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Order Picornavirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
McClenahan et al. (2010) engineered the sequences encoding the major VP1 and minor VP2 capsid proteins from two marine vesivirus isolates, namely Steller sea lion viruses V810 and V1415, for expression of the VLPs in the baculovirus expression system. The resulting VLPs were morphologically similar to native vesivirus virions. The purified VLPs were probed in immunoblots with pooled antisera specific for nine SMSV types, and a predominant protein of ~60 kDa was detected. The VLPs were used as antigens to develop an ELISA for the detection of serum antibodies to marine vesiviruses in animals from two free-ranging populations of Steller sea lion in Alaska (McClenahan et al. 2010).
Human Noroviruses
Published in Dongyou Liu, Handbook of Foodborne Diseases, 2018
G. Sanchez, W. Randazzo, D.H. D'Souza
Noroviruses are a group of nonenveloped viruses, classified under the Norovirus genus within the Caliciviridae family.4 Among this family, Norovirus together with Sapovirus are human pathogens causing gastroenteritis, while the Lagovirus, Vesivirus, and Nebovirus genera are not known to be pathogenic to humans.5,6
Safety of recombinant coagulation factors in treating hemophilia
Published in Expert Opinion on Drug Safety, 2019
Massimo Morfini, Carlo Antonio Paolo Rapisarda
The viral safety of recombinant factor VIII or IX concentrates has never been questioned, except for the first generation FVIII concentrates. The use of human albumin, produced from a large pool of donors, as a stabilizer in the final formulation of these concentrates was most likely responsible for the presence of TTV and Parvovirus B19 [1]. It is very well known that these viruses are resistant to virucidal methods, including solvent/detergent and heat treatment, and therefore they can contaminate human albumin even if it was subjected to pasteurization [2]. The viral contamination of the cell lines producing the recombinant drugs is theoretically possible, as it has been demonstrated by the detection of Vesivirus in the cell lines producing Cerezyme [3]. For these reasons, also the recombinant concentrates are subjected to inactivation or removal by nanofiltration of the hypothetical animal viruses contaminating the production cell lines. The transmission of animal viruses in patients treated with recombinant concentrates has never been detected. The problem of viral safety of clotting factor concentrates was the main topic of a review published in 2002 [4]. Nowadays this problem no longer worries treaters and patients with hemophilia because all rFVIII and rFIX concentrates are submitted to two or three viral inactivation steps (Tables 1 and 2).
Pharmacological treatment of pediatric Gaucher disease
Published in Expert Review of Clinical Pharmacology, 2018
Punita Gupta, Gregory Pastores
Alglucerase was subsequently replaced by human recombinant imiglucerase (CerezymeTM, Sanofi/Genzyme), generated using Chinese hamster ovary (CHO) cells, in the mid-1990s; this preparation continues to be the most widely used ERT in clinics across the world. In 2009, a vesivirus 2117 infection of the bioreactors in which imiglucerase was manufactured led to a global shortage of imiglucerase and expedited the approval of two ‘new’ enzymes: gene-activated human recombinant velaglucerase alfa (VPRIVTM, Shire) derived from a human fibrosarcoma cell line and plant-cell-derived human recombinant taliglucerase alfa (ElelysoTM Protalix/Pfizer). All three recombinant enzyme formulations have exposed mannosyl-residues, although the process involved in achieving this is unique for each product. These three ERTs are not biosimilar products, and there appears to be no major difference in their safety profile [45–48].