Mechanism of interferon action: Simian virus 40-specific early polypeptides synthesized in untreated and interferon-treated monkey kidney cells

Autor: Kingsman, Susan M., Smith, Mark D., Samuel, Charles E.
Zdroj: Proceedings of the National Academy of Sciences of the United States of America; May 1980, Vol. 77 Issue: 5 p2419-2423, 5p
Abstrakt: The effect of interferon treatment on proteins synthesized in simian virus 40 (SV40)-infected cells in the presence of cytosine arabinoside was investigated. The following results were obtained: (i) In addition to previously described large tumor (T) antigen (94 kilodaltons) and small tumor (t) antigen (19 kilodaltons), a 62-kilodalton polypeptide was immunoprecipitated by SV40 anti-T antiserum from extracts of infected CV-1 and BSC-1 monkey kidney cells and transformed SV3T3 mouse cells. The 94-, 62-, and 19-kilodalton polypeptides were not precipitated with normal serum from extracts of infected cells, and they were not present in extracts of uninfected cells. (ii) The de novosynthesis of the 94-, 62-, and 19-kilodalton tumor antigens was inhibited in CV-1 and BSC-1 cells treated with interferon before infection; total cellular protein synthesis was not significantly affected by interferon treatment. The relative interferon sensitivity of the three polypeptides in lytically infected monkey cells was comparable; by contrast, interferon did not affect their synthesis in transformed mouse cells. (iii) The 62-kilodalton polypeptide was detected in monkey cells infected with the following strains of SV40: tsA30 at both 33°C and 41°C; wt 708, the parent of tsA30; dI 884; and wt 830, the parent of dI 884. The amount of the 62-kilodalton species relative to T antigen was significantly greater in tsA30-infected cells as compared to cells infected with other SV40 strains. (iv) T, t, and 62-kilodalton polypeptides were readily labeled with [35S]methionine during a 10-min pulse; in a subsequent chase, the 35S-labeled 94-kilodalton T antigen was apparently converted to 89- and 84-kilodalton polypeptides but not to either the 62-kilodalton polypeptide species or t antigen. (v) Partial peptide maps suggest that the 62-kilodalton polypeptide and T antigen are closely related. (vi) In addition to the above described 62-kilodalton polypeptide, a 54-kilodalton polypeptide was also detected. However, the 54-kilodalton species appears to be of cellular origin because it was immunoprecipitated with both normal and anti-T antiserum from uninfected and lytically infected cells and from virally transformed cells.
Databáze: Supplemental Index