Identification of Potential Leptospira Phosphoheptose Isomerase Inhibitors Through Virtual High-Throughput Screening

Genomics, Proteomics and Bioinformatics

Volumn 8, Issue 4, 2010, Pages 246-255

  Umamaheswari, Amineni ^a   Pradhan, Dibyabhaba ^a   Hemanthkumar, Marisetty ^b  

^a SRI VENKATESWARA INSTITUTE OF MEDICAL SCIENCES   (India)

^b AGRICULTURAL RESEARCH STATION   (India)

Author keywords

GmhA inhibitors; Homology modeling; Leptospira; LPS biosynthesis; Virtual high throughput screening

Indexed keywords

ANTIBIOTIC AGENT; ISOMERASE INHIBITOR; PHOSPHOHEPTOSE ISOMERASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; DRUG CONFORMATION; DRUG PROTEIN BINDING; DRUG SCREENING; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SUBSTRATE; HIGH THROUGHPUT SCREENING; LEPTOSPIRA; MOLECULAR DOCKING; MOLECULAR LIBRARY; MOLECULAR MODEL; NONHUMAN; PROTEIN DATABASE; PROTEIN TARGETING; SCORING SYSTEM; SEQUENCE HOMOLOGY; VIRTUAL HIGH THROUGHPUT SCREENING;

ALDOSE-KETOSE ISOMERASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DRUG DESIGN; ENZYME INHIBITORS; HIGH-THROUGHPUT SCREENING ASSAYS; LEPTOSPIRA; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE HOMOLOGY, AMINO ACID;

LEPTOSPIRA;

EID: 79952284989     PISSN: 16720229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1672-0229(10)60026-5     Document Type: Article

References (48)

1. Bharti A.R., et al. Leptospirosis: a zoonotic disease of global importance. Lancet Infect. Dis 2003, 3:757-771.
2. Bourhy P., et al. A genomic island of the pathogen Leptospira interrogans serovar Lai can excise from its chromosome. Infect. Immun 2007, 75:677-683.
3. Trueba G., et al. Cell aggregation: a mechanism of pathogenic Leptospira to survive in fresh water. Int. Microbiol 2004, 7:35-40.
4. Levett P.N. Leptospirosis. Clin. Microbiol. Rev 2001, 14:296-326.
5. Kuriakose M., et al. Leptospirosis in Kolenchery, Kerala, India: epidemiology, prevalent local serogroups and serovars and a new serovar. Eur. J. Epidemiol 1997, 13:691-697.
6. Waitkins S.A. Leptospirosis as an occupational disease. Br. J. Ind. Med 1986, 43:721-725.
7. Wang Z., et al. Leptospirosis vaccines. Microb. Cell Fact. 2007, 6:39.
8. Farr R.W. Leptospirosis. Clin. Infect. Dis 1995, 21:1-6.
9. Ren S.X., et al. Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. Nature 2003, 422:888-893.
10. Nascimento A.L., et al. Genome features of Leptospira interrogans serovar Copenhageni. Braz. J. Med. Biol. Res 2004, 37:459-477.
11. Bulach D.M., et al. Genome reduction in Leptospira borgpetersenii reflects limited transmission potential. Proc. Natl. Acad. Sci. USA 2006, 103:14560-14565.
12. Rakesh S., et al. In silico approach for future development of subunit vaccines against Leptospira interrogans serovar Lai. Int. J. Bioinformatics Res 2009, 1:85-92.
13. Umamaheswari A., et al. In silico identification of common putative drug targets in Leptospira interrogans. J. Chem. Biol 2010, 3:175-187.
14. Umamaheswari A., et al. In silico putative drug targets in Leptospira interrogans and homology modeling of UDP-N-acetylglucosamine 1-carboxyvinyltransferase MurA. Genomic Med. 2008, 2:295.
15. Raetz C.R., Whitfield C. Lipopolysaccharide endotoxins. Annu. Rev. Biochem 2002, 71:635-700.
16. Taylor P.L., et al. Structure and function of sedo-heptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants. J. Biol. Chem 2008, 283:2835-2845.
17. Adler B., Faine S. The genus Leptospira. The Prokaryotes 2006, 297. Springer, New York, USA. M. Dworkin (Ed.).
18. Farrelly H.E., et al. Opsonic monoclonal antibodies against lipopolysaccharide antigens of Leptospira interrogans serovar hardjo. J. Med. Microbiol 1987, 23:1-7.
19. Jost B.H., et al. A monoclonal antibody reacting with a determinant on leptospiral lipopolysaccharide protects guinea pigs against leptospirosis. J. Med. Microbiol 1986, 22:269-275.
20. Midwinter A., et al. Vaccination of mice with lipopolysaccharide (LPS) and LPS-derived im-muno-conjugates from Leptospira interrogans. J. Med. Microbiol 1990, 33:199-204.
21. Vinh T.U., et al. Characterization and taxonomic significance of lipopolysaccharides of Leptospira interrogans serovar hardjo. J. Gen. Microbiol 1989, 135:2663-2673.
22. Yanagihara Y., et al. Identification of 4-O-methylmannose in cell wall polysaccharide of Leptospira. Microbiol. Immunol 1983, 27:711-715.
23. Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev 2003, 67:593-656.
24. Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev 1985, 49:1-32.
25. Yethon J.A., Whitfield C. Lipopolysaccharide as a target for the development of novel therapeutics in gram-negative bacteria. Curr. Drug Targets Infect. Disord 2001, 1:91-106.
26. Onishi H.R., et al. Antibacterial agents that inhibit lipid A biosynthesis. Science 1996, 274:980-982.
27. Valvano M.A., et al. Novel pathways for biosyn-thesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 2002, 148:1979-1989.
28. Kneidinger B., et al. Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli. J. Bacteriol 2002, 184:363-369.
29. Eidels L., Osborn M.J. Lipopolysaccharide and aldoheptose biosynthesis in transketolase mutants of Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 1971, 68:1673-1677.
30. Kneidinger B., et al. Biosynthesis of nucleo-tide-activated D-glycero-D-manno-heptose. J. Biol. Chem 2001, 276:20935-20944.
31. Anishetty S., et al. Potential drug targets in Myco-bacterium tuberculosis through metabolic pathway analysis. Comput. Biol. Chem 2005, 29:368-378.
32. Eswar N., et al. Protein structure modeling with MODELLER. Methods Mol. Biol 2008, 426:145-159.
33. Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol 1993, 234:779-815.
34. Paramasivan R., et al. Prediction of 3-dimensional structure of salivary odorant-binding protein-2 of the mosquito Culex quinquefasciatus, the vector of human lymphatic filariasis. In Silico Biol 2007, 7:1-6.
35. Wiederstein M., Sippl M.J. ProSA-web: inter-active web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 2007, 35:W407-W410.
36. Wallner B., Elofsson A. Can correct protein models be identified?. Protein Sci 2003, 12:1073-1086.
37. Kanehisa M., Goto S. KEGG: kyoto encyclo-pedia of genes and genomes. Nucleic Acids Res 2000, 28:27-30.
38. Bryson K., et al. Protein structure prediction servers at University College London. Nucleic Acids Res. 2005, 1:W36-W38.
39. Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402.
40. Berman H.M., et al. The Protein Data Bank. Nucleic Acids Res 2000, 28:235-242.
41. Thompson J.D., et al. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 24:4876-4882.
42. Laskowski R.A., et al. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst 1993, 26:283-291.
43. Holm L. Unification of protein families. Curr. Opin. Struct. Biol 1998, 8:372-379.
44. Castrignano T., et al. The PMDB Protein Model Database. Nucleic Acids Res. 2006, 34:D306-D309.
45. von Grotthuss M., et al. Ligand-Info, searching for similar small compounds using index profiles. Bioinformatics 2003, 19:1041-1042.
46. Umamaheswari A., et al. Virtual screening for potential inhibitors of homology modeled Leptospira inter-rogans MurD ligase. J. Chem. Biol 2010, 3:165-173.
47. Brooks W.H., et al. Computational validation of the importance of absolute stereochemistry in virtual screening. J. Chem. Inf. Model 2008, 48:639-645.
48. Friesner R.A., et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J. Med. Chem 2004, 47:1739-1749.