Physicochemical and Structural Properties of Interleukin-10

  • Paul P. Trotta
  • William T. Windsor
Part of the Molecular Biology Intelligence Unit book series (MBIU)


Interleukin-10 (IL-10) was first described as a murine factor produced by T helper 2 (Th 2) clones that could inhibit the production of various cytokines from Th 1 clones and hence was originally referred to as cytokine synthesis inhibition factor.1 This novel activity was the basis for the isolation of cDNA clones coding for both murine IL-102 (mIL-10) and human IL-103 (hIL-10). Characterization of recombinant mIL-10 (rmIL-10) and recombinant hIL-10 (rhIL-10) has indicated pleiotropic stimulatory and suppressive activities on both lymphoid and myeloid cells (reviewed by Rennick et al4 and Moore et al5). Interestingly, both mIL-10 and hIL-10 exhibit a high percentage of nucleotide and amino acid sequence homology to an open reading frame (BCRF1) in the Epstein-Barr virus genome.2 The product of the BCRF1 gene has been termed viral IL-10 (vIL-10) since BCRF1 apparently represents a virally transduced hIL-10 gene that expresses many of the biological properties of hIL-10.6


Apparent Molecular Weight Alpha Helix Beta Sheet Intramolecular Disulfide Bond Beta Turn 
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© Springer-Verlag Berlin Heidelberg 1995

Authors and Affiliations

  • Paul P. Trotta
  • William T. Windsor

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