The B7–CD28 superfamily (original) (raw)

• Bretscher, P. & Cohn, M. A theory of self-nonself discrimination. Science 169, 1042–1049 (1970).
  Article CAS PubMed Google Scholar
• Bretscher, P. A. A two-step, two-signal model for the primary activation of precursor helper T cells. Proc. Natl Acad. Sci. USA 96, 185–190 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Jenkins, M. K. & Schwartz, R. H. Antigen presentation by chemically modified splenocytes induces antigen-specific T cell unresponsiveness in vitro and in vivo. J. Exp. Med. 165, 302–319 (1987).
  Article CAS PubMed Google Scholar
• Viola, A. & Lanzavecchia, A. T cell activation determined by T cell receptor number and tunable thresholds. Science 273, 104–106 (1996).
  Article CAS PubMed Google Scholar
• Sloan-Lancaster, J., Evavold, B. D. & Allen, P. M. Induction of T-cell anergy by altered T-cell-receptor ligand on live antigen-presenting cells. Nature 363, 156–159 (1993).
  Article CAS PubMed Google Scholar
• Karandikar, N. J., Vanderlugt, C. L., Bluestone, J. A. & Miller, S. D. Targeting the B7/CD28:CTLA-4 costimulatory system in CNS autoimmune disease. J. Neuroimmunol. 89, 10–18 (1998).
  Article CAS PubMed Google Scholar
• Oosterwegel, M. A., Greenwald, R. J., Mandelbrot, D. A., Lorsbach, R. B. & Sharpe, A. H. CTLA-4 and T cell activation. Curr. Opin. Immunol. 11, 294–300 (1999).
  Article CAS PubMed Google Scholar
• Salomon, B. & Bluestone, J. A. Complexities of CD28/B7:CTLA-4 costimulatory pathways in autoimmunity and transplantation. Annu. Rev. Immunol. 19, 225–252 (2001).
  Article CAS PubMed Google Scholar
• Sansom, D. M. CD28, CTLA-4 and their ligands: who does what and to whom? Immunology 101, 169–177 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Chambers, C. A., Kuhns, M. S., Egen, J. G. & Allison, J. P. CTLA-4-mediated inhibition in regulation of T cell responses: mechanisms and manipulation in tumor immunotherapy. Annu. Rev. Immunol. 19, 565–594 (2001).
  Article CAS PubMed Google Scholar
• Hutloff, A. et al. ICOS is an inducible T-cell co-stimulator structurally and functionally related to CD28. Nature 397, 263–266 (1999).Identifies ICOS as a CD28 homologue on activated human T cells and shows that, in conjunction with a TCR signal, ICOS crosslinking upregulates cytokine production, particularly of IL-10 but not of IL-2.
  Article CAS PubMed Google Scholar
• Isikawa, K. et al. Prediction of the coding sequence of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5, 169–176 (1998).
  Article Google Scholar
• Swallow, M. M., Wallin, J. J. & Sha, W. C. B7h, a novel costimulatory homolog of B7.1 and B7.2, is induced by TNF-α. Immunity 11, 423–432 (1999).
  Article CAS PubMed Google Scholar
• Ling, V. et al. Cutting edge: identification of GL50, a novel B7-like protein that functionally binds to ICOS receptor. J. Immunol. 164, 1653–1657 (2000).
  Article CAS PubMed Google Scholar
• Yoshinaga, S. K. et al. T-cell co-stimulation through B7RP-1 and ICOS. Nature 402, 827–832 (1999).Identifies a B7 homologue as the ligand for ICOS and shows an important role for the ICOS pathway in regulating T-cell help for antibody production.
  Article CAS PubMed Google Scholar
• Brodie, D. et al. LICOS, a primordial costimulatory ligand? Curr. Biol. 10, 333–336 (2000).
  Article CAS PubMed Google Scholar
• Wang, S. et al. Costimulation of T cells by B7-H2, a B7-like molecule that binds ICOS. Blood 96, 2808–2813 (2000).
  Article CAS PubMed Google Scholar
• Ishida, Y., Agata, Y., Shibahara, K. & Honjo, T. Induced expression of PD-1, a novel member of the immunoglobulin gene superfamily, upon programmed cell death. EMBO J. 11, 3887–3895 (1992).
  Article CAS PubMed PubMed Central Google Scholar
• Freeman, G. J. et al. Engagement of the PD-1 immunoinhibitory receptor by a novel B7 family member leads to negative regulation of lymphocyte activation. J. Exp. Med. 192, 1–9 (2000).Identifies a B7 homologue as the receptor for PD-1 and shows that, in conjunction with a TCR signal, this ligand can inhibit T-cell activation and cytokine production.
  Article Google Scholar
• Dong, H., Zhu, G., Tamada, K. & Chen, L. B7-H1, a third member of the B7 family, co-stimulates T cell proliferation and interleukin-10 secretion. Nature Med. 5, 1365–1369 (1999).Identifies a B7 homologue, shows that it is expressed on activated T cells and APCs, and reports the stimulation of T-cell proliferation and cytokine production, particularly of IL-10.
  Article CAS PubMed Google Scholar
• Latchman, Y. et al. PD-L2 is a second ligand for PD-1 and inhibits T cell activation. Nature Immunol. 2, 261–268 (2001).Identifies a B7 homologue as a second receptor for PD-1 and shows expression on activated APCs, some non-lymphoid tissues and breast tumours. Shows inhibition of T-cell activation and cytokine production in an antigen-specific system via recruitment of SHP-2.
  Article CAS Google Scholar
• Tseng, S. Y. et al. B7-DC, a new dendritic cell molecule with potent costimulatory properties for T cells. J. Exp. Med. 193, 839–846 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Freeman, G. J. et al. Structure, expression, and T cell costimulatory activity of the murine homologue of the human B lymphocyte activation antigen B7. J. Exp. Med. 174, 625–631 (1991).
  Article CAS PubMed Google Scholar
• Freedman, A. S. et al. B7, a B cell restricted antigen which identifies pre-activated B cells. J. Immunol. 139, 3260–3267 (1987).
  CAS PubMed Google Scholar
• Yokochi, T., Holly, R. D. & Clark, E. A. Lymphoblastoid antigen (BB-1) expressed on Epstein–Barr virus-activated B cell blasts, B lymphoblastoid lines, and Burkitt's lymphomas. J. Immunol. 128, 823–827 (1982).
  CAS PubMed Google Scholar
• Freeman, G. J. et al. Cloning of B7-2: a CTLA4 counter-receptor that costimulates human T cell proliferation. Science 262, 909–911 (1993).
  Article CAS PubMed Google Scholar
• Freeman, G. J. et al. Murine B7-2, an alternative CTLA4 counter-receptor that costimulates T cell proliferation and interleukin-2 production. J. Exp. Med. 178, 2185–2192 (1993).
  Article CAS PubMed Google Scholar
• Azuma, M. et al. B70 antigen is a second ligand for CTLA-4 and CD28. Nature 366, 76–79 (1993).
  Article CAS PubMed Google Scholar
• Aruffo, A. & Seed, B. Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system. Proc. Natl Acad. Sci. USA 84, 8573–8577 (1987).
  Article CAS PubMed PubMed Central Google Scholar
• Gross, J. A., St John, T. & Allison, J. P. The murine homologue of the T lymphocyte antigen CD28. Molecular cloning and cell surface expression. J. Immunol. 144, 3201–3210 (1990).
  CAS PubMed Google Scholar
• Brunet, J. F. et al. A new member of the immunoglobulin superfamily — CTLA-4. Nature 328, 267–270 (1987).
  Article CAS PubMed Google Scholar
• Linsley, P. et al. CTLA-4 is a second receptor for the B cell activation antigen B7. J. Exp. Med. 174, 561–569 (1991).
  Article CAS PubMed Google Scholar
• Peach, R. J. et al. 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 (1994).
  Article CAS PubMed Google Scholar
• Linsley, P. S. et al. Coexpression and functional cooperation of CTLA-4 and CD28 on activated T lymphocytes. J. Exp. Med. 176, 1595–1604 (1992).
  Article CAS PubMed Google Scholar
• Linsley, P. S. et al. Human B7-1 (CD80) and B7-2 (CD86) bind with similar avidities but distinct kinetics to CD28 and CTLA4 receptors. Immunity 1, 793–801 (1994).
  Article CAS PubMed Google Scholar
• Gross, J., Callas, E. & Allison, J. Identification and distribution of the costimulatory receptor CD28 in the mouse. J. Immunol. 149, 380–388 (1992).
  CAS PubMed Google Scholar
• Linsley, P. et al. Intracellular trafficking of CTLA4 and focal localization towards sites of TCR engagement. Immunity 4, 535–543 (1996).
  Article CAS PubMed Google Scholar
• Hathcock, K. S., Laszlo, G., Pucillo, C., Linsley, P. & Hodes, R. J. Comparative analysis of B7-1 and B7-2 costimulatory ligands: expression and function. J. Exp. Med. 180, 631–640 (1994).
  Article CAS PubMed Google Scholar
• McAdam, A., Schweitzer, A. & Sharpe, A. H. The role of B7 costimulation in activation and differentiation of CD4 and CD8 T cells. Immunol. Rev. 165, 231–247 (1998).
  Article CAS PubMed Google Scholar
• Lenschow, D. J., Walunas, T. L. & Bluestone, J. A. CD28/B7 system of T cell costimulation. Annu. Rev. Immunol. 14, 233–258 (1996).
  Article CAS PubMed Google Scholar
• Lanzavecchia, A., Lezzi, G. & Viola, A. From TCR engagement to T cell activation: a kinetic view of T cell behavior. Cell 96, 1–4 (1999).
  Article CAS PubMed Google Scholar
• Thompson, C. B. et al. CD28 activation pathway regulates the production of multiple T-cell-derived lymphokines/cytokines. Proc. Natl Acad. Sci. USA 86, 1333–1337 (1989).
  Article CAS PubMed PubMed Central Google Scholar
• Lucas, P. J. et al. Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response. J. Immunol. 154, 5757–5768 (1995).
  CAS PubMed Google Scholar
• Shahinian, A. et al. Differential T cell costimulatory requirements in CD28-deficient mice. Science 261, 609–612 (1993).
  Article CAS PubMed Google Scholar
• Sperling, A. I. et al. CD28/B7 interactions deliver a unique signal to naive T cells that regulates cell survival but not early proliferation. J. Immunol. 157, 3909–3917 (1996).
  CAS PubMed Google Scholar
• Boise, L., Minn, A., Noel, P. & Thompson, C. CD28 costimulation can promote T cell survival by enhancing the expression of Bcl-xl. Immunity 3, 87–98 (1995).
  Article CAS PubMed Google Scholar
• Walunas, T. L. et al. CTLA-4 can function as a negative regulator of T cell activation. Immunity 1, 405–413 (1994).
  Article CAS PubMed Google Scholar
• Walunas, T. L., Bakker, C. Y. & Bluestone, J. A. CTLA-4 ligation blocks CD28-dependent T cell activation. J. Exp. Med. 183, 2541–2550 (1996).
  Article CAS PubMed Google Scholar
• Krummel, M. & Allison, J. CD28 and CTLA4 have opposing effects on the response of T cells to stimulation. J. Exp. Med. 182, 459–466 (1995).
  Article CAS PubMed Google Scholar
• Brunner, M., Chambers, C. & Allison, J. CTLA-4 mediates inhibition of early events of T cell proliferation. J. Immunol. 162, 5813–5820 (1999).
  CAS PubMed Google Scholar
• Greenwald, R. J., Boussiotis, V. A., Lorsbach, R. B., Abbas, A. K. & Sharpe, A. H. CTLA-4 regulates induction of anergy in vivo. Immunity 14, 145–155 (2001).
  Article CAS PubMed Google Scholar
• Waterhouse, P. et al. Lymphoproliferative disorders with early lethality in mice deficient in CTLA-4. Science 270, 985–988 (1995).
  Article CAS PubMed Google Scholar
• Tivol, E. et al. Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 3, 541–547 (1995).
  Article CAS PubMed Google Scholar
• Mandelbrot, D. A., McAdam, A. J. & Sharpe, A. H. B7-1 or B7-2 is required to produce the lymphoproliferative phenotype in mice lacking cytotoxic T lymphocyte-associated antigen 4 (CTLA-4). J. Exp. Med. 189, 435–440 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Perez, V. et al. Induction of peripheral T cell tolerance in vivo requires CTLA-4 engagement. Immunity 6, 411–417 (1997).
  Article CAS PubMed Google Scholar
• Leach, D. R., Krummel, M. F. & Allison, J. P. Enhancement of antitumor immunity by CTLA4 blockade. Science 271, 1734–1736 (1996).
  Article CAS PubMed Google Scholar
• Perrin, P. J., Maldonado, J. H., Davis, T. A., June, C. H. & Racke, M. K. CTLA-4 blockade enhances clinical disease and cytokine production during experimental allergic encephalomyelitis. J. Immunol. 157, 1333–1336 (1996).
  CAS PubMed Google Scholar
• Buonfiglio, D. et al. The T cell activation molecule H4 and the CD28-like molecule ICOS are identical. Eur. J. Immunol. 30, 3463–3467 (2000).
  Article CAS PubMed Google Scholar
• Tezuka, K. et al. Identification and characterization of rat AILIM/ICOS, a novel T-cell costimulatory molecule, related to the CD28/CTLA4 family. Biochem. Biophys. Res. Commun. 276, 335–345 (2000).
  Article CAS PubMed Google Scholar
• Beier, K. C. et al. Induction, binding specificity and function of human ICOS. Eur. J. Immunol. 30, 3707–3717 (2000).
  Article CAS PubMed Google Scholar
• Coyle, A. J. et al. The CD28-related molecule ICOS is required for effective T cell-dependent immune responses. Immunity 13, 95–105 (2000).
  Article CAS PubMed Google Scholar
• Holdorf, A. D., Kanagawa, O. & Shaw, A. S. CD28 and T cell co-stimulation. Rev. Immunogenet. 2, 175–184 (2000).
  CAS PubMed Google Scholar
• Mages, H. W. et al. Molecular cloning and characterization of murine ICOS and identification of B7h as ICOS ligand. Eur. J. Immunol. 30, 1040–1047 (2000).
  Article CAS PubMed Google Scholar
• McAdam, A. J. et al. Mouse inducible costimulatory molecule (ICOS) expression is enhanced by CD28 costimulation and regulates differentiation of CD4+ T cells. J. Immunol. 165, 5035–5040 (2000).
  Article CAS PubMed Google Scholar
• Aicher, A. et al. Characterization of human inducible costimulator ligand expression and function. J. Immunol. 164, 4689–4696 (2000).
  Article CAS PubMed Google Scholar
• Kopf, M. et al. Inducible costimulator protein (ICOS) controls T helper cell subset polarization after virus and parasite infection. J. Exp. Med. 192, 53–61 (2000).Shows that ICOS co-stimulates both T H 1 and T H 2 responses, and can regulate both CD28-dependent and CD28-independent CD4+ T-cell responses in parasite-induced T H 2 and virus-induced T H 1 models.
  Article CAS PubMed PubMed Central Google Scholar
• McAdam, A. et al. ICOS is critical for CD40 mediated antibody class switching. Nature 409, 102–105 (2001).Shows a crucial role for ICOS in regulating immunoglobulin isotype class switching and germinal centre formation, by evaluating ICOS-deficient mice (similar to Refs 68,70 ). Shows that the defects in class switching in ICOS-deficient mice could be overcome by CD40 stimulation, indicating important interactions between these pathways
  Article CAS PubMed Google Scholar
• Dong, C. et al. ICOS co-stimulatory receptor is essential for T cell activation and function. Nature 409, 97–101 (2001).
  Article CAS PubMed Google Scholar
• Dong, C., Temann, U. A. & Flavell, R. A. Cutting edge: critical role of inducible costimulator in germinal center reactions. J. Immunol. 166, 3659–3662 (2001).
  Article CAS PubMed Google Scholar
• Tafuri, A. et al. ICOS is essential for effective T helper cell responses. Nature 409, 105–109 (2001).
  Article CAS PubMed Google Scholar
• Yoshinaga, S. K. et al. Characterization of a new human B7-related protein: B7RP-1 is the ligand to the co-stimulatory protein ICOS. Int. Immunol. 12, 1439–1447 (2000).
  Article CAS PubMed Google Scholar
• Richter, G. et al. Tumor necrosis factor-α regulates the expression of ICOS ligand on CD34+ progenitor cells during differentiation into antigen presenting cells. J. Biol. Chem. 276, 45686–45693 (2001).
  Article CAS PubMed Google Scholar
• Riley, J. L. et al. ICOS costimulation requires IL-2 and can be prevented by CTLA-4 engagement. J. Immunol. 166, 4943–4948 (2001).
  Article CAS PubMed Google Scholar
• Tesciuba, A. G. et al. Inducible costimulator regulates TH2-mediated inflammation, but not TH2 differentiation, in a model of allergic airway disease. J. Immunol. 167, 1996–2003 (2001).
  Article CAS PubMed Google Scholar
• Gonzalo, J. A. et al. ICOS is critical for T helper cell-mediated lung mucosal inflammatory responses. Nature Immunol. 2, 597–604 (2001).Shows differences in the roles of CD28 and ICOS in an allergic lung inflammation model: CD28 is required for priming whereas ICOS is needed for T H effector responses.
  Article CAS Google Scholar
• Sporici, R. A. & Perrin, P. J. Costimulation of memory T-cells by ICOS: a potential therapeutic target for autoimmunity? Clin. Immunol. 100, 263–269 (2001).
  Article CAS PubMed Google Scholar
• Sperling, A. I. ICOS costimulation: is it the key to selective immunotherapy? Clin. Immunol. 100, 261–262 (2001).
  Article CAS PubMed Google Scholar
• Ozkaynak, E. et al. Importance of ICOS–B7RP-1 costimulation in acute and chronic allograft rejection. Nature Immunol. 2, 591–596 (2001).Identifies a role for ICOS in acute and chronic rejection using cardiac allograft models. Shows that a combination of anti-ICOS antibody and cyclosporin can lead to long-term graft survival.
  Article CAS Google Scholar
• Furukawa, Y., Mandelbrot, D. A., Libby, P., Sharpe, A. H. & Mitchell, R. N. Association of B7-1 co-stimulation with the development of graft arterial disease. Studies using mice lacking B7-1, B7-2, or B7-1/B7-2. Am. J. Pathol. 157, 473–484 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Kim, K. S. et al. CD28-B7-mediated T cell costimulation in chronic cardiac allograft rejection: differential role of B7-1 in initiation versus progression of graft arteriosclerosis. Am. J. Pathol. 158, 977–986 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Borriello, F. et al. B7-1 and B7-2 have overlapping, critical roles in immunoglobulin class switching and germinal center formation. Immunity 6, 303–313 (1997).
  Article CAS PubMed Google Scholar
• Rottman, J. B. et al. The costimulatory molecule ICOS plays an important role in the immunopathogenesis of EAE. Nature Immunol. 2, 605–611 (2001).
  Article CAS Google Scholar
• Sporici, R. A. et al. ICOS ligand costimulation is required for T-cell encephalitogenicity. Clin. Immunol. 100, 277–288 (2001).Shows an important role for ICOS in regulating the T H 1-mediated disease EAE and that ICOSL blockade after the onset of EAE can ameliorate clinical disease.
  Article CAS PubMed Google Scholar
• Chang, T. C., Jabs, C., Sobel, R. A., Kuchroo, V. K. & Sharpe, A. H. Studies in B7-deficient mice reveal a critical role for B7 costimulation in both the initiation and effector phases of EAE. J. Exp. Med. 190, 733–740 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Perrin, P. J., Lavi, E., Rumbley, C. A., Zekavat, S. A. & Phillips, S. M. Experimental autoimmune meningitis: a novel neurological disease in CD28-deficient mice. Clin. Immunol. 91, 41–49 (1999).
  Article CAS PubMed Google Scholar
• Segal, B. M., Dwyer, B. K. & Shevach, E. M. An interleukin (IL)-10/IL-12 immunoregulatory circuit controls susceptibility to autoimmune disease. J. Exp. Med. 187, 537–546 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Bettelli, E. et al. IL-10 is critical in the regulation of autoimmune encephalomyelitis as demonstrated by studies of IL-10- and IL-4-deficient and transgenic mice. J. Immunol. 161, 3299–3306 (1998).
  CAS PubMed Google Scholar
• Wallin, J. J., Liang, L., Bakardjiev, A. & Sha, W. C. Enhancement of CD8+ T cell responses by ICOS/B7h costimulation. J. Immunol. 167, 132–139 (2001).
  Article CAS PubMed Google Scholar
• Shinohara, T., Taniwaki, M., Ishida, Y., Kawaichi, M. & Honjo, T. Structure and chromosomal localization of the human PD-1 gene (PPCP1). Genomics 23, 704–706 (1994).
  Article CAS PubMed Google Scholar
• Vibhakar, R., Juan, G., Traganos, F., Darzynkiewicz, Z. & Finger, L. R. Activation-induced expression of human programmed death-1 gene in T-lymphocytes. Exp. Cell Res. 232, 25–28 (1997).
  Article CAS PubMed Google Scholar
• Agata, Y. et al. Expression of the PD-1 antigen on the surface of stimulated mouse T and B lymphocytes. Int. Immunol. 8, 765–772 (1996).
  Article CAS PubMed Google Scholar
• Nishimura, H. et al. Developmentally regulated expression of the PD-1 protein on the surface of double-negative (CD4− CD8−) thymocytes. Int. Immunol. 8, 773–780 (1996).
  Article CAS PubMed Google Scholar
• Nishimura, H., Honjo, T. & Minato, N. Facilitation of β selection and modification of positive selection in the thymus of PD-1 deficient mice. J. Exp. Med. 191, 891–898 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Bleul, C. C. & Boehm, T. Laser capture microdissection-based expression profiling identifies PD1-ligand as a target of the nude locus gene product. Eur. J. Immunol. 31, 2497–2503 (2001).
  Article CAS PubMed Google Scholar
• Eppihimer, M. et al. Expression and regulation of the PD-L1 immuno-inhibitory molecule on microvascular endothelial cells. Microcirculation (in the press).
• Nishimura, H., Minato, N., Nakano, T. & Honjo, T. Immunological studies on PD-1 deficient mice: implication of PD-1 as a negative regulator for B cell responses. Int. Immunol. 10, 1563–1572 (1998).
  Article CAS PubMed Google Scholar
• Nishimura, H., Nose, M., Hiai, H., Minato, N. & Honjo, T. Development of lupus-like autoimmune diseases by disruption of the PD-1 gene encoding an ITIM motif-carrying immunoreceptor. Immunity 11, 141–151 (1999).Shows that PD-1-deficient mice have a defect in peripheral tolerance with the late-onset development of lupus-like autoimmune disease. Shows that CD8+ TCR transgenic mice that escape thymic deletion become activated in the periphery and cause graft-versus-host-like disease.
  Article CAS PubMed Google Scholar
• Nishimura, H. et al. Autoimmune dilated cardiomyopathy in PD-1 receptor deficient mice. Science 291, 319–322 (2001).
  Article CAS PubMed Google Scholar
• Carter, L. L. et al. PD-1:PD-L inhibitory pathway affects both CD4+ and CD8+ T cells and is overcome by IL-2. Eur. J. Immunol. (in the press).
• Baecher-Allan, C., Brown, J. A., Freeman, G. J. & Hafler, D. A. CD4+CD25(high) regulatory cells in human peripheral blood. J. Immunol. 167, 1245–1253 (2001).
  Article CAS PubMed Google Scholar
• Tamura, H. et al. B7-H1 costimulation preferentially enhances CD28-independent T-helper cell function. Blood 97, 1809–1816 (2001).
  Article CAS PubMed Google Scholar
• Okazaki, T., Nishimura, H. & Honjo, T. PD-1 immunoreceptor inhibits B cell receptor-mediated signaling by recruiting Src homology 2-domain-containing tyrosine phosphatase 2 to phosphotyrosine. Proc. Natl. Acad. Sci. USA 98, 13866–13871 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Shlapatska, L. M. et al. CD150 association with either the SH2-containing inositol-phosphate or the SH2-containing protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A J. Immunol. 166, 5480–5487 (2001).
  Article CAS PubMed Google Scholar
• Chapoval, A. et al. B7-H3: a costimulatory molecule for T cell activation and IFN-γ production. Nature Immunol. 2, 269–274 (2001).Identifies a B7 homologue and shows that it has a receptor on T cells whose engagement co-stimulates CD4+ and CD8+ T-cell proliferation, IFNγ production, and CD8 lytic activity.
  Article CAS Google Scholar
• Ogg, S. L., Komaragiri, M. V. & Mather, I. H. Structural organization and mammary-specific expression of the butyrophilin gene. Mamm. Genome 7, 900–905 (1996).
  Article CAS PubMed Google Scholar
• Rhodes, D. A., Stammers, M., Malcherek, G., Beck, S. & Trowsdale, J. The cluster of BTN genes in the extended major histocompatibility complex. Genomics 71, 351–362 (2001).
  Article CAS PubMed Google Scholar
• Stammers, M., Rowen, L., Rhodes, D., Trowsdale, J. & Beck, S. BTL-II: a polymorphic locus with homology to the butyrophilin gene family, located at the border of the major histocompatibility complex class II and class III regions in human and mouse. Immunogenetics 51, 373–382 (2000).
  Article CAS PubMed Google Scholar
• Linsley, P. S., Peach, R., Gladstone, P. & Bajorath, J. Extending the B7 (CD80) gene family. Protein Sci. 3, 1341–1343 (1994).
  Article CAS PubMed PubMed Central Google Scholar
• Mather, I. H. A review and proposed nomenclature for major proteins of the milk-fat globule membrane. J. Dairy Sci. 83, 203–247 (2000).
  Article CAS PubMed Google Scholar
• Banghart, L. R. et al. Butyrophilin is expressed in mammary epithelial cells from a single-sized messenger RNA as a type I membrane glycoprotein. J. Biol. Chem. 273, 4171–4179 (1998).
  Article CAS PubMed Google Scholar
• Seto, M. H., Liu, H. L., Zajchowski, D. A. & Whitlow, M. Protein fold analysis of the B30.2-like domain. Proteins 35, 235–249 (1999).
  Article CAS PubMed Google Scholar
• Ishii, T. et al. Carboxy-terminal cytoplasmic domain of mouse butyrophilin specifically associates with a 150-kDa protein of mammary epithelial cells and milk fat globule membrane. Biochim. Biophys. Acta 1245, 285–292 (1995).
  Article PubMed Google Scholar
• Peterson, J. A. et al. Milk fat globule glycoproteins in human milk and in gastric aspirates of mother's milk-fed preterm infants. Pediatr. Res. 44, 499–506 (1998).
  Article CAS PubMed Google Scholar
• Stefferl, A. et al. Butyrophilin, a milk protein, modulates the encephalitogenic T cell response to myelin oligodendrocyte glycoprotein in experimental autoimmune encephalomyelitis. J. Immunol. 165, 2859–2865 (2000).
  Article CAS PubMed Google Scholar
• Fahrer, A. M., Bazan, J. F., Papathanasiou, P., Nelms, K. A. & Goodnow, C. C. A genomic view of immunology. Nature 409, 836–838 (2001).
  Article CAS PubMed Google Scholar
• Ikemizu, S. et al. Structure and dimerization of a soluble form of B7-1. Immunity 12, 51–60 (2000).
  Article CAS PubMed Google Scholar
• Schwartz, J. C., Zhang, X., Fedorov, A. A., Nathenson, S. G. & Almo, S. C. Structural basis for co-stimulation by the human CTLA-4/B7-2 complex. Nature 410, 604–608 (2001).
  Article CAS PubMed Google Scholar
• Stamper, C. C. et al. Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses. Nature 410, 608–611 (2001).
  Article CAS PubMed Google Scholar