Alanine-scanning mutations in domain 4 of anthrax toxin protective antigen reveal residues important for binding to the cellular receptor and to a neutralizing monoclonal antibody

Journal of Biological Chemistry

Volumn 278, Issue 33, 2003, Pages 30936-30944

  Rosovitz, M J ^a   Schuck, Peter ^b   Varughese, Mini ^a   Chopra, Arun P ^c   Mehra, Varsha ^c   Singh, Yogendra ^c   McGinnis, Lisa M ^a   Leppla, Stephen H ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c CSIR INSTITUTE OF GENOMICS AND INTEGRATIVE BIOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL CULTURE; ANTIGENS; BIOASSAY; MONOCLONAL ANTIBODIES; MUTAGENESIS; TOXICITY;

MUTATION;

BIOCHEMICAL ENGINEERING;

ALANINE; ANTHRAX TOXIN; ANTIGEN; ASPARAGINE; CELL RECEPTOR; LEUCINE; LYSINE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PROLINE; TYROSINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL CULTURE; CONTROLLED STUDY; CYTOTOXICITY; GENE MUTATION; MEASUREMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; RECEPTOR BINDING; ULTRACENTRIFUGATION;

ALANINE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIGENS, BACTERIAL; ASPARTIC ACID; BACTERIAL TOXINS; BINDING SITES; CELL LINE; MACROPHAGES; MICE; MODELS, CHEMICAL; MUTATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, PEPTIDE;

ANIMALIA; ANTHRAX; PROKARYOTA;

EID: 0042232277     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M301154200     Document Type: Article

References (51)

1. Stanley, J. L., and Smith, H. (1961) J. Gen. Microbiol. 26, 49-66
2. Beall, F. A., Taylor, M. J., and Thorne, C. B. (1962) J. Bacteriol. 83, 1274-1280
3. Leppla, S. H. (2000) in Bacterial Protein Toxins (Aktories, K., and Just, I., eds) Springer, Berlin
4. Bradley, K. A., Mogridge, J., Mourez, M., Collier, R. J., and Young, J. A. (2001) Nature 414, 225-229
5. 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. (2000) Science 289, 1197-1202
6. Liu, S., and Leppla, S. H. (2002) J. Biol. Chem. 278, 5227-5234
7. Scobie, H. M., Rainey, G. J., Bradley, K. A., and Young, J. A. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 5170-5174
8. Leppla, S. H., Friedlander, A. M., and Cora, E. (1988) in Bacterial Protein Toxins (Fehrenbach, F., Alouf, J. E., Falmagne, P., Goebel, W., Jeljaszewicz, J., Jurgen, D., and Rappuoli, R., eds) pp. 111-112, Gustav Fischer, New York
9. Milne, J. C., Furlong, D., Hanna, P. C., Wall, J. S., and Collier, R. J. (1994) J. Biol. Chem. 269, 20607-20612
10. Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R., and Thomas, G. (1992) J. Biol. Chem. 267, 16396-16402
11. Klimpel, K. R., Molloy, S. S., Thomas, G., and Leppla, S. H. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 10277-10281
12. Mogridge, J., Cunningham, K., Lacy, D. B., Mourez, M., and Collier, R. J. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 7045-7048
13. Abrami, L., Liu, S., Cosson, P., Leppla, S. H., and van der Goot, F. G. (2003) J. Cell Biol. 3, 321-328
14. Blaustein, R. O., Koehler, T. M., Collier, R. J., and Finkelstein, A. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 2209-2213
15. Milne, J. C., and Collier, R. J. (1993) Mol. Microbiol. 10, 647-653
16. Petosa, C., Collier, R. J., Klimpel, K. R., Leppla, S. H., and Liddington, R. C. (1997) Nature 385, 833-838
17. Little, S. F., Novak, J. M., Lowe, J. R., Leppla, S. H., Singh, Y., Klimpel, K. R., Lidgerding, B. C., and Friedlander, A. M. (1996) Microbiology 142, 707-715
18. Singh, Y., Klimpel, K. R., Arora, N., Sharma, M., and Leppla, S. H. (1994) J. Biol. Chem. 269, 29039-29046
19. Khanna, H., Chopra, A. P., Arora, N., Chaudhry, A., and Singh, Y. (2001) FEMS Microbiol. Lett. 199, 27-31
20. Nassi, S., Collier, R. J., and Finkelstein, A. (2002) Biochemistry 41, 1445-1450
21. Mogridge, J., Mourez, M., and Collier, R. J. (2001) J. Bacteriol. 183, 2111-2116
22. Ahuja, N., Kumar, P., and Bhatnagar, R. (2001) Biochem. Biophys. Res. Commun. 287, 542-549
23. Noskov, A. N., Kravchenko, T. B., and Noskova, V. P. (1996) Mol. Gen. Mikrobiol. Virusol. 6, 16-20
24. Brossier, F., Sirard, J. C., Guidi-Rontani, C., Duflot, E., and Mock, M. (1999) Infect. Immun. 67, 964-967
25. Varughese, M., Teixeira, A. V., Liu, S., and Leppla, S. H. (1999) Infect. Immun. 67, 1860-1865
26. Little, S. F., Leppla, S. H., and Cora, E. (1988) Infect. Immun. 56, 1807-1813
27. Leppla, S. H., Robbins, J. B., Schneerson, R., and Shiloach, J. (2002) J. Clin. Invest. 110, 141-144
28. Maynard, J. A., Maassen, C. B., Leppla, S. H., Brasky, K., Patterson, J. L., Iverson, B. L., and Georgiou, G. (2002) Nat. Biotechnol. 20, 597-601
29. Leppla, S. H. (1988) Methods Enzymol. 165, 103-116
30. Park, S., and Leppla, S. H. (2000) Protein Expression Purif 18, 293-302
31. Gordon, V. M., Klimpel, K. R., Arora, N., Henderson, M. A., and Leppla, S. H. (1995) Infect. Immun. 63, 82-87
32. Singh, Y., Chaudhary, V. K., and Leppla, S. H. (1989) J. Biol. Chem. 264, 19103-19107
33. Ramirez, D. M., Leppla, S. H., Schneerson, R., and Shiloach, J. (2002) J. Ind. Microbiol. Biotechnol. 28, 232-238
34. Varughese, M., Chi, A., Teixeira, A. V., Nicholls, P. J., Keith, J. M., and Leppla, S. H. (1998) Mol. Med. 4, 87-95
35. Schuck, P., Boyd, L. F., and Andersen, P. S. (1999) in Current Protocols in Protein Science (Coligan, J. E., Dunn, B. M., Ploegh, H. L., Speicher, D. W., and Wingfield, P. T., eds) pp. 20.2.1-20.2.21, John Wiley & Sons, Inc., New York
36. Svitel, J., Balbo, A., Mariuzza, R. A., Gonzales, N. R., and Schuck, P. (2003) Biophys. J. 84, 4062-4077
37. Langmuir, I. (1918) J. Am. Chem. Soc. 40, 1361-1403
38. Svedberg, T., and Pedersen, K. O. (1940) The Ultracentrifuge, Oxford University Press, London
39. Schuck, P., and Braswell, E. H. (2000) in Current Protocols in Immunology (Coligan, J. E., Kruisbeek, A. M., Margulies, D. H., Shevach, E. M., and Strober, W., eds) John Wiley & Sons, Inc., New York
40. Kar, S. R., Kingsbury, J. S., Lewis, M. S., Laue, T. M., and Schuck, P. (2000) Anal. Biochem. 285, 135-142
41. Schuck, P. (2000) Biophys. J. 78, 1606-1619
42. Schuck, P., Perugini, M. A., Gonzales N. R., Howlett G. J., and Schubert, D. (2002) Biophys. J. 82, 1096-1111
43. Escuyer, V., and Collier, R. J. (1991) Infect. Immun. 59, 3381-3386
44. Arora, N., Klimpel K. R., Singh, Y., and Leppla, S. H. (1992) J. Biol. Chem. 267, 15542-15548
45. Schuck, P. (1997) Annu. Rev. Biophys. Biomol. Struct. 26, 541-566
46. Dickeson, S. K., Walsh, J. J., and Santoro, S. A. (1997) J. Biol. Chem. 272, 7661-7668
47. Emsley, J., King, S. L., Bergelson, J. M., and Liddington, R. C. (1997) J. Biol. Chem. 272, 28512-28517
48. Kamata, T., Liddington, R. C., and Takada, Y. (1999) J. Biol. Chem. 274, 32108-32111
49. Emsley, J., Knight, C. G., Farndale, R. W., Barnes, M. J., and Liddington, R. C. (2000) Cell 101, 47-56
50. Stanley, P., and Hogg, N. (1998) J. Biol. Chem. 273, 3358-3362
51. Legge, G. B., Morris, G. M., Sanner, M. F., Takada, Y., Olson, A. J., and Grynszpan, F. (2002) Proteins 48, 151-160