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The cysteines in position 1 and 86 of rat interferon‐α 1 are indispensable for antiviral activity
Author(s) -
Spanjaard Remco A.,
van Himbergen John A.J.,
van Duin Jan
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80621-0
Subject(s) - alpha interferon , alpha (finance) , interferon , biology , subspecies , microbiology and biotechnology , biochemistry , disulfide bond , chemistry , virology , medicine , paleontology , construct validity , nursing , patient satisfaction
The human, bovine, murine and rat interferon (IFN)‐α families contain 4 conserved cysteines located at positions 1, 29, 99 and 139 that are involved in disulfide bridges. Rat and murine IFN‐α subspecies carry a fifth Cys (Cys‐86) which is not conserved in bovine and human IFN‐α subspecies except for human IFN‐α 1 . Changing Cys‐86 in rat IFN‐α 1 , into Ser or Tyr virtually abolished antiviral activity. As shown by others, the substitution of Cys‐86 to Ser in human IFN‐α 1 had no pronounced effect on activity. This suggests that in contrast to human and bovine IFN‐α, Cys‐86 in rodent IFN‐α plays a crucial role in receptor binding. Changing Cys‐1 to Gly in rat IFN‐α 1 also destroyed activity, in agreement with results obtained in the human IFN‐α 1 system.