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Amino acid substitutions which alter the antiviral activity of human interferon-alpha 1 on mouse cells
M W Beilharz1, M J Tymms, P J Chambers
1Centre for Molecular Biology and Medicine, Monash University, Clayton, Victoria, Australia.
Human interferon-alpha 1 (IFN-alpha 1) is one of only three human (Hu) IFN-alphas having significant antiviral activity on mouse cells. Specific amino acid substitutions in HuIFN-alpha 1 in the region from amino acids 121 to 136 indicate that this region is critical to the determination of mouse and human cell antiviral activities. Bovine cell activities are relatively unaffected by changes in this region. In particular we have identified the arginine residue at position 125 of human IFN-alpha 1 as a major mediator of the molecules antiviral activity on mouse cells. Various substitutions in the carboxy-terminal region of human IFN-alpha 1 are also evaluated and discussed in the context of recently published data.
Human interferon-alpha 1 (IFN-alpha 1) is one of only three human (Hu) IFN-alphas having significant antiviral activity on mouse cells. Specific amino acid substitutions in HuIFN-alpha 1 in the region from amino acids 121 to 136 indicate that this region is critical to the determination of mouse and human cell antiviral activities. Bovine cell activities are relatively unaffected by changes in this region. In particular we have identified the arginine residue at position 125 of human IFN-alpha 1 as a major mediator of the molecules antiviral activity on mouse cells. Various substitutions in the carboxy-terminal region of human IFN-alpha 1 are also evaluated and discussed in the context of recently published data.