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Gene Review

PPIB  -  peptidylprolyl isomerase B (cyclophilin B)

Homo sapiens

Synonyms: CYP-S1, CYPB, Cyclophilin B, HEL-S-39, OI9, ...
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Disease relevance of PPIB


High impact information on PPIB


Chemical compound and disease context of PPIB

  • The crystal structures analyzed in this study show two complexes in which peptides having a trans-form proline, i.e. succinyl-Ala-trans-Pro-Ala-p-nitroanilide and acetyl-Ala-Ala-trans-Pro-Ala-amidomethylcoumarin, are bound on a K163T mutant of Escherichia coli cyclophilin B, the preprotein of which has a signal sequence [3].

Biological context of PPIB


Anatomical context of PPIB


Associations of PPIB with chemical compounds

  • To identify potential cellular homologues of cyclosporin A that might regulate calcium signalling, we have cloned human genes encoding cyclophilin B-binding-proteins using the yeast two-hybrid system [6].
  • The higher potency of the CypB/CsA complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent protein phosphatase calcineurin is discussed in terms of the structural differences between the two complexes [17].
  • Mutational analysis of CyPB has revealed that W128, which is part of the CsA-binding pocket, is implicated in the binding to the functional type I receptors and that two amino acid clusters located in the N-terminus ensure the binding to GAGs [9].
  • Sequencing of this protein revealed identity of the NH2-terminal amino acids with those of human cyclophilin A. The finding is unexpected since cyclophilin B rather than A is generally regarded as the secreted isoform, the presence of cyclophilin A being confined to the cytoplasm [18].
  • These findings argue in favor of a role for cyclophilin B as a chaperone to proteins destined for the plasma membrane, rather than solely as a proline isomerase functioning within the endoplasmic reticulum [16].

Other interactions of PPIB


Analytical, diagnostic and therapeutic context of PPIB

  • Amplification of the target gene in the duplex NASBA assay was disrupted when this latter was mixed with a large amount of the housekeeping PPIB gene, suggesting that it is preferable for the normalizing gene chosen to have an expression level comparable to the target gene [21].
  • Using surface plasmon resonance spectroscopy, Far Western blot, and pulldown experiments a physical interaction of Vpr with the major host PPIase cyclophilin A (CypA) is now demonstrated [22].
  • Taken together, our results demonstrate that CyPB-binding sites are mainly associated with resting cells of the helper T lymphocyte, and that CyPB might modulate the distribution of CsA through the drug targeting to sensitive cells [23].
  • The polymerase chain reaction (PCR) technique was used to generate a unique probe complementary to the hydrophobic 5' end of the human cyclophilin B gene [24].
  • By site-directed mutagenesis of CyPD that compromises peptidyl-prolyl cis-trans isomerase (PPIase) activity, we demonstrate that the mechanism involved in this protective effect requires PPIase activity [25].
  • Cyclophilin B (CypB) is a potential biomarker for pancreatic cancer. An RNA aptamer (M9-5) was selected by comparing human pancreatic cell secretomes by in vitro aptamer selection technique (SELEX). The aptamer (M9-5) discriminates between the sera of pancreatic cancer patients and healthy volunteers with high sensitivity and specificity. Utilizing chromatographic methods and mass-spectrometric analysis the M9-5 target was identified as CypB. Additionally, by using ELISA it was demonstrated that the CypB level is elevated in the sera of pancreatic cancer patients as compared to the healthy volunteers [26]. Recent work has demonstrated that the M9-5 could discriminate between recombinant human Cyclophilin B expressed in mammalian cells versus bacteria. Using mass-spectrometric analysis, post-translational modifications on Cyclophilin B were discovered that might be responsible for this aptamer selectivity [27].


  1. Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase. Watashi, K., Ishii, N., Hijikata, M., Inoue, D., Murata, T., Miyanari, Y., Shimotohno, K. Mol. Cell (2005) [Pubmed]
  2. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Gitti, R.K., Lee, B.M., Walker, J., Summers, M.F., Yoo, S., Sundquist, W.I. Science (1996) [Pubmed]
  3. Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer. Konno, M., Sano, Y., Okudaira, K., Kawaguchi, Y., Yamagishi-Ohmori, Y., Fushinobu, S., Matsuzawa, H. Eur. J. Biochem. (2004) [Pubmed]
  4. Cyclophilin B escorts the hepatitis C virus RNA polymerase: a viral achilles heel? Heitman, J., Cullen, B.R. Mol. Cell (2005) [Pubmed]
  5. A cyclophilin B gene encodes antigenic epitopes recognized by HLA-A24-restricted and tumor-specific CTLs. Gomi, S., Nakao, M., Niiya, F., Imamura, Y., Kawano, K., Nishizaka, S., Hayashi, A., Sobao, Y., Oizumi, K., Itoh, K. J. Immunol. (1999) [Pubmed]
  6. Calcium signalling in T cells stimulated by a cyclophilin B-binding protein. Bram, R.J., Crabtree, G.R. Nature (1994) [Pubmed]
  7. Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix. Allain, F., Vanpouille, C., Carpentier, M., Slomianny, M.C., Durieux, S., Spik, G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  8. Structural basis for phosphoserine-proline recognition by group IV WW domains. Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T., Noel, J.P. Nat. Struct. Biol. (2000) [Pubmed]
  9. Receptor type I and type II binding regions and the peptidyl-prolyl isomerase site of cyclophilin B are required for enhancement of T-lymphocyte adhesion to fibronectin. Carpentier, M., Allain, F., Slomianny, M.C., Durieux, S., Vanpouille, C., Haendler, B., Spik, G. Biochemistry (2002) [Pubmed]
  10. The role of immunophilins in mutant superoxide dismutase-1linked familial amyotrophic lateral sclerosis. Lee, J.P., Palfrey, H.C., Bindokas, V.P., Ghadge, G.D., Ma, L., Miller, R.J., Roos, R.P. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  11. Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location. Bram, R.J., Hung, D.T., Martin, P.K., Schreiber, S.L., Crabtree, G.R. Mol. Cell. Biol. (1993) [Pubmed]
  12. Two distinct regions of cyclophilin B are involved in the recognition of a functional receptor and of glycosaminoglycans on T lymphocytes. Carpentier, M., Allain, F., Haendler, B., Denys, A., Mariller, C., Benaïssa, M., Spik, G. J. Biol. Chem. (1999) [Pubmed]
  13. Involvement of the N-terminal part of cyclophilin B in the interaction with specific Jurkat T-cell binding sites. Mariller, C., Haendler, B., Allain, F., Denys, A., Spik, G. Biochem. J. (1996) [Pubmed]
  14. In situ detection of cyclosporin A: evidence for nuclear localization of cyclosporine and cyclophilins. Le Hir, M., Su, Q., Weber, L., Woerly, G., Granelli-Piperno, A., Ryffel, B. Lab. Invest. (1995) [Pubmed]
  15. Role of cyclophilins in somatolactogenic action. Rycyzyn, M.A., Clevenger, C.V. Ann. N. Y. Acad. Sci. (2000) [Pubmed]
  16. Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A. Price, E.R., Jin, M., Lim, D., Pati, S., Walsh, C.T., McKeon, F.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  17. X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain. Mikol, V., Kallen, J., Walkinshaw, M.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  18. Presence of cyclophilin A in synovial fluids of patients with rheumatoid arthritis. Billich, A., Winkler, G., Aschauer, H., Rot, A., Peichl, P. J. Exp. Med. (1997) [Pubmed]
  19. Role of cyclophilin B in activation of interferon regulatory factor-3. Obata, Y., Yamamoto, K., Miyazaki, M., Shimotohno, K., Kohno, S., Matsuyama, T. J. Biol. Chem. (2005) [Pubmed]
  20. Light-regulated, tissue-specific immunophilins in a higher plant. Luan, S., Albers, M.W., Schreiber, S.L. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  21. Multiparametric duplex real-time nucleic acid sequence-based amplification assay for mRNA profiling. Verjat, T., Cerrato, E., Jacobs, M., Leissner, P., Mougin, B. BioTechniques (2004) [Pubmed]
  22. Cyclophilin A interacts with HIV-1 Vpr and is required for its functional expression. Zander, K., Sherman, M.P., Tessmer, U., Bruns, K., Wray, V., Prechtel, A.T., Schubert, E., Henklein, P., Luban, J., Neidleman, J., Greene, W.C., Schubert, U. J. Biol. Chem. (2003) [Pubmed]
  23. Distribution of cyclophilin B-binding sites in the subsets of human peripheral blood lymphocytes. Denys, A., Allain, F., Foxwell, B., Spik, G. Immunology (1997) [Pubmed]
  24. Somatic cell mapping of the human cyclophilin B gene (PPIB) to chromosome 15. Peddada, L.B., McPherson, J.D., Law, R., Wasmuth, J.J., Youderian, P., Deans, R.J. Cytogenet. Cell Genet. (1992) [Pubmed]
  25. Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. Lin, D.T., Lechleiter, J.D. J. Biol. Chem. (2002) [Pubmed]
  26. Comparing human pancreatic cell secretomes by in vitro aptamer selection identifies cyclophilin B as a candidate pancreatic cancer biomarker. Ray, P., Rialon-Guevara, K.L., Veras, E., Sullenger, B.A., White, R.R. J. Clin. Invest. (2012) [Pubmed]
  27. Further characterization of the target of a potential aptamer biomarker for pancreatic cancer: cyclophilin B and its posttranslational modifications. Ray, P., Sullenger, B.A., White, R.R. Nucleic. Acid. Ther. (2013) [Pubmed]
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