SpringerProtocols: Abstract: Single-Domain VH Antibody Fragments from a Phage Display Library

Single-Domain VH Antibody Fragments from a Phage Display Library

By: Liat Binyamin³, Daniel Plaksin⁴, Yoram Reiter³

Abstract

Full Text

Download PDF (105K)

The interaction between antigens and antibodies can be viewed as a protein engineering system that was optimized by nature and is capable of recognizing any given molecular entity (antigen). Antigen recognition is conferred to the antibody by a limited number of hypervariable surface loops, differing in sequence and in length, which are connected to a conserved framework structure.

Affiliation(s): (3) Faculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel
(4) Molecular Biology Group, Peptor Ltd., Kiryat Weizmann, Israel

Book Title: Recombinant Antibodies for Cancer Therapy: Methods and Protocols

Series: Methods in Molecular Biology | Volume: 207 | Pub. Date: Sep-16-2002 | Page Range: 133-143 | DOI: 10.1385/1-59259-334-8:133

Subject: Cancer Research

References

Download References

1.	Reiter Y. and Pastan I. (1998). Fv fragments of antibodies as novel reagents for cancer therapy and diagnosis. Trends Biotechnol. 16, 513–520. <Occurrence Type="DOI"><Handle>10.1016/S0167-7799(98)01226-8</Handle></Occurrence>

2.	Vitetta E. S., Thorpe P. E., and Uhr J. (1993). Immunotoxins: magic bullets or misguided missiles. Trends Pharmacol. Sci. 14, 148–154. <Occurrence Type="DOI"><Handle>10.1016/0165-6147(93)90199-T</Handle></Occurrence>

3.	Haard H., Henderikx P., and Hoogenboom H. R. (1998). Creating and engineering human antibodies for immunotherapy. Advan. Drug Del. Rev. 31, 5–31. <Occurrence Type="DOI"><Handle>10.1016/S0169-409X(97)00091-4</Handle></Occurrence>

4.	Winter G., Griffith A. D., Hawkins R. E., and Hoogenboom H. R. (1994). Making antibodies by phage display technology. Annu. Rev. Immunol. 12, 433–455.

5.	Barbas C. F. (1995). Synthetic human antibodies. Nature Med. 1, 837–839.

6.	Hoogenboom H. R., Bruine A. P., Hufton S. E., Hoet R. M., Arends J., and Roovers R. C. (1998). Antibody phage display technology and its applications. Immunotechnology 4, 1–20. <Occurrence Type="DOI"><Handle>10.1016/S1380-2933(98)00007-4</Handle></Occurrence>

7.	Bird R. E., Hardman K. D., Jacobson J. W., Johnson S., Kaufman B. M., and Lee S. M. (1988). Single-chain antigen binding proteins. Science 242, 423–426.

8.	Huston J. S., Levinson D., Mudghett-Hunter M., Tai M. S., Novotny J., and Margolies M. N. (1988). Protein enginnering of antibody binding sites: recovery of specific activity in an anti dogoxigenin single-chain Fv analogue produced in Escherichia coli. Proc. Natl Acad. Sci. USA 85, 5879–5883.

9.	Glockshuber R., Malia M., Pfitzinger I., and Pluckthun A. (1990). A comparision of strategies to stabilize immunoglobulin Fv fragments. Biochemistry 29 1362–1376.

10.	Reiter Y., Brinkmann U., Lee B. K., and Pastan I. (1996). Engineering antibody Fv fragments for cancer detection and therapy: Disulfide-stabilized Fv fragments. Nature Biotechnol. 14, 1239–1245.

11.	Padlan E. A. (1994). Anatomy of the antibody molecule. Mol. Immunol. 31, 169–217. <Occurrence Type="DOI"><Handle>10.1016/0161-5890(94)90001-9</Handle></Occurrence>

12.	Webster D. M., Henry A. H., and Rees A. R. (1994). Antibody-antigen interactions. Curr. Opin. Struct. Biol. 4, 123–129. <Occurrence Type="DOI"><Handle>10.1016/S0959-440X(94)90070-1</Handle></Occurrence>

13.	Chothia C. and Lesk A. (1987). Canonical structures of the hypervariable regions of immunoglobulins. J. Mol. Biol. 196, 904–917. <Occurrence Type="DOI"><Handle>10.1016/0022-2836(87)90412-8</Handle></Occurrence>

14.	Chothia C., Novotny J., Bruccoleri R., and Karplus M. (1985). Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186, 651–663. <Occurrence Type="DOI"><Handle>10.1016/0022-2836(85)90137-8</Handle></Occurrence>

15.	Ward E. S., Gussow D., Griffith A. D., Jones P. T., and Winter G. (1989). Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341, 544–546.

16.	Muyldermans S., Atarhouch T., Saldanha J., Barbosa J. A. and Hamers R. (1994). Sequence and structure of VH domain from naturally occuring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 7, 1129–1135.

17.	Davies J. and Riechmann L. (1995). Antibody V_H domains as small recognition units. Biotechnology 13, 475–479.

18.	Davies J. and Riechmann L. (1996). Affinity improvement of single antibody V_H domains. Residues in all three hypervariable regions affect antigen binding. Immunotechnology 2, 169–179.

19.	Kortt A. A., Guthrie R. E., Hinds M. G., Power B. E., Ivancic N., Caldwell B. J., et al. (1995). Solution properties of Escherichia coli-expressed V_H domain of anti-neuraminidase antibody NC41. J. Protein Chem. 14, 167–178.

20.	Ghahroudi M. A., Desmyter A., Wyns L., Hamers R., and Muyldermans S. (1997). Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 414, 521–526. <Occurrence Type="DOI"><Handle>10.1016/S0014-5793(97)01062-4</Handle></Occurrence>

21.	Lauwereys M., Ghahroudi M. A., Desmyter A., Kinne J., Holzer W., DeGenst E., et al. (1998). Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. EMBO J. 17, 3512–3520.

22.	Martin F., Volpari C., Steinkuhler C., Dimasi N., Brunetti M., Biasiol G. et al. (1997). Affinity selection of a camelized V_H domain antibody inhibitor of hepatitis C virus NS3 protease. Protein Eng. 10, 607–614.

23.	Sheriff S. and Constantine K. L. (1996). Redefining the minimal antigen-binding fragment. Nature Struct. Biol. 3, 733–736.

24.	Reiter Y., Schuck P., Boyd L., and Plaksin D. (1999). An Antibody Single-domain Phage Display Library of a Native Heavy Chain Variable Region: Isolation of Functional Singledomain V_H Molecules with a Unique Interface. J. Mol. Biol. 292, 685–698.

25.	Polakova K., Plaksin D., Chung D. H., Belyakov I. M., Berzofsky J. A., and Margulies D. H. (2000). Antibodies directed against the MHC-I molecule H-2D(d) complexed with an antigenic peptide: similarities to a T cell receptor with the same specificity. J. Immunol. 165, 5703–5712.

Comments (Loading...)

Post comment/View all comments