#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

Structure Elucidation of Coxsackievirus A16 in Complex with GPP3 Informs a Systematic Review of Highly Potent Capsid Binders to Enteroviruses


Our research provides new insights into the design of inhibitors for the treatment of different pathogenic enterovirus infections.


Vyšlo v časopise: Structure Elucidation of Coxsackievirus A16 in Complex with GPP3 Informs a Systematic Review of Highly Potent Capsid Binders to Enteroviruses. PLoS Pathog 11(10): e32767. doi:10.1371/journal.ppat.1005165
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1005165

Souhrn

Our research provides new insights into the design of inhibitors for the treatment of different pathogenic enterovirus infections.


Zdroje

1. Zeng M, Li YF, Wang XH, Lu GP, Shen HG, et al. (2012) Epidemiology of hand, foot, and mouth disease in children in Shanghai 2007–2010. Epidemiol Infect 140: 1122–1130. doi: 10.1017/S0950268811001622 21878145

2. Wong SS, Yip CC, Lau SK, Yuen KY (2010) Human enterovirus 71 and hand, foot and mouth disease. Epidemiol Infect 138: 1071–1089. doi: 10.1017/S0950268809991555 20056019

3. Chen X, Tan X, Li J, Jin Y, Gong L, et al. (2013) Molecular epidemiology of coxsackievirus A16: intratype and prevalent intertype recombination identified. PLoS One 8: e82861. doi: 10.1371/journal.pone.0082861 24340064

4. Dang M, Wang X, Wang Q, Wang Y, Lin J, et al. (2014) Molecular mechanism of SCARB2-mediated attachment and uncoating of EV71. Protein Cell 5: 692–703. doi: 10.1007/s13238-014-0087-3 24986489

5. Wang X, Peng W, Ren J, Hu Z, Xu J, et al. (2012) A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nature structural & molecular biology 19: 424–429. doi: 10.1016/j.psychres.2015.09.034

6. Ren J, Wang X, Hu Z, Gao Q, Sun Y, et al. (2013) Picornavirus uncoating intermediate captured in atomic detail. Nat Commun 4: 1929. doi: 10.1038/ncomms2889 23728514

7. Strauss M, Filman DJ, Belnap DM, Cheng N, Noel RT, et al. (2015) Nectin-Like Interactions between Poliovirus and Its Receptor Trigger Conformational Changes Associated with Cell Entry. Journal of virology 89: 4143–4157. doi: 10.1128/JVI.03101-14 25631086

8. De Colibus L, Wang X, Spyrou JAB, Kelly J, Ren J, et al. (2014) More-powerful virus inhibitors from structure-based analysis of HEV71 capsid-binding molecules. Nature structural & molecular biology 21: 282–288. doi: 10.1016/j.psychres.2015.09.034

9. Axford D, Owen RL, Aishima J, Foadi J, Morgan AW, et al. (2012) In situ macromolecular crystallography using microbeams. Acta crystallographica Section D, Biological crystallography 68: 592–600. doi: 10.1107/S0907444912006749 22525757

10. Ren J, Wang X, Zhu L, Hu Z, Gao Q, et al. (2015) Structures of coxsackievirus A16 capsids with native antigenicity, implications for particle expansion, receptor binding and immunogenicity. J Virol.

11. Winn MD, Ballard CC, Cowtan KD, Dodson EJ, Emsley P, et al. (2011) Overview of the CCP4 suite and current developments. Acta crystallographica Section D, Biological crystallography 67: 235–242. doi: 10.1107/S0907444910045749 21460441

12. Cho AE, Guallar V, Berne BJ, Friesner R (2005) Importance of accurate charges in molecular docking: quantum mechanical/molecular mechanical (QM/MM) approach. J Comput Chem 26: 915–931. 15841474

13. Miller ST, Hogle JM, Filman DJ (2001) Ab initio phasing of high-symmetry macromolecular complexes: successful phasing of authentic poliovirus data to 3.0 A resolution. J Mol Biol 307: 499–512. 11254378

14. Lentz KN, Smith AD, Geisler SC, Cox S, Buontempo P, et al. (1997) Structure of poliovirus type 2 Lansing complexed with antiviral agent SCH48973: comparison of the structural and biological properties of three poliovirus serotypes. Structure 5: 961–978. 9261087

15. Muckelbauer JK, Kremer M, Minor I, Tong L, Zlotnick A, et al. (1995) Structure determination of coxsackievirus B3 to 3.5 A resolution. Acta Crystallogr D Biol Crystallogr 51: 871–887. 15299757

16. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt A 276: 307–326.

17. French G.S. and Wilson K.S. (1978) On the treatment of negative intensity observations. Acta Cryst A34: 517–525.

18. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallographica Section D-Biological Crystallography 54: 905–921.

19. Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallographica Section D-Biological Crystallography 66: 213–221.

20. Emsley P, Lohkamp B, Scott WG, Cowtan K (2010) Features and development of Coot. Acta Crystallographica Section D-Biological Crystallography 66: 486–501.

21. Schüttelkopf AW, van Aalten DMF (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr 1355–1363.

22. Kleywegt GJ (1995) Dictionaries for Heteros. CCP4/ESF-EACBM Newsletter on Protein Crystallography 45–50.

23. Chen VB, Arendall WB, Headd JJ, Keedy DA, Immormino RM, et al. (2010) MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallographica Section D-Biological Crystallography 66: 12–21.

24. Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256–2268. 15572779

25. Pei J, Grishin NV (2007) PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23: 802–808. 17267437

26. Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, et al. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 33: W299–302. 15980475

27. Banks JLea (2005) Integrated modeling program, applied chemical theory (IMPACT). J Comput Chem: 1752–1780. 16211539

28. Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, et al. (2004) Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47: 1739–1749. 15027865

29. Halgren TA, Murphy RB, Friesner RA, Beard HS, Frye LL, et al. (2004) Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J Med Chem 47: 1750–1759. 15027866

30. Dubey KD, Chaubey AK, Ojha RP (2012) Role of polarization in ligand docking and binding affinity prediction for inhibitors of dengue virus. Medicinal Chemistry Research 21: 1030–1038.

31. Humphrey W, Dalke A, Schulten K (1996) VMD: Visual molecular dynamics. Journal of Molecular Graphics & Modelling 14: 33–38.

Štítky
Hygiena a epidemiológia Infekčné lekárstvo Laboratórium

Článok vyšiel v časopise

PLOS Pathogens


2015 Číslo 10
Najčítanejšie tento týždeň
Najčítanejšie v tomto čísle
Kurzy

Zvýšte si kvalifikáciu online z pohodlia domova

Aktuální možnosti diagnostiky a léčby litiáz
nový kurz
Autori: MUDr. Tomáš Ürge, PhD.

Všetky kurzy
Prihlásenie
Zabudnuté heslo

Zadajte e-mailovú adresu, s ktorou ste vytvárali účet. Budú Vám na ňu zasielané informácie k nastaveniu nového hesla.

Prihlásenie

Nemáte účet?  Registrujte sa

#ADS_BOTTOM_SCRIPTS#