Immune modulation by butyrophilins (original) (raw)
Heid, H. W., Winter, S., Bruder, G., Keenan, T. W. & Jarasch, E. D. Butyrophilin, an apical plasma membrane-associated glycoprotein characteristic of lactating mammary glands of diverse species. Biochim. Biophys. Acta728, 228–238 (1983). CASPubMed Google Scholar
Franke, W. W. et al. Antibodies to the major insoluble milk fat globule membrane-associated protein: specific location in apical regions of lactating epithelial cells. J. Cell Biol.89, 485–494 (1981). CASPubMed Google Scholar
Abeler-Dorner, L., Swamy, M., Williams, G., Hayday, A. C. & Bas, A. Butyrophilins: an emerging family of immune regulators. Trends Immunol.33, 34–41 (2012). This review provides a good summary of butyrophilin expression patterns. PubMed Google Scholar
Afrache, H., Gouret, P., Ainouche, S., Pontarotti, P. & Olive, D. The butyrophilin (BTN) gene family: from milk fat to the regulation of the immune response. Immunogenetics64, 781–794 (2012). This paper provides a comprehensive phylogenetic analysis of the relationships between mammalian butyrophilin family members and a proposal for a new naming convention. CASPubMed Google Scholar
Arnett, H. A., Escobar, S. S. & Viney, J. L. Regulation of costimulation in the era of butyrophilins. Cytokine46, 370–375 (2009). CASPubMed Google Scholar
Tazi-Ahnini, R. et al. Cloning, localization, and structure of new members of the butyrophilin gene family in the juxta-telomeric region of the major histocompatibility complex. Immunogenetics47, 55–63 (1997). CASPubMed Google Scholar
Rhodes, D. A., Stammers, M., Malcherek, G., Beck, S. & Trowsdale, J. The cluster of BTN genes in the extended major histocompatibility complex. Genomics71, 351–362 (2001). CASPubMed Google Scholar
Ikemizu, S. et al. Structure and dimerization of a soluble form of B7-1. Immunity12, 51–60 (2000). CASPubMed Google Scholar
Malcherek, G. et al. The B7 homolog butyrophilin BTN2A1 is a novel ligand for DC-SIGN. J. Immunol.179, 3804–3811 (2007). CASPubMed Google Scholar
Compte, E., Pontarotti, P., Collette, Y., Lopez, M. & Olive, D. Frontline: characterization of BT3 molecules belonging to the B7 family expressed on immune cells. Eur. J. Immunol.34, 2089–2099 (2004). CASPubMed Google Scholar
Chapoval, A. I. et al. BTNL8, a butyrophilin-like molecule that costimulates the primary immune response. Mol. Immunol.56, 819–828 (2013). This is one of the few papers demonstrating that recombinant butyrophilins can activate and enhance T cell responses. CASPubMed Google Scholar
Arnett, H. A. et al. BTNL2, a butyrophilin/B7-like molecule, is a negative costimulatory molecule modulated in intestinal inflammation. J. Immunol.178, 1523–1533 (2007). CASPubMed Google Scholar
Jeong, J. et al. The PRY/SPRY/B30.2 domain of butyrophilin 1A1 (BTN1A1) binds to xanthine oxidoreductase: implications for the function of BTN1A1 in the mammary gland and other tissues. J. Biol. Chem.284, 22444–22456 (2009). CASPubMedPubMed Central Google Scholar
Vorbach, C., Scriven, A. & Capecchi, M. R. The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary gland. Genes Dev.16, 3223–3235 (2002). CASPubMedPubMed Central Google Scholar
Sandstrom, A. et al. The intracellular B30.2 domain of butyrophilin 3A1 binds phosphoantigens to mediate activation of human Vγ9Vδ2 T cells. Immunity40, 490–500 (2014). This paper demonstrates that the intracellular B30.2 domain of butyrophilins can mediate a biological effect that results in the activation ofγδT cells. CASPubMedPubMed Central Google Scholar
Smith, I. A. et al. BTN1A1, the mammary gland butyrophilin, and BTN2A2 are both inhibitors of T cell activation. J. Immunol.184, 3514–3525 (2010). CASPubMed Google Scholar
Nguyen, T., Liu, X. K., Zhang, Y. & Dong, C. BTNL2, a butyrophilin-like molecule that functions to inhibit T cell activation. J. Immunol.176, 7354–7360 (2006). CASPubMedPubMed Central Google Scholar
Yamazaki, T. et al. A butyrophilin family member critically inhibits T cell activation. J. Immunol.185, 5907–5914 (2010). CASPubMed Google Scholar
Yang, Y. et al. Characterization of B7S3 as a novel negative regulator of T cells. J. Immunol.178, 3661–3667 (2007). CASPubMed Google Scholar
Mana, P. et al. Tolerance induction by molecular mimicry: prevention and suppression of experimental autoimmune encephalomyelitis with the milk protein butyrophilin. Int. Immunol.16, 489–499 (2004). CASPubMed 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). CASPubMed Google Scholar
Messal, N. et al. Differential role for CD277 as a co-regulator of the immune signal in T and NK cells. Eur. J. Immunol.41, 3443–3454 (2011). CASPubMed Google Scholar
Yamashiro, H., Yoshizaki, S., Tadaki, T., Egawa, K. & Seo, N. Stimulation of human butyrophilin 3 molecules results in negative regulation of cellular immunity. J. Leukoc. Biol.88, 757–767 (2010). CASPubMed Google Scholar
Palakodeti, A. et al. The molecular basis for modulation of human Vγ9Vδ2 T cell responses by CD277/butyrophilin-3 (BTN3A)-specific antibodies. J. Biol. Chem.287, 32780–32790 (2012). This paper provides an insight into the molecular basis of how different BTN3A-specific monoclonal antibodies can drive disparate, and even opposing, biological functions. CASPubMedPubMed Central Google Scholar
Ammann, J. U., Cooke, A. & Trowsdale, J. Butyrophilin Btn2a2 inhibits TCR activation and phosphatidylinositol 3-kinase/Akt pathway signaling and induces Foxp3 expression in T lymphocytes. J. Immunol.190, 5030–5036 (2013). CASPubMedPubMed Central Google Scholar
Swanson, R. M. et al. Butyrophilin-like 2 modulates B7 costimulation to induce Foxp3 expression and regulatory T cell development in mature T cells. J. Immunol.190, 2027–2035 (2013). This is one of the first papers demonstrating that butyrophilins support the differentiation of naive T cells into TRegcells. CASPubMed Google Scholar
Boyden, L. M. et al. Skint1, the prototype of a newly identified immunoglobulin superfamily gene cluster, positively selects epidermal γδ T cells. Nature Genet.40, 656–662 (2008). This study suggests that butyrophilins may have a role in thymic selection of T cells. CASPubMed Google Scholar
Turchinovich, G. & Hayday, A. C. Skint-1 identifies a common molecular mechanism for the development of interferon-γ-secreting versus interleukin-17-secreting γδ T cells. Immunity35, 59–68 (2011). CASPubMed Google Scholar
Bas, A. et al. Butyrophilin-like 1 encodes an enterocyte protein that selectively regulates functional interactions with T lymphocytes. Proc. Natl Acad. Sci. USA108, 4376–4381 (2011). CASPubMed Google Scholar
Barbee, S. D. et al. Skint-1 is a highly specific, unique selecting component for epidermal T cells. Proc. Natl Acad. Sci. USA108, 3330–3335 (2011). CASPubMed Google Scholar
Harly, C. et al. Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress sensing by a major human γδ T-cell subset. Blood120, 2269–2279 (2012). CASPubMedPubMed Central Google Scholar
Wang, H. et al. Butyrophilin 3A1 plays an essential role in prenyl pyrophosphate stimulation of human Vγ2Vδ2 T cells. J. Immunol.191, 1029–1042 (2013). This is one of the first papers to suggest that BTN3A1 is a key molecular player in facilitating the activation ofγδT cells in response to prenyl pyrophosphate antigens during cellular stress. CASPubMed Google Scholar
Decaup, E. et al. Phosphoantigens and butyrophilin 3A1 induce similar intracellular activation signaling in human TCRVγ9 γδ T lymphocytes. Immunol. Lett.161, 133–137 (2014). CASPubMed Google Scholar
Esser, C. A fat story–antigen presentation by butyrophilin 3A1 to γδ T cells. Cell. Mol. Immunol.11, 5–7 (2014). PubMed Google Scholar
Kabelitz, D. Critical role of butyrophilin 3A1 in presenting prenyl pyrophosphate antigens to human γδ T cells. Cell. Mol. Immunol.11, 117–119 (2014). CASPubMed Google Scholar
Vavassori, S. et al. Butyrophilin 3A1 binds phosphorylated antigens and stimulates human γδ T cells. Nature Immunol.14, 908–916 (2013). CAS Google Scholar
Simone, R. et al. Ligation of the BT3 molecules, members of the B7 family, enhance the proinflammatory responses of human monocytes and monocyte-derived dendritic cells. Mol. Immunol.48, 109–118 (2010). CASPubMed Google Scholar
Viken, M. K. et al. Reproducible association with type 1 diabetes in the extended class I region of the major histocompatibility complex. Genes Immun.10, 323–333 (2009). CASPubMed Google Scholar
Fujimaki, T. et al. Association of a polymorphism of BTN2A1 with dyslipidemia in East Asian populations. Exp. Ther. Med.2, 745–749 (2011). CASPubMedPubMed Central Google Scholar
Hiramatsu, M. et al. Synergistic effects of genetic variants of APOA5 and BTN2A1 on dyslipidemia or metabolic syndrome. Int. J. Mol. Med.30, 185–192 (2012). CASPubMed Google Scholar
Horibe, H. et al. Association of a polymorphism of BTN2A1 with dyslipidemia in community-dwelling individuals. Mol. Med. Rep.9, 808–812 (2014). CASPubMed Google Scholar
Yamada, Y. et al. Association of a polymorphism of BTN2A1 with myocardial infarction in East Asian populations. Atherosclerosis215, 145–152 (2011). CASPubMed Google Scholar
Yoshida, T. et al. Association of polymorphisms of BTN2A1 and ILF3 with myocardial infarction in Japanese individuals with different lipid profiles. Mol. Med. Rep.4, 511–518 (2011). CASPubMed Google Scholar
Cubillos-Ruiz, J. R. et al. CD277 is a negative co-stimulatory molecule universally expressed by ovarian cancer microenvironmental cells. Oncotarget1, 329–338 (2010). PubMedPubMed Central Google Scholar
Peedicayil, A. et al. Risk of ovarian cancer and inherited variants in relapse-associated genes. PLoS ONE5, e8884 (2010). PubMedPubMed Central Google Scholar
Fitzgerald, L. M. et al. Germline missense variants in the BTNL2 gene are associated with prostate cancer susceptibility. Cancer Epidemiol. Biomarkers Prev.22, 1520–1528 (2013). CASPubMedPubMed Central Google Scholar
Jacques, P. & Van den Bosch, F. Emerging therapies for rheumatoid arthritis. Expert Opin. Emerg. Drugs18, 231–244 (2013). CASPubMed Google Scholar
Yao, S., Zhu, Y. & Chen, L. Advances in targeting cell surface signalling molecules for immune modulation. Nature Rev. Drug Discov.12, 130–146 (2013). CAS Google Scholar
Cubillos-Ruiz, J. R. & Conejo-Garcia, J. R. It never rains but it pours: potential role of butyrophilins in inhibiting anti-tumor immune responses. Cell Cycle10, 368–369 (2011). CASPubMedPubMed Central Google Scholar
Bonneville, M. & Scotet, E. Human Vγ9Vδ2 T cells: promising new leads for immunotherapy of infections and tumors. Curr. Opin. Immunol.18, 539–546 (2006). CASPubMed Google Scholar
Chiplunkar, S., Dhar, S., Wesch, D. & Kabelitz, D. γδ T cells in cancer immunotherapy: current status and future prospects. Immunotherapy1, 663–678 (2009). CASPubMed Google Scholar
Cavaletto, M. et al. A proteomic approach to evaluate the butyrophilin gene family expression in human milk fat globule membrane. Proteomics2, 850–856 (2002). CASPubMed Google Scholar
Giuffrida, M. G. et al. Proteolysis of milk fat globule membrane proteins in preterm milk: a transient phenomenon with a possible biological role? Int. J. Immunopathol. Pharmacol.21, 959–967 (2008). CASPubMed Google Scholar
Cavaletto, M., Giuffrida, M. G. & Conti, A. Milk fat globule membrane components—a proteomic approach. Adv. Exp. Med. Biol.606, 129–141 (2008). CASPubMed Google Scholar
Lonnerdal, B., Woodhouse, L. R. & Glazier, C. Compartmentalization and quantitation of protein in human milk. J. Nutr.117, 1385–1395 (1987). CASPubMed Google Scholar
Peterson, J. A., Scallan, C. D., Ceriani, R. L. & Hamosh, M. Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane. Adv. Exp. Med. Biol.501, 179–187 (2001). CASPubMed Google Scholar
Ogg, S. L., Weldon, A. K., Dobbie, L., Smith, A. J. & Mather, I. H. Expression of butyrophilin (Btn1a1) in lactating mammary gland is essential for the regulated secretion of milk-lipid droplets. Proc. Natl Acad. Sci. USA101, 10084–10089 (2004). CASPubMed Google Scholar
Robenek, H. et al. Butyrophilin controls milk fat globule secretion. Proc. Natl Acad. Sci. USA103, 10385–10390 (2006). CASPubMed Google Scholar
Hiramatsu, M. et al. Association of a polymorphism of BTN2A1 with type 2 diabetes mellitus in Japanese individuals. Diabet Med.28, 1381–1387 (2011). CASPubMed Google Scholar
Horibe, H. et al. Association of a polymorphism of BTN2A1 with hypertension in Japanese individuals. Am. J. Hypertens.24, 924–929 (2011). CASPubMed Google Scholar
Oguri, M. et al. Association of a genetic variant of BTN2A1 with metabolic syndrome in East Asian populations. J. Med. Genet.48, 787–792 (2011). CASPubMed Google Scholar
Yoshida, T. et al. Association of a genetic variant of BTN2A1 with chronic kidney disease in Japanese individuals. Nephrol.16, 642–648 (2011). CAS Google Scholar
Konno, S. et al. Genetic impact of a butyrophilin-like 2 (BTNL2) gene variation on specific IgE responsiveness to Dermatophagoides farinae (Der f) in Japanese. Allergol Int.58, 29–35 (2009). CASPubMed Google Scholar
Li, Y., Pabst, S., Lokhande, S., Grohe, C. & Wollnik, B. Extended genetic analysis of BTNL2 in sarcoidosis. Tissue Antigens73, 59–61 (2009). CASPubMed Google Scholar
Mitsunaga, S. et al. Exome sequencing identifies novel rheumatoid arthritis-susceptible variants in the BTNL2. J. Hum. Genet.58, 210–215 (2013). CASPubMed Google Scholar
Morais, A. et al. BTNL2 gene polymorphism associations with susceptibility and phenotype expression in sarcoidosis. Respir. Med.106, 1771–1777 (2012). PubMed Google Scholar
Orozco, G. et al. Analysis of a functional BTNL2 polymorphism in type 1 diabetes, rheumatoid arthritis, and systemic lupus erythematosus. Hum. Immunol.66, 1235–1241 (2005). CASPubMed Google Scholar
Pathan, S. et al. Confirmation of the novel association at the BTNL2 locus with ulcerative colitis. Tissue Antigens74, 322–329 (2009). CASPubMed Google Scholar
Rybicki, B. A. et al. The BTNL2 gene and sarcoidosis susceptibility in African Americans and Whites. Am. J. Hum. Genet.77, 491–499 (2005). CASPubMedPubMed Central Google Scholar
Simmonds, M. J., Heward, J. M., Barrett, J. C., Franklyn, J. A. & Gough, S. C. Association of the BTNL2 rs2076530 single nucleotide polymorphism with Graves' disease appears to be secondary to DRB1 exon 2 position β74. Clin. Endocrinol.65, 429–432 (2006). CAS Google Scholar
Spagnolo, P. et al. Analysis of BTNL2 genetic polymorphisms in British and Dutch patients with sarcoidosis. Tissue Antigens70, 219–227 (2007). CASPubMed Google Scholar
Valentonyte, R. et al. Sarcoidosis is associated with a truncating splice site mutation in BTNL2. Nature Genet.37, 357–364 (2005). This is an elegant study that presents a molecular model of BTNL2 and its genetic variants. CASPubMed Google Scholar
Aigner, J. et al. A common 56-kilobase deletion in a primate-specific segmental duplication creates a novel butyrophilin-like protein. BMC Genet.14, 61 (2013). CASPubMedPubMed Central Google Scholar
Lian, Y., Yue, J., Han, M., Liu, J. & Liu, L. Analysis of the association between BTNL2 polymorphism and tuberculosis in Chinese Han population. Infect. Genet. Evol.10, 517–521 (2010). CASPubMed Google Scholar
Price, P. et al. Two major histocompatibility complex haplotypes influence susceptibility to sporadic inclusion body myositis: critical evaluation of an association with HLA-DR3. Tissue Antigens64, 575–580 (2004). CASPubMed Google Scholar
Wijnen, P. A. et al. Butyrophilin-like 2 in pulmonary sarcoidosis: a factor for susceptibility and progression? Hum. Immunol.72, 342–347 (2011). CASPubMed Google Scholar
Hsueh, K. C., Lin, Y. J., Chang, J. S., Wan, L. & Tsai, F. J. BTNL2 gene polymorphisms may be associated with susceptibility to Kawasaki disease and formation of coronary artery lesions in Taiwanese children. Eur. J. Pediatr.169, 713–719 (2010). PubMed Google Scholar
Johnson, C. M. et al. Analysis of the BTNL2 truncating splice site mutation in tuberculosis, leprosy and Crohn's disease. Tissue Antigens69, 236–241 (2007). CASPubMed Google Scholar
Mochida, A. et al. Butyrophilin-like 2 gene is associated with ulcerative colitis in the Japanese under strong linkage disequilibrium with HLA-DRB1*1502. Tissue Antigens70, 128–135 (2007). CASPubMed Google Scholar
Scott, A. P. et al. Recombination mapping of the susceptibility region for sporadic inclusion body myositis within the major histocompatibility complex. J. Neuroimmunol.235, 77–83 (2011). CASPubMed Google Scholar
Henry, J. et al. Cloning, structural analysis, and mapping of the B30 and B7 multigenic families to the major histocompatibility complex (MHC) and other chromosomal regions. Immunogenetics46, 383–395 (1997). CASPubMed Google Scholar
Rhodes, D. A., de Bono, B. & Trowsdale, J. Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence? Immunology116, 411–417 (2005). CASPubMedPubMed Central Google Scholar
Perfetto, L. et al. Exploring the diversity of SPRY/B30.2-mediated interactions. Trends Biochem. Sci.38, 38–46 (2013). CASPubMed Google Scholar
D'Cruz, A. A., Babon, J. J., Norton, R. S., Nicola, N. A. & Nicholson, S. E. Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity. Protein Sci.22, 1–10 (2013). CASPubMed Google Scholar
Chae, J. J. et al. The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1β production. Proc. Natl Acad. Sci. USA103, 9982–9987 (2006). CASPubMed Google Scholar
Chae, J. J. et al. The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-κB through its N-terminal fragment. Blood112, 1794–1803 (2008). CASPubMedPubMed Central Google Scholar
Le Page, C. et al. BTN3A2 expression in epithelial ovarian cancer is associated with higher tumor infiltrating T cells and a better prognosis. PLoS ONE7, e38541 (2012). CASPubMedPubMed Central Google Scholar