Conserved motifs in T-cell receptor CDR1 and CDR2: Implications for ligand and CD8 co-receptor binding

Current Opinion in Immunology

Volumn 10, Issue 1, 1998, Pages 74-81

  Arden, Bernhard ^a  

^a LUDWIG MAXIMILIANS UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CD8 ANTIGEN; HLA A2 ANTIGEN; T LYMPHOCYTE RECEPTOR;

COMPLEMENTARITY DETERMINING REGION; GENE SEQUENCE; GERM LINE; LIGAND BINDING; MOLECULAR MODEL; NONHUMAN; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN STRUCTURE; RECEPTOR BINDING; REVIEW; X RAY CRYSTALLOGRAPHY;

EID: 0032006927     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(98)80035-6     Document Type: Article

References (47)

1. Davies DR, Padlan EA, Sheriff S. Antibody-antigen complexes. Annu Rev Biochem. 59:1990;439-473.
2. Wilson IA, Stanfield RL. Antibody-antigen interactions: New structures and new conformational changes. Curr Opin Struct Biol. 4:1994;857-867.
3. Davis MM, Bjorkman PJ. T-cell antigen receptor genes and T-cell recognition. Nature. 334:1988;395-402.
4. Garcia KC, Degano M, Stanfield RL, Brunmark A, Jackson MR, Peterson PA, Teyton L, Wilson IA. An αβ T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. of outstanding interest Science. 274:1996;209-219 This paper describes the X-ray structure of a murine TCR αβ heterodimer and defines its orientation with respect to a class I MHC-peptide complex. The Vα complementarity-determining regions (CDRs) 1 and 2 are positioned over the amino-terminal region of the peptide and the Vβ CDRs 1 and 2 over the carboxy-terminal region of the peptide. The Vα and Vβ CDR3s form a hydrophobic cavity over the central position of the peptide.
5. Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. of outstanding interest Nature. 384:1996;134-141 This study describes the crystal structure of a ternary complex containing a human T-cell receptor, peptide and HLA-A2, and defines contact points between the T-cell receptor, peptide and MHC, thus providing evidence for the generality of the diagonal orientation of binding.
6. Sun R, Shepherd SE, Geier SS, Thomson CT, Sheil JM, Nathenson SG. Evidence that the antigen receptors of cytotoxic T lymphocytes interact with a common recognition pattern on the H-2 Kb molecule. Immunity. 3:1995;573-582.
7. Sant'Angelo DB, Waterbury G, Preston-Hurlburt P, Yoon ST, Medzhitov R, Hong S-C, Janeway CA. The specificity and orientation of a TCR to its peptide-MHC class II ligands. of special interest Immunity. 4:1996;367-376 Using peptide immunizations of mice carrying α of β chain T-cell receptor (TCR) transgenes this study identifies three contact residues that protrude upwards from a peptide bound to the MHC class II molecule I-Ak. This information supports the orientation shown for class I restricted TCR [6].
8. Ignatowicz L, Kappler J, Marrack P. The repertoire of T cells shaped by a single MHC/peptide ligand. of special interest Cell. 84:1996;521-529 This paper describes the expression of a transgene encoding a class II MHC protein occupied by a single antigenic peptide covalently attached by a flexible linker. All detectable class II molecules in these mice carry the transgene-encoded peptide. As they mature in the thymus, T cells frequently react with foreign MHC. Results suggest that the repertoire of T-cell receptor αβ receptors may be even more biased to react with MHC molecules of any type, including foreign MHC, than was previously suspected.
9. + T cells was quite efficient, yielding a large and broad repertoire.
10. Chothia C, Lesk AM. Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol. 196:1987;901-918.
11. Chothia C, Lesk AM, Tramontano A, Levitt M, Smith-Gill SJ, Air G, Sheriff S, Padlan EA, Davies D, Tulip WR, et al. Conformations of immunoglobulin hypervariable regions. Nature. 342:1989;877-883.
12. Fields BA, Ober B, Malchiodi EL, Lebedeva MI, Braden BC, Ysern X, Kim J-K, Shao X, Ward ES, Mariuzza RA. Crystal structure of the Vα domain of a T cell antigen receptor. Science. 270:1995;1821-1824.
13. Arden B, Clark SP, Kabelitz D, Mak TW. Mouse T-cell receptor variable gene segment families. Immunogenetics. 42:1995;501-530.
14. Housset D, Mazza G, Grégoire C, Piras C, Malissen B, Fontecilla-Camps JC. The three-dimensional structure of a T-cell antigen receptor Vα Vβ heterodimer reveals a novel arrangement of the Vβ domain. EMBO J. 16:1997;4205-4216.
15. Bentley GA, Boulot G, Karjaleinen K, Mariuzza RA. Crystal structure of the β chain of a T cell antigen receptor. Science. 267:1995;1984-1987.
16. Bentley GA, Boulot G, Mariuzza RA. The structure of the antigen-binding site of immunoglobulins and T-cell receptors. Res Immunol. 146:1995;277-290.
17. Padlan EA. On the nature of antibody combining sites: unusual structural features that may confer on these sites an enhanced capacity for binding ligands. Proteins. 7:1990;112-124.
18. Bentley GA, Mariuzza RA. The structure of the T cell antigen receptor. Annu Rev Immunol. 14:1996;563-590.
19. Arden B, Clark SP, Kabelitz D, Mak TW. Human T-cell receptor variable gene segment families. Immunogenetics. 42:1995;455-500.
20. Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
21. Clark SP, Arden B, Kabelitz D, Mak TW. Comparison of human and murine T-cell receptor variable gene segment subfamilies. Immunogenetics. 42:1995;531-540.
22. Chothia C, Lesk AM, Gherardi E, Tomlinson I, Walter G, Marks JD, Llewelyn MB, Winter G. Structural repertoire of the human VH segments. J Mol Biol. 227:1992;799-817.
23. Tomlinson IM, Cox JPL, Gherardi E, Lesk AM, Chothia C. The structural repertoire of the human Vκ domain. EMBO J. 14:1995;4628-4638.
24. Tramontano A, Chothia C, Lesk AM. Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulins. J Mol Biol. 215:1990;175-182.
25. Bork P, Holm L, Sander C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J Mol Biol. 242:1994;309-320.
26. Sloan-Lancaster J, Allen P. Altered peptide ligand-induced partial T cell activation: molecular mechanisms and role in T cell biology. Annu Rev Immunol. 14:1996;1-27.
27. Luescher IF, Vivier E, Layer A, Mahiou J, Godeau F, Malissen B, Romero P. CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes. Nature. 373:1995;353-356.
28. Garcia KC, Scott CA, Brunmark A, Carbone FR, Peterson PA, Wilson IA, Teyton L. CD8 enhances formation of stable T-cell receptor/MHC class I molecule complexes. of outstanding interest Nature. 384:1996;577-581 This study used surface plasmon resonance to obtain data on the kinetics of the receptor - ligand interactions. It reports that the affinity of the T-cell receptor (TCR) for its specific peptide - MHC complex is enhanced through a reduced off rate in the presence of the CD8 molecule. It is concluded that CD8 guides an energetically favorable docking of the TCR onto MHC.
29. Gao GF, Tormo J, Gerth UC, Wyer JR, McMichael AJ, Stuart DI, Bell JI, Jones EY, Jakobsen BK. Crystal structure of the complex between human CD8αα and HLA-A2. of outstanding interest Nature. 387:1997;630-634 A flexible loop of the α3 domain of HLA-A2 is clamped between the complementarity-determining region-like loops of the two CD8 subunits in the classic manner seen with antibody - antigen interaction. The position of the α3 domain is different from that in uncomplexed HLA-A2, but no conformational change extends to the MHC/peptide surface presented for T-cell receptor recognition.
30. Von Itzstein M, Wu W-Y, Kok GB, Pegg MS, Dyason JC, Jin B, Phan TV, Smythe ML, White HF, Oliver SW, et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature. 363:1993;418-423.
31. Stehle T, Yan Y, Benjamin TL, Harrison SC. Structure of human polyoma virus complexed with an oligosaccharide receptor fragment. Nature. 369:1994;160-163.
32. Kelm S, Pelz A, Schauer R, Filbin MT, Tang S, de Bellard M-E, Schnaar RL, Mahoney JA, Hartnell A, Bradfield P, Cocker PR. Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr Biol. 4:1994;965-972.
33. Nath D, van der Merwe A, Kelm S, Bradfield P, Crocker PR. The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. J Biol Chem. 270:1995;26184-26191.
34. Van der Merwe PA, Crocker PR, Vinson M, Barclay AN, Schauer R, Kelm S. Localization of the putative sialic acid-binding site on the immunoglobulin superfamily cell-surface molecule CD22. of outstanding interest J Biol Chem. 271:1996;9273-9280 Using surface plasmon resonance this study characterizes the interaction of CD22 with CD45. By in situ desialylation and resialylation it is shown that CD22 binds to sialoglycoconjugates carried on CD45. All 12 mutations that abrogated binding were of residues within domain 1 of CD22, centered around a conserved arginine residue. This paper provides further evidence that immunoglobulin superfamily cell adhesion molecules use one β sheet of the membrane-distal variable domains to bind structurally diverse ligands for cell - cell recognition.
35. Cyster JG, Goodnow CC. Tuning antigen receptor signaling by CD22: Integrating cues from antigens and the microenvironment. of special interest Immunity. 6:1997;509-517 Review of evidence demonstrating that regulation of B-cell antigen receptor signaling by CD22 may be mediated by the amino-terminal lectin domains of CD22 binding to sialic-acid-containing sugars expressed on immunoglobulin M. This association could be altered by competition for binding to other sialylated proteins in the microenvironment or on activated B cells wich increase expression of sialytransferase.
36. Nitschke L, Carsetti R, Ocker B, Köhler G, Lamers MC. CD22 is a negative regulator of B-cell receptor signalling. Curr Biol. 7:1997;133-143.
37. Freeman SD, Kelm S, Barber EK, Crocker PR. Characterization of CD33 as a new member of the sialoadhesin family of cellular interaction molecules. Blood. 85:1995;2005-2012.
38. Vinson M, van der Merwe PA, Kelm S, May A, Jones EY, Crocker PR. Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis. of outstanding interest J Biol Chem. 271:1996;9267-9272 The sialic acid binding site of sialoadhesin is located in the amino-terminal V-set domain of 17 extracellular immunoglobulin-like domains. By site-directed mutagenesis a contiguous binding site is located on the GFCC′ C″β sheet centered around an arginine in the F strand, the key residue in mediating sialic-acid-dependent binding.
39. Morschhäuser J, Hoschützky H, Jann K, Hacker J. Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis. Infect Immun. 58:1990;2133-2138.
40. König R, Huang L-Y, Germain RN. MHC class II interaction with CD4 mediated by a region analogous to the MHC class I binding site for CD8. Nature. 356:1992;796-798.
41. Huang B, Yachou A, Fleury S, Hendrickson WA, Sekali R-P. Analysis of the contact sites on the CD4 molecule with class II MHC molecules. Co-ligand versus co-receptor function. J Immunol. 158:1997;216-225.
42. Wang J, Yan Y, Garrett TPJ, Liu J, Rodgers DW, Garlick RL, Tarr GE, Husain Y, Reinherz EL, Harrison SC. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature. 348:1990;411-418.
43. Brady RL, Dodson EJ, Lange G, Davis SJ, Williams AF, Barclay AN. Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains. Science. 260:1993;979-983.
44. Bernard O, Hozumi N, Tonegawa S. Sequences of mouse immunoglobulin light chain genes before and after somatic changes. Cell. 15:1990;1133-1144.
45. Pech M, Höchtl J, Schnell H, Zachau HG. Differences between germ-line and rearranged immunoglobulin Vκ coding sequences suggests a localized mutation mechanism. Nature. 291:1981;668-670.
46. Schiff C, Milili M, Fougereau M. Functional and pseudogenes are similarly organized and may equally contribute to the extensive antibody diversity of the immunoglobulinVHII family. EMBO J. 4:1985;1225-1230.
47. Kabat EA, Wu TT, Perry HM, Gottesman KS, Foeller C. Edn 5 Sequences of Proteins of Immunological Interest. 1991;Public Health Service, NIH, Washington, DC.