Isolation and characterization of full-length recombinant cattle PrPC protein

Институт вирусологии им. Д.И. Ивановского ФГБУ «Национальный исследовательский центр эпидемиологии и микробиологии имени почётного академика Н.Ф. Гамалеи» Минздрава России, 123098, Москва, Россия В обзоре представлено современное состояние проблемы прионов и прионных болезней с акцентом на эпидемическую и эпизоотическую опасность возбудителей, вызывающих смертельные нейродегенеративные болезни человека и животных. Описаны результаты молекулярно-генетических исследований конверсии нормальных молекул прионного белка (PrP c) в их инфекционные формы (PrP d), устойчивость последних к физическим методам дезинфекции, особенно к высоким температурам, а также их способность преодолевать межвидовые барьеры, увеличивая при этом вирулентность. Подчёркнуты необычно продолжительный инкубационный период, возможность заражения не только алиментарным путём,при употреблении в пищу даже термически обработанного мяса заражённых животных, но и вследствие хирургических вмешательств, особенно нейрохирургических и офтальмологических, а также в результате использования иммунобиологических препаратов. Отсутствие средств лечения прионных болезней обосновывает крайнюю необходимость разработки отечественных высокочувствительных тест-систем, способных эффективно обнаруживать инфекционный прионный белок прижизненно, на доклинической стадии заболевания. Кратко описаны новейшие методы автоматической белковой амплификации и идентификации прионных белков как наиболее перспективные направления исследований в области диагностики прионных болезней.

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Problems of ante mortem diagnostics of prion diseases

Kalnov

Verkhovsky

Цибезов

et al. 2021

Voprosy virusologii

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The review presents the state-of-the-art on the problem of diagnosis of prion diseases (PD) in humans and animals with a brief description of their etiology and pathogenesis. We pointed out that understanding the nature of the etio logical agent of PD determined their zoonotic potential and led to the development of highly specific immunological diagnostic methods aimed at identifying the infectious isoform of prion protein (PrPd) as the only marker of the disease. In this regard, we briefly summarize the results of studies, including our own, concerning the conversion of normal prion protein molecules (PrPc) to PrPd, the production of monoclonal antibodies and their application as immunodiagnostic reagents for the post-mortem detection of PrPd in various formats of immunoassay. We also emphasize the issues related to the development of methods for ante mortem diagnostics of PD. In this regard, a method for amplifying amino acid sequences using quacking-induced conversion of PrPc to PrPd in real time (RTQuIC) described in details. The results of recent studies on the assessment of the sensitivity, specificity and reproducibility of this method, carried out in various laboratories around the world, are presented. The data obtained indicate that RT-QuIC is currently the most promising laboratory assay for detecting PrPd in biological material at the preclinical stage of the disease. The significant contribution of US scientists to the introduction of this method into clinical practice on the model of diagnosis of chronic wasting disease of wild Cervidae (CWD) is noted. The possible further spread of CWD in the population of moose and deer in the territories bordering with Russia, as well as the established fact of alimentary transmission of CWD to macaques, indicate the threat of the appearance of PD in our country. In conclusion, the importance of developing new hypersensitive and/or selective components of known methods for PrPd identification from the point of view of assessing the risks of creating artificial infectious prion proteins in vivo or in vitro, primarily new pathogenic isoforms (“strains”) and synthetic prions, was outlined.

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Isolation and characterization of full-length recombinant cattle PrPC protein

Cited by 3 publications

References 10 publications

Fibrillization of recombinant bovine prion protein (rec-PrP) in vitro

Fibrillization of recombinant bovine prion protein (rec-PrP) in vitro

Prion diseases and the biosecurity problems

Problems of ante mortem diagnostics of prion diseases

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