TY - JOUR
T1 - Echinhibin-1 - an inhibitor of Sendai virus isolated from the venom of the snake Echis coloratus
AU - Borkow, Gadi
AU - Ovadia, Michael
PY - 1994/2
Y1 - 1994/2
N2 - The snake venom of Echis coloratus was found to abolish the hemagglutinating activity, hemolytic activity and in vivo infectivity of Sendai virus. The active factor (Echinhibin-1) was purified by gel filtration on Sephadex G-50, followed by chromatography on DEAE-Sepharose and CM-Sepharose. Echinhibin-1 is a protease with a molecular weight of about 25 kDa, an isoelectric point of 7 and is stained by PAS, indicating that it is a glycoprotein. It showed a strong azocollase activity that was stable up to 68°C and at pH values of 4.5-10.5. Ten μg/ml were sufficient to abolish the hemolytic effect of the virus on human erythocytes when inculbation was at 37°C for 2 h, while 20 μg/ml abolished the hemagglutinating activity. Addition of Echinhibin-1 after the adsorption of Sendai virions onto washed erythrocytes at 4 °C did not inhibit the subsequently hemolytic activity at 37 °C, indicating that Echinhibin-1 interferes with virus adsorption to the cells. Of various protease inhibitors, only Na2 EDTA and o-phenanthroline inhibited the antiviral activity of the purified factor, indicating that it is a metalloproteinase. In vivo, mice inoculated intranasally with the virus pretreated with Echinhibin-1 developed well and gained weight, whereas untreated virus-infected mice lost weight and died within 1 week. Intravenous administrations of the purified factor up to 80 μg/mouse produced no signs of toxicity and subcutaneous injections caused no hemorrhagic activity, while the whole venom is very hemorrhagic with an LD50 of 250 μg/kg for mice.
AB - The snake venom of Echis coloratus was found to abolish the hemagglutinating activity, hemolytic activity and in vivo infectivity of Sendai virus. The active factor (Echinhibin-1) was purified by gel filtration on Sephadex G-50, followed by chromatography on DEAE-Sepharose and CM-Sepharose. Echinhibin-1 is a protease with a molecular weight of about 25 kDa, an isoelectric point of 7 and is stained by PAS, indicating that it is a glycoprotein. It showed a strong azocollase activity that was stable up to 68°C and at pH values of 4.5-10.5. Ten μg/ml were sufficient to abolish the hemolytic effect of the virus on human erythocytes when inculbation was at 37°C for 2 h, while 20 μg/ml abolished the hemagglutinating activity. Addition of Echinhibin-1 after the adsorption of Sendai virions onto washed erythrocytes at 4 °C did not inhibit the subsequently hemolytic activity at 37 °C, indicating that Echinhibin-1 interferes with virus adsorption to the cells. Of various protease inhibitors, only Na2 EDTA and o-phenanthroline inhibited the antiviral activity of the purified factor, indicating that it is a metalloproteinase. In vivo, mice inoculated intranasally with the virus pretreated with Echinhibin-1 developed well and gained weight, whereas untreated virus-infected mice lost weight and died within 1 week. Intravenous administrations of the purified factor up to 80 μg/mouse produced no signs of toxicity and subcutaneous injections caused no hemorrhagic activity, while the whole venom is very hemorrhagic with an LD50 of 250 μg/kg for mice.
KW - Antiviral protease
KW - Echinhibin-1
KW - Sendai virus
KW - Snake venom
UR - http://www.scopus.com/inward/record.url?scp=0028158046&partnerID=8YFLogxK
U2 - 10.1016/0166-3542(94)90042-6
DO - 10.1016/0166-3542(94)90042-6
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AN - SCOPUS:0028158046
SN - 0166-3542
VL - 23
SP - 161
EP - 176
JO - Antiviral Research
JF - Antiviral Research
IS - 2
ER -