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At least 811 records · Page 45Linked to original sources
PubMed2006

Evaluation of viral clearance in the production of HPV-16 L1 virus-like particles purified from insect cell cultures.

Biopharmaceutical products produced from cell cultures have a potential for viral contamination from cell sources or from adventitious introduction during production. The objective of this study was to assess viral clearance in the production of insect cell-derived recombinant human papillomavirus (HPV)-16 type L1 virus-like particles (VLPs). We selected Japanese encephalitis virus (JEV), bovine viral diarrhea virus (BVDV), and minute virus of mice (MVM) as relevant viruses to achieve the aim of this study. A downstream process for the production of purified HPV-16 L1 VLPs consisted of detergent lysis of harvested cells, sonication, sucrose cushion centrifugation, and cesium chloride (CsCl) equilibrium density centrifugation. The capacity of each purification/treatment step to clear viruses was expressed as reduction factor by measuring the difference in log virus infectivity of sample pools before and after each process. As a result, detergent treatment (0.5% v/v, Nonidet P-40/phosphate-buffered saline) was effective for inactivating enveloped viruses such as JEV and BVDV, but no significant reduction (< 1.0 log(10)) was observed in the non-enveloped MVM. The CsCl equilibrium density centrifugation was fairly effective for separating all three relevant adventitious viruses with different CsCl buoyant density from that of HPV-16 L1 VLPs (JEV, BVDV, and MVM = 4.30, 3.10, > or = 4.40 log(10) reductions). Given the study conditions we used, overall cumulative reduction factors for clearance of JEV, BVDV, and MVM were > or = 10.50, > or = 9.20, and > or = 6.40 log(10) in 150 ml of starting cell cultures, respectively.

Animals↗
PubMed1977

Characterization of N-polyhedrin of two baculovirus strains pathogenic for Orgyia pseudotsugata.

N-polyhedrin of inclusion bodies of two nucleopolyhedrosis viruses of Orgyia pseudotsugata was characterized. Alkali-dissolved N-polyhedrin from both virus strains was of similar size and consisted of 12S molecule of 209 000 daltons. Eight subunits of approximately 26 000 daltons were found to form the 12S molecules. N-polyhedrin from both viruses showed two main antigens by immunodiffusion. The subunits appear to possess one antigen and, upon formation of the 12S molecule, a new antigen is created. Both the subunit and 12S antigens from the two virus strains were shown to be antigenically related. The 12S molecule of both viruses also appears to possess a minor antigen unique to each virus.

Amino Acids↗
PubMed1988

Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector.

Patatin is a family of glycoproteins that accounts for 30-40% of the total soluble protein in potato (Solanum tuberosum) tubers. This protein has been reported not only to serve as a storage protein, but also to exhibit enzymic activity. By using a baculovirus system to express protein from the patatin cDNA clone pGM01, it was unambiguously shown that the patatin coded by this DNA has lipid acyl hydrolase and acyltransferase activities. The enzyme is active with phospholipids, monoacylglycerols and p-nitrophenyl esters, moderately active with galactolipids, but is apparently inactive with di- and tri-acylglycerols.

Acyltransferases↗