Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni

Journal of Structural Biology

Volumn 177, Issue 2, 2012, Pages 583-588

  Kawai, Fumihiro ^a   Paek, Seonghee ^a   Choi, Kyoung Jae ^a   Prouty, Michael ^b   Kanipes, Margaret I ^c   Guerry, Patricia ^b   Yeo, Hye Jeong ^a  

^a University of Houston   (United States)

^b NAVAL MEDICAL RESEARCH CENTER   (United States)

^c NORTH CAROLINA A AND T STATE UNIVERSITY   (United States)

Author keywords

Bacterial lipoprotein; Campylobacter jejuni; Crystal structure; JlpA

Indexed keywords

ADHESIN; BACTERIAL PROTEIN; JLPA PROTEIN; LIPOPROTEIN; LOLB PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; CAMPYLOBACTER JEJUNI; CELL SURFACE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN TARGETING; SURFACE PROPERTY;

ADHESINS, BACTERIAL; AMINO ACID SEQUENCE; CAMPYLOBACTER JEJUNI; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; LIPOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; SURFACE PROPERTIES;

BACTERIA (MICROORGANISMS); CAMPYLOBACTER JEJUNI;

EID: 84857029797     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.01.001     Document Type: Article

References (30)

1. Aliprantis A.O., Yang R.B., Mark M.R., Suggett S., Devaux B., et al. Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2. Science 1999, 285:736-739.
2. Ashgar S.S., Oldfield N.J., Wooldridge K.G., Jones M.A., Irving G.J., et al. CapA, an autotransporter protein of Campylobacter jejuni, mediates association with human epithelial cells and colonization of the chicken gut. J. Bacteriol. 2007, 189:1856-1865.
3. Bacon D.J., Szymanski C.M., Burr D.H., Silver R.P., Alm R.A., et al. A phase-variable capsule is involved in virulence of Campylobacter jejuni 81-176. Mol. Microbiol. 2001, 40:769-777.
4. Brunger A.T. Version 1.2 of the crystallography and NMR system. Nat. Protoc. 2007, 2:2728-2733.
5. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50:760-763. CCP4.
6. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:2126-2132.
7. Flanagan R.C., Neal-McKinney J.M., Dhillon A.S., Miller W.G., Konkel M.E. Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization. Infect. Immun. 2009, 77:2399-2407.
8. Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., et al. Major structural differences and novel potential virulence mechanisms from the genomes of multiple campylobacter species. PLoS Biol. 2005, 3:e15.
9. Hendrickson W.A., Smith J.L., Sheriff S. Direct phase determination based on anomalous scattering. Methods Enzymol. 1985, 115:41-55.
10. Jin S., Joe A., Lynett J., Hani E.K., Sherman P., et al. JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells. Mol. Microbiol. 2001, 39:1225-1236.
11. Jin S., Song Y.C., Emili A., Sherman P.M., Chan V.L. JlpA of Campylobacter jejuni interacts with surface-exposed heat shock protein 90alpha and triggers signalling pathways leading to the activation of NF-kappaB and p38 MAP kinase in epithelial cells. Cell Microbiol. 2003, 5:165-174.
12. Kowarik M., Young N.M., Numao S., Schulz B.L., Hug I., et al. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J. 2006, 25:1957-1966.
13. Minor W., Cymborowski M., Otwinowski Z., Chruszcz M. HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:859-866.
14. Monteville M.R., Yoon J.E., Konkel M.E. Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization. Microbiology 2003, 149:153-165.
15. Moser I., Schroeder W., Salnikow J. Campylobacter jejuni major outer membrane protein and a 59-kDa protein are involved in binding to fibronectin and INT 407 cell membranes. FEMS Microbiol. Lett. 1997, 157:233-238.
16. Murshudov G.N., Vagin A.A., Lebedev A., Wilson K.S., Dodson E.J. Efficient anisotropic refinement of macromolecular structures using FFT. Acta Crystallogr. D Biol. Crystallogr. 1999, 55:247-255.
17. Nachamkin I., Liu J., Li M., Ung H., Moran A.P., et al. Campylobacter jejuni from patients with Guillain-Barré syndrome preferentially expresses a GD(1a)-like epitope. Infect. Immun. 2002, 70:5299-5303.
18. Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991, 11:281-296.
19. Pei Z., Burucoa C., Grignon B., Baqar S., Huang X.Z., et al. Mutation in the peb1A locus of Campylobacter jejuni reduces interactions with epithelial cells and intestinal colonization of mice. Infect. Immun. 1998, 66:938-943.
20. Poly F., Guerry P. Pathogenesis of Campylobacter. Curr. Opin. Gastroenterol. 2008, 24:27-31.
21. Scott N.E., Bogema D.R., Connolly A.M., Falconer L., Djordjevic S.P., et al. Mass spectrometric characterization of the surface-associated 42kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J. Proteome Res. 2009, 8:4654-4664.
22. Sulzenbacher G., Canaan S., Bordat Y., Neyrolles O., Stadthagen G., et al. LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis. EMBO J. 2006, 25:1436-1444.
23. Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., et al. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J. 2003, 22:3199-3209.
24. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D Biol. Crystallogr. 2000, 56:965-972.
25. Terwilliger T.C., Grosse-Kunstleve R.W., Afonine P.V., Moriarty N.W., Zwart P.H., et al. Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard. Acta Crystallogr. D Biol. Crystallogr. 2008, 64:61-69.
26. Tokuda H., Matsuyama S. Sorting of lipoproteins to the outer membrane in E. coli. Biochim. Biophys. Acta 2004, 1693:5-13.
27. Vandeputte-Rutten L., Bos M.P., Tommassen J., Gros P. Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential. J. Biol. Chem. 2003, 278:24825-24830.
28. Vonrhein C., Blanc E., Roversi P., Bricogne G. Automated structure solution with autoSHARP. Methods Mol. Biol. 2006, 364:215-230.
29. Winn M.D., Murshudov G.N., Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 2003, 374:300-321.
30. Zilbauer M., Dorrell N., Wren B.W., Bajaj-Elliott M. Campylobacter jejuni-mediated disease pathogenesis: an update. Trans R. Soc. Trop. Med. Hyg. 2008, 102:123-129.