Author/Editor		van Holten, R; Autenrieth, S; Boose, JA; Bird, R; Hsieh, WT; Dolan, S; Ciavarella, D
Title		Removal of prion challenge from a human anti-D immunoglobulin preparation using a viresolve 180TM size exclusion filter
Type		članek
Source		In: Novak-Antolič Ž, editor. Prezgodnji porod in nedonošenček. Zbornik prispevkov 8. Novakovi dnevi z mednarodno udeležbo; 2001 maj 31-jun 2; Maribor. Ljubljana: Slovensko zdravniško društvo, Združenje za perinatalno medicino,
Publication year		2001
Volume		str. 24-6
Language		eng
Abstract		Background. There exists a theoretical risk of transmission of Transmissible Spongiform Encephalopathies (TSE) by blood. A variety of studies have been performed to assess the potential removal of the TSE agent, abnormal prion proteins designated PrPsc, from plasmaderived medicinal products. We studied the ability of the ViresolveTM 180 Ultra-Filter, a validated viral clearance step used in the manufacture of RhoGAM HYman anti-D immunoglobulin, to remove prion protein during ultrafiltration. Materials and Methods. Hamster 263k scrapie brain homogenate (SBH) was spiked into RhoGAM at 1:300 and 1:1000 dilution. Prior to spiking, the SBH was lysolecithin-treated sonicated and pre-filtered through Durapore (0.45/0.22/0.1 micron) filters to insure a worst case scenario filter challenge. The SBH was observed to be completely translucent after this preparatory treatment. Process parameters were monitored throughout the ultrafiltration to insure that the spiked material did not compromise the ultra-membrane flux. Removal of PrPsc material was determined by use of a sensitive Western blot assay. Results. The filtration of RhoGAM containing PrP sc scrapie material was more difficult to perform than normal cellular isoform PrP c containing material. Even during tangeltial flow filtration, the fibrillary prion protein (6 nm diameter and up to 1000 nm in length) caused the IgG not to pass as readily through the filter. Western blot results indicate a removal of greater than 2.7 log of SBH prion material from RhoGAM. Conclusion. The Viresolve 180 Ultra-Filter removed a significant amount of spiked SBH prion protein from RhoGAM. The composition, physical condition and amount of prion material introduced has a significant effect on the ease of filtartion and the log removal values obtained
Descriptors		ENCEPHALOPATHY, BOVINE SPONGIFORM PRIONS HAMSTERS ULTRAFILTRATION BRAIN BLOTTING, WESTERN RHO(D) IMMUNE GLOBULIN