TY - JOUR
T1 - Further characterization of a broad-spectrum antiviral substance in human serum
AU - Singh, I. P.
AU - Coppenhaver, D. H.
AU - Chopra, A. K.
AU - Baron, S.
PY - 1992
Y1 - 1992
N2 - A broadly active antiviral glycoprotein (UTIβ) occurs naturally in human sera at an average antiviral titer of 50U/ml. This inhibitor is active against all virus families tested to date, including representative poxviruses, herpesviruses, enteroviruses, paramyxoviruses, alphaviruses, flaviviruses, bunyaviruses, and rhabdoviruses. It is a glycoprotein of approximately 60,000±10,000Da, which is stable at pH 2 to 10 and at 80°C for up to 10 min. Mild oxidation with NaIO4 and treatment with glycosidases inactivates the material. Proteolytic degradation of the inhibitor molecule releases small active components of <1000Da, which retain antiviral activity. This activity of the small components has increased heat stability (120°C for 15 min) and is inactivated by glycosidases. The antiviral activity thus appears to reside mainly in the oligosaccharide moiety of the glycoprotein. The inhibitor does not neutralize virions, but prevents attachment of most viruses to cells. These properties occur also in highly purified preparations. These findings indicate that human serum contains significant concentrations of a broadly active antiviral glycoprotein, which is distinct from interferon and other antiviral substances naturally found in human body fluids and tissues.
AB - A broadly active antiviral glycoprotein (UTIβ) occurs naturally in human sera at an average antiviral titer of 50U/ml. This inhibitor is active against all virus families tested to date, including representative poxviruses, herpesviruses, enteroviruses, paramyxoviruses, alphaviruses, flaviviruses, bunyaviruses, and rhabdoviruses. It is a glycoprotein of approximately 60,000±10,000Da, which is stable at pH 2 to 10 and at 80°C for up to 10 min. Mild oxidation with NaIO4 and treatment with glycosidases inactivates the material. Proteolytic degradation of the inhibitor molecule releases small active components of <1000Da, which retain antiviral activity. This activity of the small components has increased heat stability (120°C for 15 min) and is inactivated by glycosidases. The antiviral activity thus appears to reside mainly in the oligosaccharide moiety of the glycoprotein. The inhibitor does not neutralize virions, but prevents attachment of most viruses to cells. These properties occur also in highly purified preparations. These findings indicate that human serum contains significant concentrations of a broadly active antiviral glycoprotein, which is distinct from interferon and other antiviral substances naturally found in human body fluids and tissues.
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U2 - 10.1089/vim.1992.5.293
DO - 10.1089/vim.1992.5.293
M3 - Article
C2 - 1335259
AN - SCOPUS:0027093570
SN - 0882-8245
VL - 5
SP - 293
EP - 303
JO - Viral Immunology
JF - Viral Immunology
IS - 4
ER -