Caruso A, Viani E, Tiberio L, Pollara P, Monti E, Bonfanti C, Gao J, Landolfo S, Balsari A, Turano A
Institute of Microbiology, University of Brescia, Italy.
J Interferon Res. 1992 Feb;12(1):49-54. doi: 10.1089/jir.1992.12.49.
To study the domain(s) responsible for the different biological activities of human interferon-gamma (HuIFN-gamma), rabbits were immunized with peptides corresponding to the five most hydrophilic amino acid sequences of the lymphokine. The resulting antisera were able to recognize both the immunizing peptide and the native protein. Antibodies to the carboxy-terminal region (amino acids 125-137) of HuIFN-gamma were able to interfere with the immunomodulating, antiviral, and antiproliferative activities of the lymphokine. Inhibition of the antiproliferative and antiviral activity was also observed using antibodies raised against the amino-terminal region (amino acids 4-16) and amino acids 80-95, respectively, but to a lesser extent than that observed with antibodies to the carboxyl terminus. The capability of these antibody preparations to partially interfere with only one of the lymphokine's biological activities might be explained by a mechanism of steric hindrance. The use of polyclonal antibodies allowed us to limit the presence of epitopes responsible for recombinant (r)HuIFN-gamma biological activities to the carboxy-terminal region.
为研究负责人类干扰素-γ（HuIFN-γ）不同生物学活性的结构域，用与该淋巴因子五个最具亲水性氨基酸序列相对应的肽免疫兔子。所得抗血清能够识别免疫肽和天然蛋白。针对HuIFN-γ羧基末端区域（氨基酸125 - 137）的抗体能够干扰该淋巴因子的免疫调节、抗病毒和抗增殖活性。分别使用针对氨基末端区域（氨基酸4 - 16）和氨基酸80 - 95产生的抗体也观察到了抗增殖和抗病毒活性的抑制，但程度低于针对羧基末端的抗体。这些抗体制剂仅部分干扰淋巴因子一种生物学活性的能力可能由空间位阻机制来解释。使用多克隆抗体使我们能够将负责重组（r）HuIFN-γ生物学活性的表位限制在羧基末端区域。
