Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 69, 2005 - Issue 12
Journal homepage
149
Views
3
CrossRef citations to date
0
Altmetric
Original Articles

Neutralization of Burkholderia pseudomallei Protease by Fabs Generated through Phage Display

Sheila NATHANSchool of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia
,
Christoph RADERDepartment of Molecular Biology, Scripps Research Institute
&
Carlos F. BARBASDepartment of Molecular Biology, Scripps Research Institute
Pages 2302-2311 | Received 16 May 2005, Accepted 22 Aug 2005, Published online: 22 May 2014

  • 1) Wang, C.-I., Qing, Y., and Crik, C. S., Phage display of proteases and macromolecular inhibitors. Methods Enzym., 267, 52–68 (1996).
  • 2) Whitaker, M., Discovery of protease inhibitors using targeted libraries. Curr. Opin. Chem. Biol., 2, 386–396 (1998).
  • 3) Rader, C., and Barbas, C. F., III., Phage display of combinatorial antibody libraries. Curr. Opin. Biotech., 8, 503–508 (1997).
  • 4) Barbas, C. F., Scott, J. M., Silverman, G., and Burton, D. R., “Phage Display: A Laboratory Manual”, Cold Spring Harbor Laboratory Press, Plainview (2001).
  • 5) White, N. J., Melioidosis. Lancet, 361, 1715–1722 (2003).
  • 6) Brett, P. J., and Woods, D. E., Pathogenesis of and immunity to melioidosis. Acta Tropica, 74, 201–210 (2000).
  • 7) Esselman, M. T., and Liu, P. V., Lecithinase production by gram-negative bacteria. J. Bacteriol., 81, 939–945 (1961).
  • 8) Ashdown, L. R., and Koehler, J. M., Production of hemolysin and other extracellular enzymes by clinical isolates of Pseudomonas pseudomallei. J. Clin. Microbiol., 28, 2331–2334 (1990).
  • 9) Sexton, M. M., Jones, A. L., Chaowagul, W., and Woods, D. E., Purification and characterization of a protease from Pseudomonas pseudomallei. Can. J. Microbiol., 40, 903–910 (1994).
  • 10) Kondo, E., Kurata, T., Naigowit, P., and Kanai, K., Evolution of cell-surface acid phosphatase of Burkholderia pseudomallei. Asian J. Trop. Med. Public Health., 27, 592–599 (1996).
  • 11) Steinmetz, I., Rohde, M., and Brenneke, B., Purification and characterization of an exopolysaccharide of Burkholderia (Pseudomonas) pseudomallei. Infect. Immun., 63, 3959–3965 (1995).
  • 12) Harlow, E., and Lane, D., “Antibodies: A Laboratory Manual”, CSHL Press, N.Y., pp. 53–139 (1988).
  • 13) Barbas, C. F., Kang, A., Lerner, R., and Benkovic, S., Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. U.S.A., 88, 7978–7982 (1991).
  • 14) Rader, C., Ritter, G., Nathan, S., Elia, M., Gout, I., Jungbluth, A. A., Cohen, L. S., Welt, S., Old, L. J., and Barbas, C. F., III., The rabbit antibody repertoire as a novel source for the generation of therapeutic human antibodies. J. Biol. Chem., 275, 13668–13676 (2000).
  • 15) Percheron, G., Thibault, F., Paucod, J. C., and Vidal, D., Burkholderia pseudomallei requires Zn2+ for optimal exoprotease production in chemically defined media. Appl. Environ. Microbiol., 61, 3151–3153 (1995).
  • 16) Raffai, R., Vukmirica, J., Weisgraber, K. H., Rassart, E., Innerarity, T. L., and Milne, R., Bacterial expression and purification of the Fab fragment of a monoclonal antibody specific for the low-density lipoprotein receptor-binding site of human apolipoprotein E. Protein Express Purif., 16, 84–90 (1999).
  • 17) Donovan, R. S., Robinson, C. W., and Glick, B. R., Optimizing the expression of a monoclonal antibody fragment under the transcriptional control of the Escherichia coli lac promoter. Can. J. Microbiol., 46, 532–541 (2000).
  • 18) Rader, C., Cheresh, D. A., and Barbas, C. F., III., A phage display approach for rapid antibody humanization: designed combinatorial V gene libraries. Proc. Natl. Acad. Sci. U.S.A., 95, 8910–8915 (1998).
  • 19) Markland, W., Roberts, B. L., and Ladner, R. C., Selection for protease inhibitors using bacteriophage display. Methods Enzym., 267, 28–51 (1996).
  • 20) Kabat, E. A., Wu, T. T., Perry, H. M., Gottesman, K. S., and Foeller, C., “Sequences of Proteins of Immunological Interest” 5th ed., Public Health Service, National Institutes of Health, Bethesda (1991).
  • 21) Rodi, D. J., and Makowski, L., Phage display technology: finding a needle in a vast molecular haystack. Curr. Opin. Biotech., 10, 87–93 (1999).
  • 22) Griffiths, A. D., and Duncan, A. R., Strategies for selection of antibodies by phage display. Curr. Opin. Biotech., 9, 102–108 (1998).
  • 23) Hudson, P. J., Recombinant antibody constructs in cancer therapy. Curr. Opin. Immunol., 11, 548–557 (1999).
  • 24) Rader, C., Antibody libraries in drug and target discovery. Drug Disc. Today, 6, 36–40 (2001).
  • 25) Suzuki, Y., Ito, S., Otsuka, K., Iwasawa, E., Nakajima, M., and Yamaguchi, I., Preparation of functional single-chain antibodies against bioactive gibberellins by utilizing randomly mutagenized phage-display libraries. Biosci. Biotechnol. Biochem., 69, 610–619 (2005).
  • 26) Ling, J. M. L., Nathan, S., Lee, K. H., and Mohamed, R., Expression and characterisation of a B. pseudomallei serinemetalloprotease from a recombinant Escherichia coli. J. Biochem. Mol. Biol., 34, 509–516 (2001).
  • 27) Chan, S. W., Ong, G. I., and Nathan, S., Neutralizing chimeric mouse-human antibodies against Burkholderia pseudomallei protease: expression, purification and characterization. J. Biochem. Mol. Biol., 37, 556–564 (2004).
  • 28) Lee, M. A., and Liu, Y., Sequencing and characterization of a novel serine metalloprotease from Burkholderia pseudomallei. FEMS Microbiol. Lett., 192, 67–72 (2000).
  • 29) Nathan, S., Yap, T. L., and Sa’arwijaya, M. S. F., Burkholderia pseudomallei secretes metallo and serine protease in culture. Mal. J. Biochem. Mol. Biol., 11, 13–19 (2005).
  • 30) Volpert, O. V., Ward, W. F., Lingen, M. W., Chesler, L., Solt, D. B., Johnson, M. D., Molteni, A., Polverini, P. J., and Bouck, N. P., Captopril inhibits angiogenesis and slows the growth of experimental tumors in rats. J. Clin. Invest., 98, 671–679 (1996).
  • 31) Hugli, T. E., Protease inhibitors: novel therapeutic applications and development. TIBTECH, 14, 1–4 (1996).
  • 32) Gal-Tanamy, M., Zemel, R., Berdichevsky, Y., Bachmatov, L., Tur-Kaspa, R., and Benhar, I., HCV NS3 serine protease-neutralizing single-chain antibodies isolated by a novel genetic screen. J. Mol. Biol., 347, 991–1003 (2005).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.