Putative N-terminal sequence of murine soluble immune response suppressor (SIRS): significant homology with short neurotoxin 1.

Autor: Webb, D. R., Mensi, N., Freire-Moar, J., Schnaper, H. W., Lewis, R. V., Semenuk, G., Devens, B. H., Koontz, A., Danho, W., Pan, Y.-C., Wesselschmidt, R., Aune, T. M., Pierce, C. W.
Zdroj: International Immunology; Aug1990, Vol. 2 Issue 8, p765-774, 10p
Abstrakt: Soluble immune response suppressor (SIRS) is a low-molecular-weight protein (˜10,000 daltons) produced by mitogen- or interferon-activated T lymphocytes that can block development of humoral or cell-mediated immune responses or . As previously reported, murine SIRS is heterogeneous, eluting in two broad peaks on high performance reverse phase chromatography as well as displaying several broad isoelectric point forms. A putative N-terminal 21 amino acid sequence has been obtained for one of the less hydrophobic isoforms, SIRS-α7. The sequence of SIRS-α7 is unique in mammals but shows a remarkable homology to the family of short neurotoxins (short neurotoxin I) found in sea snake, adder, and cobra species. A degenerate oligonucleotide probe based on the protein sequence was synthesized and was shown to hybridize to SIRS messenger RNA as measured by SIRS synthesis in a rabbit reticulocyte lysate system. A synthetic polypeptide based on the 21-residue sequence was also prepared and coupled to thyroglobulin or keyhole limpet hemocyanin. These were used to prepare rabbit antisera that neutralize SIRS bioactivity and precipitate authentic SIRS. [ABSTRACT FROM PUBLISHER]
Databáze: Complementary Index