Expression and purification of functional human anthrax toxin receptor (ATR/TEM8) binding domain from Escherichia coli

Protein Expression and Purification

Volumn 49, Issue 1, 2006, Pages 121-128

  Ding, Zhiping ^a   Bradley, Kenneth A ^b   Amin Arnaout, M ^a   Xiong, Jian Ping ^a  

^a Renal Unit   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Anthrax; Anthrax toxin receptor; Expression; Purification; VWA domain

Indexed keywords

ANTHRAX TOXIN; ANTHRAX TOXIN RECEPTOR 1, HUMAN; BACTERIAL ANTIGEN; BACTERIAL TOXIN; CELL SURFACE RECEPTOR; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; TUMOR PROTEIN;

ANIMAL; ARTICLE; BACILLUS ANTHRACIS; BINDING SITE; BIOSYNTHESIS; CHO CELL; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; HAMSTER; HUMAN; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; SURFACE PLASMON RESONANCE;

ANIMALS; ANTIGENS, BACTERIAL; BACILLUS ANTHRACIS; BACTERIAL TOXINS; BINDING SITES; CHO CELLS; CRICETINAE; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; MASS SPECTROMETRY; MEMBRANE PROTEINS; NEOPLASM PROTEINS; RECEPTORS, CELL SURFACE; RECOMBINANT PROTEINS; SURFACE PLASMON RESONANCE;

BACILLUS ANTHRACIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA; POSIBACTERIA;

EID: 33748038360     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.04.011     Document Type: Article

References (44)

1. Lane H.C., Montagne J.L., and Fauci A.S. Bioterrorism: a clear and present danger. Nat. Med. 7 (2001) 1271-1273
2. Keim P., and Smith K.L. Bacillus anthracis evolution and epidemiology. Curr. Top. Microbiol. Immunol. 271 (2002) 21-32
3. Turnbull P.C. Introduction: anthrax history, disease and ecology. Curr. Top. Microbiol. Immunol. 271 (2002) 1-19
4. Mock M., and Fouet A. Anthrax. Annu. Rev. Microbiol. 55 (2001) 647-671
5. Little S.F., and Ivins B.E. Molecular pathogenesis of Bacillus anthracis infection. Microbes. Infect. 1 (1999) 131-139
6. Hanna P.C., and Ireland J.A. Understanding Bacillus anthracis pathogenesis. Trends Microbiol. 7 (1999) 180-182
7. Smith H. Discovery of the anthrax toxin: the beginning of in vivo studies on pathogenic bacteria. Trends Microbiol. 8 (2000) 199-200
8. Brossier F., Sirard J.C., Guidi-Rontani C., Duflot E., and Mock M. Functional analysis of the carboxy-terminal domain of Bacillus anthracis protective antigen. Infect. Immun. 67 (1999) 964-967
9. Lincoln R.E., Hodges D.R., Klein F., Mahlandt B.G., Jones Jr. W.I., Haines B.W., Rhian M.A., and Walker J.S. Role of the lymphatics in the pathogenesis of anthrax. J. Infect. Dis. 115 (1965) 481-494
10. Shafa F., Moberly B.J., and Gerhardt P. Cytological features of anthrax spores phagocytized in vitro by rabbit alveolar macrophages. J. Infect. Dis. 116 (1966) 401-413
11. Firoved A.M., Miller G.F., Moayeri M., Kakkar R., Shen Y., Wiggins J.F., McNally E.M., Tang W.J., and Leppla S.H. Bacillus anthracis edema toxin causes extensive tissue lesions and rapid lethality in mice. Am. J. Pathol. 167 (2005) 1309-1320
12. Leppla S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic amp concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. USA 79 (1982) 3162-3166
13. Duesbery N.S., Webb C.P., Leppla S.H., Gordon V.M., Klimpel K.R., Copeland T.D., Ahn N.G., Oskarsson M.K., Fukasawa K., Paull K.D., and Vande Woude G.F. Proteolytic inactivation of map-kinase-kinase by anthrax lethal factor. Science 280 (1998) 734-737
14. Vitale G., Pellizzari R., Recchi C., Napolitani G., Mock M., and Montecucco C. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248 (1998) 706-711
15. Bradley K.A., Mogridge J., Mourez M., Collier R.J., and Young J.A.T. Identification of the cellular receptor for anthrax toxin. Nature 414 (2001) 225-229
16. St Croix B., Rago C., Velculescu V., Traverso G., Romans K.E., Montgomery E., Lal A., Riggins G.J., Lengauer C., Vogelstein B., and Kinzler K.W. Genes expressed in human tumor endothelium. Science 289 (2000) 1197-1202
17. Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W., and St Croix B. Cell surface tumor endothelial markers are conserved in mice and humans. Cancer Res. 61 (2001) 6649-6655
18. Hotchkiss K.A., Basile C.M., Spring S.C., Bonuccelli G., Lisanti M.P., and Terman B.I. Tem8 expression stimulates endothelial cell adhesion and migration by regulating cell-matrix interactions on collagen. Exp. Cell Res. 305 (2005) 133-144
19. Bell S.E., Mavila A., Salazar R., Bayless K.J., Kanagala S., Maxwell S.A., and Davis G.E. Differential gene expression during capillary morphogenesis in 3D collagen matrices: regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and g-protein signaling. J. Cell Sci. 114 (2001) 2755-2773
20. Dowling O., Difeo A., Ramirez M.C., Tukel T., Narla G., Bonafe L., Kayserili H., Yuksel-Apak M., Paller A.S., Norton K., Teebi A.S., Grum-Tokars V., Martin G.S., Davis G.E., Glucksman M.J., and Martignetti J.A. Mutations in capillary morphogenesis gene-2 result in the allelic disorders juvenile hyaline fibromatosis and infantile systemic hyalinosis. Am. J. Hum. Genet. 73 (2003) 957-966
21. Hanks S., Adams S., Douglas J., Arbour L., Atherton D.J., Balci S., Bode H., Campbell M.E., Feingold M., Keser G., Kleijer W., Mancini G., McGrath J.A., Muntoni F., Nanda A., Teare M.D., Warman M., Pope F.M., Superti-Furga A., Futreal P.A., and Rahman N. Mutations in the gene encoding capillary morphogenesis protein 2 cause juvenile hyaline fibromatosis and infantile systemic hyalinosis. Am. J. Hum. Genet. 73 (2003) 791-800
22. Scobie H.M., Rainey G.J.A., Bradley K.A., and Young J.A.T. Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor. PNAS 100 (2003) 5170-5174
23. Liu S., and Leppla S.H. Cell surface tumor endothelium marker 8 cytoplasmic tail-independent anthrax toxin binding, proteolytic processing, oligomer formation, and internalization. J. Biol. Chem. 278 (2003) 5227-5234
24. Bradley K.A., Mogridge J., Jonah G., Rainey A., Batty S., and Young J.A. Binding of anthrax toxin to its receptor is similar to alpha integrin-ligand interactions. J. Biol. Chem. 278 (2003) 49342-49347
25. Lee J.O., Rieu P., Arnaout M.A., and Liddington R. Crystal structure of the a-domain from the alpha subunit of integrin cr3 (cd11b/cd18). Cell 80 (1995) 631-638
26. Xiong J.-P., Stehle T., Goodman S.L., and Arnaout M.A. Integrins, cations and ligands: making the connection. J. Thromb. Haemost. 1 (2003) 1642-1654
27. Lacy D.B., Wigelsworth D.J., Scobie H.M., Young J.A.T., and Collier R.J. Crystal structure of the von Willebrand factor a domain of human capillary morphogenesis protein. 2. An anthrax toxin receptor. PNAS 101 (2004) 6367-6372
28. Santelli E., Bankston L.A., Leppla S.H., and Liddington R.C. Crystal structure of a complex between anthrax toxin and its host cell receptor. Nature 430 (2004) 905-908
29. Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., and Collier R.J. Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Proc. Natl. Acad. Sci. USA 101 (2004) 13147-13151
30. Lee J.O., Bankston L.A., Arnaout M.A., and Liddington R.C. Two conformations of the integrin a-domain (i-domain): a pathway for activation?. Structure 3 (1995) 1333-1340
31. Xiong J.-P., Li R., Essafi M., Stehle T., and Arnaout M.A. An isoleucine-based allosteric switch controls affinity and shape shifting in integrin cd11b a-domain. J. Biol. Chem. 275 (2000) 38762-38767
32. Emsley J., Knight C.G., Farndale R.W., Barnes M.J., and Liddington R.C. Structural basis of collagen recognition by integrin alpha2beta1. Cell 101 (2000) 47-56
33. Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H., and Springer T.A. Structures of the alpha l i domain and its complex with icam-1 reveal a shape-shifting pathway for integrin regulation. Cell 112 (2003) 99-111
34. Scobie H.M., Thomas D., Marlett J.M., Destito G., Wigelsworth D.J., Collier R.J., Young J.A., and Manchester M. A soluble receptor decoy protects rats against anthrax lethal toxin challenge. J. Infect. Dis. 192 (2005) 1047-1051
35. Kruger N.J. The Bradford method for protein quantitation. Methods Mol. Biol. 32 (1994) 9-15
36. Wigelsworth D.J., Krantz B.A., Christensen K.A., Lacy D.B., Juris S.J., and Collier R.J. Binding stoichiometry and kinetics of the interaction of a human anthrax toxin receptor, cmg2, with protective antigen. J. Biol. Chem. 279 (2004) 23349-23356
37. Smith D.B., and Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67 (1988) 31-40
38. Park J.H., Choi E.A., Cho E.W., Hahm K.S., and Kim K.L. Maltose binding protein (MBP) fusion proteins with low or no affinity to amylose resins can be single-step purified using a novel anti-MBP monoclonal antibody. Mol. Cells 8 (1998) 709-716
39. Fox J.D., and Waugh D.S. Maltose-binding protein as a solubility enhancer. Methods Mol. Biol. 205 (2003) 99-117
40. Sorensen H.P., and Mortensen K.K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115 (2005) 113-128
41. Schein C.H. Optimizing protein folding to the native state in bacteria. Curr. Opin. Biotechnol. 2 (1991) 746-750
42. Vasina J.A., and Baneyx F. Expression of aggregation-prone recombinant proteins at low temperatures: a comparative study of the Escherichia coli cspa and tac promoter systems. Protein Expr. Purif. 9 (1997) 211-218
43. Leushner J. Maldi TOF mass spectrometry: an emerging platform for genomics and diagnostics. Expert Rev. Mol. Diagn. 1 (2001) 11-18
44. Malmqvist M. BIAcore: an affinity biosensor system for characterization of biomolecular interactions. Biochem. Soc. Trans. 27 (1999) 335-340