Comparative analyses of the β -tubulin gene and molecular modeling reveal molecular insight into the colchicine resistance in kinetoplastids organisms

BioMed Research International

Volumn 2013, Issue , 2013, Pages

  Luis, Luis ^a   Serrano, María Luisa ^b   Hidalgo, Mariana ^c   Mendoza León, Alexis ^a  

^a FACULTAD DE CIENCIAS   (Venezuela)

^b UNIVERSIDAD CENTRAL DE VENEZUELA   (Venezuela)

^c INSTITUTO VENEZOLANO DE INVESTIGACIONES CIENTÍFICAS   (Venezuela)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA TUBULIN; COLCHICINE; PROTOZOAL PROTEIN; TUBULIN; PROTEIN BINDING;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; GENE MUTATION; GENE SEQUENCE; LEISHMANIA; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI; TRYPANOSOMA EVANSI; AMINO ACID SEQUENCE; ANIMAL; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECT; DRUG RESISTANCE; GENETICS; KINETOPLASTIDA; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; BOVINE; DRUG EFFECTS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CATTLE; COLCHICINE; DRUG RESISTANCE; KINETOPLASTIDA; LEISHMANIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; TUBULIN;

EID: 84884849436     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/843748     Document Type: Article

References (41)

1. WHO, Control of the leishmaniasis. WHO Technical Report Series 2010 Geneva, Switzerland WHO
2. Mendoza-León A., Shaw J. J., Tapia F. J., Tapia F. J., Cáceres-Dittmar G., Sánchez M. A., A guide for the cutaneous leishmaniasis connoisseur. Molecular and Immune Mechanisms in the Pathogenesis of Cutaneous Leishmaniasis 1996 Austin, Tex, USA R.G. Landes Company Biomedical Publishers 1 23
3. Croft S. L., Sundar S., Fairlamb A. H., Drug resistance in leishmaniasis. Clinical Microbiology Reviews 2006 19 1 111 126 2-s2.0-31544439919 10.1128/CMR.19.1.111-126.2006 (Pubitemid 43157649)
4. Sundar S., Rosenkaimer F., Makharia M. K., Goyal A. K., Mandal A. K., Voss A., Hilgard P., Murray H. W., Trial of oral miltefosine for visceral leishmaniasis. The Lancet 1998 352 9143 1821 1823 2-s2.0-0032488285 (Pubitemid 28550072)
5. Serrano-Martín X., Payares G., De Lucca M., Martinez J. C., Mendoza-León A., Benaim G., Amiodarone and miltefosine act synergistically against Leishmania mexicana and can induce parasitological cure in a murine model of cutaneous leishmaniasis. Antimicrobial Agents and Chemotherapy 2009 53 12 5108 5113 2-s2.0-71249161926 10.1128/AAC.00505-09
6. Kavallaris M., Microtubules and resistance to tubulin-binding agents. Nature Reviews Cancer 2010 10 3 194 204 2-s2.0-77649191871 10.1038/nrc2803
7. Fennell B. J., Naughton J. A., Barlow J., Brennan G., Fairweather I., Hoey E., McFerran N., Trudgett A., Bell A., Microtubules as antiparasitic drug targets. Expert Opinion on Drug Discovery 2008 3 5 501 518 2-s2.0-44649163877 10.1517/17460441.3.5.501 (Pubitemid 351771991)
8. Jackson A. P., Vaughan S., Gull K., Comparative genomics and concerted evolution of β -tubulin paralogs in Leishmania spp. BMC Genomics 2006 7 137 2-s2.0-33747003223 10.1186/1471-2164-7-137 (Pubitemid 44202786)
9. Luis L., Ramírez A., Aguilar C. M., Eresh S., Barker D. C., Mendoza-León A., The genomic fingerprinting of the coding region of the β -tubulin gene in Leishmania identification. Acta Tropica 1998 69 3 193 204 2-s2.0-0344541957 10.1016/S0001-706X(97)00128-9 (Pubitemid 28243242)
10. Mendoza-León A., Barker D. C., Tapia F. J., Cáceres-Dittmar G., Sánchez M. A., Variation of a multigene family in New World Leishmania: the β -tubulin gene region. Molecular and Immune Mechanisms in the Pathogenesis of Cutaneous Leishmaniasis 1996 Austin, Tex, USA R.G. Landes Company Biomedical Publishers 107 128
11. Mendoza-León A., Luis L., Martinez C., Aquino de Muro M., Rapley R., The β -tubulin gene region as a molecular marker to distinguish Leishmania parasites. Methods in Molecular Biology. Gene Probes Principles and Protocols 2002 179 Totowa, NJ, USA Humana Press 61 83
12. Délye C., Menchari Y., Michel S., Darmency H., Molecular bases for sensitivity to tubulin-binding herbicides in green foxtail. Plant Physiology 2004 136 4 3920 3932 2-s2.0-16644399138 10.1104/pp.103.037432 (Pubitemid 41096271)
13. Werbovetz K. A., Sackett D. L., Delfín D., Bhattacharya G., Salem M., Obrzut T., Rattendi D., Bacchi C., Selective antimicrotubule activity of N1-phenyl-3,5-dinitro-N4,N4-di-n-propylsulfanilamide (GB-II-5) against kinetoplastid parasites. Molecular Pharmacology 2003 64 6 1325 1333 2-s2.0-0346996811 10.1124/mol.64.6.1325 (Pubitemid 37532222)
14. Werbovetz K. A., Brendle J. J., Sackett D. L., Purification, characterization, and drug susceptibility of tubulin from Leishmania. Molecular and Biochemical Parasitology 1999 98 1 53 65 2-s2.0-0032929522 10.1016/S0166-6851(98)00146-7 (Pubitemid 29027929)
15. Werbovetz K. A., Morgan R. E., Selective lead compounds against kinetoplastid tubulin. Advances in Experimental Medicine and Biology 2008 625 33 47 2-s2.0-42949157714 10.1007/978-0-387-77570-8-4
16. Macrae T. H., Gull K., Purification and assembly in vitro of tubulin from Trypanosoma brucei brucei. Biochemical Journal 1990 265 1 87 93 2-s2.0-0025128705 (Pubitemid 20037677)
17. Yakovich A. J., Ragone F. L., Alfonzo J. D., Sackett D. L., Werbovetz K. A., Leishmania tarentolae: purification and characterization of tubulin and its suitability for antileishmanial drug screening. Experimental Parasitology 2006 114 4 289 296 2-s2.0-33750333141 10.1016/j.exppara.2006.04.008 (Pubitemid 44634436)
18. Gull K., The cytoskeleton of trypanosomatid parasites. Annual Review of Microbiology 1999 53 629 655 2-s2.0-0032724638 10.1146/annurev.micro.53.1.629 (Pubitemid 29503743)
19. Bai R., Covell D. G., Pei X., Ewell J. B., Nguyen N. Y., Brossi A., Hamel E., Mapping the binding site of colchicinoids on β -tubulin: 2-chloroacetyl-2-demethylthiocolchicine covalently reacts predominantly with cysteine 239 and secondarily with cysteine 354. Journal of Biological Chemistry 2000 275 51 40443 40452 2-s2.0-0034704077 10.1074/jbc.M005299200 (Pubitemid 32064679)
20. Uppuluri S., Knipling L., Sackett D. L., Wolff J., Localization of the colchicine-binding site of tubulin. Proceedings of the National Academy of Sciences of the United States of America 1993 90 24 11598 11602 2-s2.0-0027140153 10.1073/pnas.90.24.11598 (Pubitemid 24008686)
21. Downing K. H., Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annual Review of Cell and Developmental Biology 2000 16 89 111 2-s2.0-0034518173 10.1146/annurev.cellbio. 16.1.89 (Pubitemid 32037501)
22. Nogales E., Wolf S. G., Downing K. H., Structure of the α β tubulin dimer by electron crystallography. Nature 1998 391 6663 199 203 2-s2.0-0032495513 10.1038/34465 (Pubitemid 28092482)
23. Ravelli R. B. G., Gigant B., Curmi P. A., Jourdain I., Lachkar S., Sobel A., Knossow M., Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 2004 428 6979 198 202 2-s2.0-1642401199 10.1038/nature02393 (Pubitemid 38374318)
24. Mendoza-Leon A., Havercroft J. C., Barker D. C., The RFLP analysis of the β -tubulin gene region in New World Leishmania. Parasitology 1995 111 1 1 9 2-s2.0-0028979853
25. Ng P. C., Henikoff S., SIFT: predicting amino acid changes that affect protein function. Nucleic Acids Research 2003 31 13 3812 3814 2-s2.0-0043122919 10.1093/nar/gkg509 (Pubitemid 37442253)
26. Ng P. C., Henikoff S., Predicting the effects of amino acid substitutions on protein function. Annual Review of Genomics and Human Genetics 2006 7 61 80 2-s2.0-33750353461 10.1146/annurev.genom.7.080505.115630 (Pubitemid 44627922)
27. Xi T., Jones I. M., Mohrenweiser H. W., Many amino acid substitution variants identified in DNA repair genes during human population screenings are predicted to impact protein function. Genomics 2004 83 6 970 979 2-s2.0-2642527702 10.1016/j.ygeno.2003.12.016 (Pubitemid 38726046)
28. Gigant B., Wang C., Ravelli R. B. G., Roussi F., Steinmetz M. O., Curmi P. A., Sobel A., Knossow M., Structural basis for the regulation of tubulin by vinblastine. Nature 2005 435 7041 519 522 2-s2.0-19544393159 10.1038/nature03566 (Pubitemid 40734250)
29. Schwede T., Kopp J., Guex N., Peitsch M. C., SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Research 2003 31 13 3381 3385 2-s2.0-0042622380 10.1093/nar/gkg520 (Pubitemid 37442164)
30. Guex N., Peitsch M. C., SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997 18 15 2714 2723 2-s2.0-0031473847 10.1002/elps.1150181505 (Pubitemid 28059943)
31. Phillips J. C., Braun R., Wang W., Gumbart J., Tajkhorshid E., Villa E., Chipot C., Skeel R. D., Kalé L., Schulten K., Scalable molecular dynamics with NAMD. Journal of Computational Chemistry 2005 26 16 1781 1802 2-s2.0-27344436659 10.1002/jcc.20289 (Pubitemid 43078511)
32. Pedretti A., Villa L., Vistoli G., VEGA-an open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming. Journal of Computer-Aided Molecular Design 2004 18 3 167 173 2-s2.0-4043162793 10.1023/B:JCAM.0000035186.90683.f2 (Pubitemid 39069412)
33. Wiederstein M., Sippl M. J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic acids research 2007 35 W407 W410 2-s2.0-34547566446 10.1093/nar/gkm290
34. Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M., PROCHECK-a program to check the stereochemical quality of protein structures. Journal of Applied Crystallography 1993 26 283 291 10.1107/S0021889892009944
35. Li S.-Q., Fung M.-C., Reid S. A., Inoue N., Lun Z.-R., Immunization with recombinant β -tubulin from Trypanosoma evansi induced protection against T. evansi, T. equiperdum and T. b. brucei infection in mice. Parasite Immunology 2007 29 4 191 199 2-s2.0-33947212508 10.1111/j.1365-3024.2006.00933.x (Pubitemid 46434885)
36. Massarotti A., Coluccia A., Silvestri R., Sorba G., Brancale A., The tubulin colchicine domain: a molecular modeling perspective. ChemMedChem 2012 7 1 33 42 2-s2.0-84555195099 10.1002/cmdc.201100361
37. Henriquez F. L., Ingram P. R., Muench S. P., Rice D. W., Roberts C. W., Molecular basis for resistance of Acanthamoeba tubulins to all major classes of antitubulin compounds. Antimicrobial Agents and Chemotherapy 2008 52 3 1133 1135 2-s2.0-40549095339 10.1128/AAC.00355-07 (Pubitemid 351358398)
38. Lu Y., Chen J., Xiao M., Li W., Miller D. D., An overview of tubulin inhibitors that interact with the colchicine binding site. Pharmaceutical Research 2012 29 11 2943 2971 10.1007/s11095-012-0828-z
39. Chen K., Huzil J. T., Freedman H., Ramachandran P., Antoniou A., Tuszynski J. A., Kurgan L., Identification of tubulin drug binding sites and prediction of relative differences in binding affinities to tubulin isotypes using digital signal processing. Journal of Molecular Graphics and Modelling 2008 27 4 497 505 2-s2.0-55949099299 10.1016/j.jmgm.2008.09.001
40. Cheung C. H. A., Wu S.-Y., Lee T.-R., Chang C.-Y., Wu J.-S., Hsieh H., Chang J., Cancer cells acquire mitotic drug resistance properties through β I-tubulin mutations and alterations in the expression of β -tubulin isotypes. PloS one 2010 5 9 e12564 2-s2.0-79952276720
41. Stengel C., Newman S. P., Leese M. P., Potter B. V. L., Reed M. J., Purohit A., Class III Β -tubulin expression and in vitro resistance to microtubule targeting agents. British Journal of Cancer 2010 102 2 316 324 2-s2.0-75549087583 10.1038/sj.bjc.6605489