1707–1715.
- [5] C. Büchen-Osmond, ICTVdB - The universal virus database, Version 4, ICTVdB Management, New York, 2006.
- [6] I.L. Byeon, X. Meng, J. Jung, G. Zhao, R. Yang, J. Ahn, J. Shi, J. Concel, C. Aiken, P. Zhang, and A.M. Gronenborn, Structural convergence between cryo-EM and NMR reveals intersubunit interations critical for HIV-1 capsid function. Cell 139(2009), 780–790. [WoS]
- [7] D. Caspar and A. Klug, Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27(1962), 1–24. [Crossref]
- [8] T. Douglas and M. Young, Virus: Making friends with old foes. Science 312(2006), 873–875.
- [9] O.M. Elrad and M.F. Hagan, Encapsulation of a polymer by an icosahedral virus. Phys. Biol. 7(2010), 045003. [Crossref][WoS][PubMed]
- [10] A. de la Escosura, R. Nolte, and J. Cornelissen, Viruses and protein cages as nanocontainers and nanoreactors. J. Mater. Chem. 19(2009), 2274–2278. [WoS]
- [11] B.K. Ganser, S. Li, V.Y. Klishko, J.T. Finch, and W.I. Sundquist, Assembly and analysis of conical models for the HIV-1 core. Science 80(1999), 80–83.
- [12] B.K. Ganser-Pornillos, M. Yeager, and O. Pornillos, Assembly and architecture of HIV. Adv. Exp. Med. Biol. 726(2012), 441– 465.
- [13] Y. Gogotsi, Nanomaterial Handbook, Taylor & Francis Group, Florida, 2006.
- [14] J. Heymann, C. Butan, D. Winkler, R. Craven, and A. Steven, Irregular and semi-regular polyhedral models for Rous sarcoma virus cores. Comput. Math. Meth. Med. 9(2008), 197–210. [WoS][Crossref] Zbl1160.92021
- [15] Y. Hu, R. Zandi, A. Anavitarte, C.M. Knobler, andW.M. Gelbart, Packaging of a polymer by a viral capsid: The interplay between polymer length and capsid size. Biophys. J. 94(2008), 1428–1436. [Crossref][WoS]
- [16] J. Liu, F. Sadre-Marandi, S. Tavener, and C. Chen, Curvature concentrations on the HIV-1 capsid. Preprint, Colorado State University, (2014).
- [17] A. Luque and D. Reguera, The structure of elongated viral capsids. Biophys. J. 98(2010), 2993–3003. [WoS][PubMed][Crossref]
- [18] E.R. May, J. Feng, and C.L. Brooks III, Exploring the symmetry and mechanism of virus capsid maturation via an ensemble of pathways. Biophys. J. 102(2012), 606–612. [WoS][Crossref]
- [19] M.F. Moody, The shape of the T-even bacteriophage head. Virology 26(1965), 567–576. [Crossref]
- [20] M.F. Moody, Geometry of phage head construction. J. Mol. Biol. 293(1999), 401–433.
- [21] T.T. Nguyen, R.F. Bruinsma, and W.M. Gelbart, Elasticity theory and shape transitions of viral shells. Phys. Rev. E 72(2005), 1–19. [WoS]
- [22] J.K. Pokorski and N.F. Steinmetz, The art of engineering viral nanoparticles. Mol. Pharma. 8(2011), 29–43. [Crossref]
- [23] O. Pornillos, B.K. Ganser-Pornillos, and M. Yeager, Atomic-level modelling of the HIV capsid. Nature (Letter) 469(2011), 424– 428. [WoS]
- [24] A. Siber, Continuum and all-atom description of the energetics of graphene nanocones. Nanotech. 18(2007), 1–6.
- [25] Y. Tao, N.H. Olson,W. Xu, D.L. Anderson, M.G. Rossmann, and T.S. Baker, Assembly of a tailed bacterial virus and its genome release studied in there dimensions. Cell 95(1998), 431–437. [Crossref][PubMed]
- [26] B. Turner and M. Summers, Structural biology of HIV. J. Mol. Biol. 285(1999), 1–32.
- [27] R. Welker, H. Hohenberg, U. Tessmer, C. Huckhagel, and H-G. Kräusslich, Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J. Virol. 74(2000), 1168–1177. [Crossref]
- [28] F.F. Xu, Y. Bando, and D. Golberg, The tubular conical helix of graphitic boron nitride. New J. Phys. 5(2003), 1–16.
- [29] R. Zandi, D. Reguera, R. Bruinsma, W. Gelbart, and J. Rudnick, Origin of icosahedral symmetry in viruses. PNAS 101(2004), 15556–15560.
- [30] G. Zhao, J. Perilla, E. Yufenyuy, X. Meng, B. Chen, J. Ning, J. Ahn, A. Gronenborn, K. Schulten, C. Aiken, and P. Zhang, Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature (Letter) 497(2013), 642–646.
- [31] www.thebacteriophages.org/chapters/0180_figure_003.htm
NotesEmbed ?
topTo embed these notes on your page include the following JavaScript code on your page where you want the notes to appear.