Zhirnov O P, Golyando P B, Ovcharenko A V
D.I. Ivanovsky Virology Institute, Moscow, Russia.
Arch Virol. 1994;135(1-2):209-16. doi: 10.1007/BF01309780.
Chicken embryo proteinases, one of which is a blood clotting factor Xa-like proteinase, are known to effectively cleave the haemagglutinin (HA) of Influenza B viruses to permit their replication in chicken embryonated eggs. Here we show that injection of the serine proteinase inhibitor, aprotinin, into the allantoic cavity of eggs infected with Influenza B/Hong Kong/73 and B/Lee/40 viruses suppresses the viral HA cleavage and reduces the virus proteolytic activation and replication. Effective inhibition dose was determined as approximately 10.0 micrograms of aprotinin per embryo that corresponds to 0.1 microM concentration. However, heparin, which is known to be a direct inhibitor of the Factor Xa, was not able to suppress Influenza B virus hemagglutinin cleavage and replication in chicken embryo system. These data shed light on the pattern of proteinases involved in the Influenza B virus proteolytic activation and indicate that aprotinin possesses antiviral potential against Influenza B viruses.
鸡胚蛋白酶（其中一种是类似凝血因子Xa的蛋白酶）已知能有效切割乙型流感病毒的血凝素（HA），从而使其能在鸡胚中复制。在此我们表明，将丝氨酸蛋白酶抑制剂抑肽酶注射到感染乙型流感病毒/香港/73株和B/李/40株病毒的鸡蛋尿囊腔中，可抑制病毒HA的切割，并减少病毒的蛋白水解激活和复制。有效抑制剂量确定为每个胚胎约10.0微克抑肽酶，相当于0.1微摩尔浓度。然而，已知作为因子Xa直接抑制剂的肝素，在鸡胚系统中无法抑制乙型流感病毒血凝素的切割和复制。这些数据揭示了参与乙型流感病毒蛋白水解激活的蛋白酶模式，并表明抑肽酶具有抗乙型流感病毒的潜力。
