Structural basis of inducible costimulator ligand costimulatory function: Determination of the cell surface oligomeric state and functional mapping of the receptor binding site of the protein

Journal of Immunology

Volumn 177, Issue 6, 2006, Pages 3920-3929

  Chattopadhyay, Kausik ^a   Bhatia, Sumeena ^a   Fiser, Andras ^a   Almo, Steven C ^a   Nathenson, Stanley G ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

B7 ANTIGEN; CD28 ANTIGEN; CD86 ANTIGEN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; GLYCOPROTEIN; IMMUNOGLOBULIN; INDUCIBLE COSTIMULATOR LIGAND; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIGEN STRUCTURE; ARTICLE; BETA SHEET; BINDING SITE; CELL SURFACE; GENE MUTATION; LIGAND BINDING; LYMPHOCYTE FUNCTION; MOLECULAR RECOGNITION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR BINDING; SEQUENCE HOMOLOGY; T LYMPHOCYTE ACTIVATION;

EID: 33748509734     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.6.3920     Document Type: Article

References (33)

1. Sharpe, A. H., and G. J. Freeman. 2002. The B7-CD28 superfamily. Nat. Rev. Immunol. 2: 116-126.
2. Alegre, M. L., K. A. Frauwirth, and C. B. Thompson. 2001. T cell regulation by CD28 and CTLA-4. Nat. Rev. Immunol. 1: 220-228.
3. Greenwald, R. J., G. J. Freeman, and A. H. Sharpe. 2005. The B7-family revisited. Annu. Rev. Immunol. 23: 515-548.
4. Hutloff, A., A. M. Dittrich, K. C. Beier, B. Eljaschewitsch, R. Kraft, I. Anagnostopoulos, and R. A. Kroczek. 1999. ICOS is an inducible T cell costimulator structurally and functionally related to CD28. Nature 397: 263-266.
5. Yoshinaga, S. K., J. S. Whoriskey, S. D. Khare, U. Sarmiento, J. Guo, T. Horan, G. Shih, M. Zhang, M. A. Coccia, T. Kohno, et al. 1999. T cell co-stimulation through B7RP-1 and ICOS. Nature 402: 827-832.
6. Dong, C., A. E. Juedes, U. A. Temann, S. Shresta, J. P. Allison, N. H. Ruddle, and R. A. Flavell. 2001. ICOS co-stimulatory receptor is essential for T cell activation and function. Nature 409: 97-101.
7. Tafuri, A., A. Shahinian, F. Bladt, S. K. Yoshinaga, M. Jordana, A. Wakeham, L. M. Boucher, D. Bouchard, V. S. F. Chan, G. Duncan, et al. 2001. ICOS is essential for effective T helper cell responses. Nature 409: 105-109.
8. McAdam, A. J., R. J. Greenwald, M. A. Levin, T. Chernova, N. Malenkovich, V. Ling, G. J. Freeman, and A. H. Sharpe. 2001. ICOS is critical for CD40-mediated antibody class switching. Nature 409: 102-105.
9. Nurieva, R. I., X. M. Mai, K. Forbush, M. J. Bevan, and C. Dong. 2003. B7h is required for T cell activation, differentiation, and effector function. Proc. Natl. Acad. Sci. USA 100: 14163-14168.
10. Wang, S., G. Zhu, K. Tamada, L. Chen, and J. Bajorath. 2002. Ligand binding sites of inducible costimulator and high avidity mutants with improved function J. Exp. Med. 195: 1033-1041.
11. Peach, R. J., J. Bajorath, W. Brady, G. Leytze, J. Greene, J. Naemura, and P. S. Linsley. 1994. Complementarity determining region 1 (CDR1)- and CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1. J. Exp. Med. 180: 2049-2058.
12. Wang, S., G. Zhu, A. I. Chapoval, H. Dong, K. Tamada, J. Ni, and L. Chen. 2000. Costimulation of T cells by B7-H2, a B7-like molecule that binds ICOS. Blood 96: 2808-2813.
13. + T cells. Proc. Natl. Acad. Sci. USA 99: 6198-6203.
14. Bhatia, S., M. Edidin, S. C. Almo, and S. G. Nathenson. 2005. Different cell surface oligomeric states of B7-1 and B7-2: Implications for signaling. Proc. Natl. Acad. Sci. USA 102: 15569-15574.
15. Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
16. Gouet, P., X. Robert, and E. Courcelle. 2003. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31: 3320-3323.
17. Sali, A., and T. L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234: 779-815.
18. Bourne, P.E., K. J. Addess, W. F. Bluhm, L. Chen, N. Deshpande, Z. Feng, W. Fieri, R. Green, J. C. Merino-Ott, W. Townsend-Merino, et al. 2004. The distribution and query systems of the RCSB Protein Data Bank. Nucleic Acids Res. 32(database issue): D223-D225.
19. Altschul, S. F., T. L. Madden, A. A. Schaffer, J. Zhang, Z. Zhang, W. Miller, and D. J. Lipman. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25: 3389-3402.
20. Rai, B. K., and A. Fiser. 2006. Multiple Mapping Method: a novel approach to the sequence-to-structure alignment problem in comparative protein structure modeling. Proteins 63: 644-661.
21. Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
22. Edidin, M. 2002. Fluorescence resonance energy transfer: techniques for measuring molecular conformation and molecular proximity. In Current Protocols in Immunology. J. E. Coligan, A. M. Cruisbeek, D. H. Margulies, E. M. Shevach, and W. Strober, eds. Wiley, Hoboken, pp. 18.10.1-18.10.18.
23. Kenworthy, A. K., and M. Edidin. 1998. Distributions of a GPI-anchored protein at the apical surface of MDCK cells examined at a resolution of <100Å using imaging fluorescence resonance energy transfer. J. Cell Biol. 142: 69-84.
24. Pentcheva, T., and M. Edidin. 2001. Clustering of peptide-loaded MHC class I molecules for ER export imaged by fluorescence resonance energy transfer. J. Immunol. 166: 6625-6632.
25. Adair, B. D., and D. M. Engelman. 1994. Glycophorin A helical transmembrane domains dimerize in phospholipid bilayers: a resonance energy transfer study. Biochemistry 33: 5539-5544.
26. Li, E., M. You, and K. Hristova. 2005. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and forster resonance energy transfer suggest weak interactions between fibroblast growth factor receptor 3 (FGFR3) transmembrane domains in the absence of extracellular domains and ligands. Biochemistry 44: 352-360.
27. Majeti, R., Z. Xu, T. G. Parslow, J. L. Olson, D. I. Daikh, N. Killeen, and A. Weiss. 2000. An inactivating point mutation in the inhibitory wedge of CD45 causes lymphoproliferation and autoimmunity. Cell 103: 1059-1070.
28. Stamper, C. C., Y. Zhang, J. F. Tobin, D. V. Erbe, S. Ikemizu, S. J. Davis, M. L. Stahl, J. Seehra, W. S. Somers, and L. Mosyak. 2001. Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses. Nature 410: 608-611.
29. Schwartz, J. C., X. Zhang, A. A. Fedorov, S. G. Nathenson, and S. C. Almo. 2001. Structural basis for co-stimulation by the human CTLA-4/B7-2 complex. Nature 410: 604-608.
30. Peach, R. J., J. Bajorath, J. Naemura, G. Leytze, J. Greene, A. Aruffo, and P. S. Linsley. 1995. Both extracellular immunoglobulin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28. J. Biol. Chem. 270: 21181-21187.
31. Fargeas, C. A., A. Truneh, M. Reddy, M. Hurle, R. Sweet, and R. P. Sekaly. 1995. Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA4. J. Exp. Med. 182: 667-675.
32. Ikemizu, S., R. J. C. Gilbert, J. A. Fennelly, A. V. Collins, K. Harlos, E. Y. Jones, D. I. Stuart, and S. J. Davis. 2000. Structure and dimerization of a soluble form of B7-1. Immunity 12: 51-60.
33. Zhang, X., J. C. Schwartz, S. C. Almo, and S. G. Nathenson. 2003. Crystal structure of the receptor binding domain of human B7-2: insights into organization and signaling. Proc. Natl. Acad. Sci. USA 100: 2586-2591.