Arginine facilitates inactivation of enveloped viruses.
Virus inactivation is a key step for the purification of pharmaceutical proteins derived from recombinant mammalian expression systems and conventionally done using low pH-treatment, which is often harmful to the proteins to be purified. This is particularly true for antibodies, because immunoglobulin proteins undergo conformational changes at acidic pH. We have been developing mild elution solvents using arginine for Protein-A chromatography to minimize the low pH-induced damages on the antibodies. Here we have tested the aqueous solutions containing arginine or butyroyl-arginine at or above pH 4.0 for their effects on virus inactivation, since these solvents are effective above pH 4.0 in elution of bound antibodies from Protein-A columns. When the virus was incubated on ice, 0.1 M sodium citrate was totally ineffective above pH 4.0, but aqueous solutions containing arginine above 0.35 M or butyroyl-arginine above 0.28 M showed extensive virus killing at or even above pH 4.0.
Yamasaki
Hisashi
H
Division of Virology, Department of Cellular and Molecular Medicine, Wakayama Medical University Graduate School of Medicine, Wakayama 641-8509, Japan.
Tsujimoto
Kazuko
K
Koyama
A Hajime
AH
Ejima
Daisuke
D
Arakawa
Tsutomu
T
D000818:Animals; D001120:Arginine / Q000494:pharmacology*; D002460:Cell Line; D002522:Chlorocebus aethiops; D004285:Dogs; D006863:Hydrogen-Ion Concentration; D053122:Influenza A Virus, H3N2 Subtype / Q000187:drug effects*; D038301:Virus Inactivation / Q000187:drug effects*
D001120:Arginine