Characterization of Putative Cholesterol Recognition/Interaction Amino Acid Consensus-Like Motif of Campylobacter jejuni Cytolethal Distending Toxin C

PLoS ONE

Volumn 8, Issue 6, 2013, Pages

  Lai, Chih Ho ^a   Lai, Cheng Kuo ^a,b   Lin, Ying Ju ^c   Hung, Chiu Lien ^d   Chu, Chia Han ^e   Feng, Chun Lung ^f   Chang, Chia Shuo ^a   Su, Hong Lin ^b,c  

^a CHINA MEDICAL UNIVERSITY   (Taiwan)

^b NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^c CHINA MEDICAL UNIVERSITY   (Taiwan)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^f CHINA MEDICAL UNIVERSITY HOSPITAL   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; CYTOLETHAL DISTENDING TOXIN; CYTOLETHAL DISTENDING TOXIN B; CYTOLETHAL DISTENDING TOXIN C; UNCLASSIFIED DRUG; BACTERIAL TOXIN; PROTEIN BINDING; PROTEIN SUBUNIT; TYROSINE;

ANIMAL CELL; ARTICLE; CAMPYLOBACTER JEJUNI; CHOLESTEROL RECOGNITION INTERACTION AMINO ACID CONSENSUS DOMAIN; CONTROLLED STUDY; HUMAN; LIPID RAFT; MEMBRANE BINDING; MOLECULAR MODEL; MUTATIONAL ANALYSIS; NONHUMAN; PROTEIN DOMAIN; PROTEIN MOTIF; ANIMAL; BINDING SITE; CELL MEMBRANE; CHEMICAL PHENOMENA; CHEMISTRY; CHO CELL LINE; CRICETULUS; GENETICS; METABOLISM; MOLECULAR DOCKING; MOLECULAR GENETICS; MUTATION; PATHOGENICITY; PROTEIN SUBUNIT;

BACTERIA (MICROORGANISMS); CAMPYLOBACTER JEJUNI;

AMINO ACID MOTIFS; ANIMALS; BACTERIAL TOXINS; BINDING SITES; CAMPYLOBACTER JEJUNI; CHO CELLS; CHOLESTEROL; CRICETULUS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MEMBRANE MICRODOMAINS; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN SUBUNITS; TYROSINE;

EID: 84878782140     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066202     Document Type: Article

References (36)

1. Tauxe RV, (1997) Emerging foodborne diseases: an evolving public health challenge. Emerg Infect Dis 3: 425-434.
2. Black RE, Levine MM, Clements ML, Hughes TP, Blaser MJ, (1988) Experimental Campylobacter jejuni infection in humans. J Infect Dis 157: 472-479.
3. Wooldridge KG, Williams PH, Ketley JM, (1996) Host signal transduction and endocytosis of Campylobacter jejuni. Microb Pathog 21: 299-305.
4. Lara-Tejero M, Galan JE, (2000) A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein. Science 290: 354-357.
5. Lara-Tejero M, Galan JE, (2001) CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity. Infect Immun 69: 4358-4365.
6. Smith JL, Bayles DO, (2006) The contribution of cytolethal distending toxin to bacterial pathogenesis. Crit Rev Microbiol 32: 227-248.
7. Lee RB, Hassane DC, Cottle DL, Pickett CL, (2003) Interactions of Campylobacter jejuni cytolethal distending toxin subunits CdtA and CdtC with HeLa cells. Infect Immun 71: 4883-4890.
8. Nesic D, Stebbins CE, (2005) Mechanisms of assembly and cellular interactions for the bacterial genotoxin CDT. PLoS Pathog 1: e28.
9. McSweeney LA, Dreyfus LA, (2004) Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit. Cell Microbiol 6: 447-458.
10. Nesic D, Hsu Y, Stebbins CE, (2004) Assembly and function of a bacterial genotoxin. Nature 429: 429-433.
11. Jinadasa RN, Bloom SE, Weiss RS, Duhamel GE, (2011) Cytolethal distending toxin: a conserved bacterial genotoxin that blocks cell cycle progression, leading to apoptosis of a broad range of mammalian cell lineages. Microbiology 157: 1851-1875.
12. Mao X, DiRienzo JM, (2002) Functional studies of the recombinant subunits of a cytolethal distending holotoxin. Cell Microbiol 4: 245-255.
13. McSweeney LA, Dreyfus LA, (2005) Carbohydrate-binding specificity of the Escherichia coli cytolethal distending toxin CdtA-II and CdtC-II subunits. Infect Immun 73: 2051-2060.
14. Eshraghi A, Maldonado-Arocho FJ, Gargi A, Cardwell MM, Prouty MG, et al. (2010) Cytolethal distending toxin family members are differentially affected by alterations in host glycans and membrane cholesterol. J Biol Chem 285: 18199-18207.
15. Boesze-Battaglia K, Besack D, McKay T, Zekavat A, Otis L, et al. (2006) Cholesterol-rich membrane microdomains mediate cell cycle arrest induced by Actinobacillus actinomycetemcomitans cytolethal-distending toxin. Cell Microbiol 8: 823-836.
16. Lin CD, Lai CK, Lin YH, Hsieh JT, Sing YT, et al. (2011) Cholesterol depletion reduces entry of Campylobacter jejuni cytolethal distending toxin and attenuates intoxication of host cells. Infect Immun 79: 3563-3575.
17. Damek-Poprawa M, Jang JY, Volgina A, Korostoff J, DiRienzo JM, (2012) Localization of Aggregatibacter actinomycetemcomitans cytolethal distending toxin subunits during intoxication of live cells. Infect Immun 80: 2761-2770.
18. Lin CJ, Rao YK, Hung CL, Feng CL, Lane HY, et al. (2013) Inhibition of Helicobacter pylori CagA-Induced Pathogenesis by Methylantcinate B from Antrodia camphorata. Evid Based Complement Alternat Med 2013: 682418.
19. Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
20. Yang JM, Chen CC, (2004) GEMDOCK: a generic evolutionary method for molecular docking. Proteins 55: 288-304.
21. Wu G, Robertson DH, Brooks CL, 3rd, Vieth M (2003) Detailed analysis of grid-based molecular docking: A case study of CDOCKER-A CHARMm-based MD docking algorithm. J Comput Chem 24: 1549-1562.
22. Li H, Papadopoulos V, (1998) Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 139: 4991-4997.
23. Simons K, Ikonen E, (1997) Functional rafts in cell membranes. Nature 387: 569-572.
24. Wolf AA, Fujinaga Y, Lencer WI, (2002) Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol. J Biol Chem 277: 16249-16256.
25. Abrami L, Liu S, Cosson P, Leppla SH, van der Goot FG, (2003) Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol 160: 321-328.
26. Abrami L, Fivaz M, Glauser PE, Parton RG, van der Goot FG, (1998) A pore-forming toxin interacts with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. J Cell Biol 140: 525-540.
27. Coconnier MH, Lorrot M, Barbat A, Laboisse C, Servin AL, (2000) Listeriolysin O-induced stimulation of mucin exocytosis in polarized intestinal mucin-secreting cells: evidence for toxin recognition of membrane-associated lipids and subsequent toxin internalization through caveolae. Cell Microbiol 2: 487-504.
28. Zitzer A, Bittman R, Verbicky CA, Erukulla RK, Bhakdi S, et al. (2001) Coupling of cholesterol and cone-shaped lipids in bilayers augments membrane permeabilization by the cholesterol-specific toxins streptolysin O and Vibrio cholerae cytolysin. J Biol Chem 276: 14628-14633.
29. Ricci V, Galmiche A, Doye A, Necchi V, Solcia E, et al. (2000) High cell sensitivity to Helicobacter pylori VacA toxin depends on a GPI-anchored protein and is not blocked by inhibition of the clathrin-mediated pathway of endocytosis. Mol Biol Cell 11: 3897-3909.
30. Guerra L, Teter K, Lilley BN, Stenerlow B, Holmes RK, et al. (2005) Cellular internalization of cytolethal distending toxin: a new end to a known pathway. Cell Microbiol 7: 921-934.
31. Lai CH, Hsu YM, Wang HJ, Wang WC, (2013) Manipulation of host cholesterol by Helicobacter pylori for their beneficial ecological niche. BioMedicine 3: 27-33.
32. Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK, (2010) Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci U S A 107: 4341-4346.
33. Boesze-Battaglia K, Brown A, Walker L, Besack D, Zekavat A, et al. (2009) Cytolethal distending toxin-induced cell cycle arrest of lymphocytes is dependent upon recognition and binding to cholesterol. J Biol Chem 284: 10650-10658.
34. Zhou M, Zhang Q, Zhao J, Jin M, (2012) Haemophilus parasuis encodes two functional cytolethal distending toxins: CdtC contains an atypical cholesterol recognition/interaction region. PLoS One 7: e32580.
35. Mise K, Akifusa S, Watarai S, Ansai T, Nishihara T, et al. (2005) Involvement of ganglioside GM3 in G(2)/M cell cycle arrest of human monocytic cells induced by Actinobacillus actinomycetemcomitans cytolethal distending toxin. Infect Immun 73: 4846-4852.
36. Yamada T, Komoto J, Saiki K, Konishi K, Takusagawa F, (2006) Variation of loop sequence alters stability of cytolethal distending toxin (CDT): crystal structure of CDT from Actinobacillus actinomycetemcomitans. Protein Sci 15: 362-372.