<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kurz M</submitter><funding>Austrian Science Fund FWF</funding><funding>Austrian Science fund</funding><pagination>48-55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3437442</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>168(1-2)</volume><pubmed_abstract>The replication of tick-borne encephalitis virus (TBEV), like that of all flaviviruses, is absolutely dependent on proteolytic processing. Production of the mature proteins C and prM from their common precursor requires the activity of the viral NS2B/3 protease (NS2B/3(pro)) at the C-terminus of protein C and the host signal peptidase I (SPaseI) at the N-terminus of protein prM. Recently, we have shown in cell culture that the cleavage of protein C and the subsequent production of TBEV particles can be made dependent on the activity of the foot-and-mouth disease virus 3C protease, but not on the activity of the HIV-1 protease (HIV1(pro)) (Schrauf et al., 2012). To investigate this failure, we developed an in vitro cleavage assay to assess the two cleavage reactions performed on the C-prM p</pubmed_abstract><journal>Virus research</journal><pubmed_title>NS2B/3 proteolysis at the C-prM junction of the tick-borne encephalitis virus polyprotein is highly membrane dependent.</pubmed_title><pmcid>PMC3437442</pmcid><funding_grant_id>P 19528</funding_grant_id><funding_grant_id>FWF-P19528</funding_grant_id><pubmed_authors>Zhu J</pubmed_authors><pubmed_authors>Stefan N</pubmed_authors><pubmed_authors>Skern T</pubmed_authors><pubmed_authors>Kurz M</pubmed_authors></additional><is_claimable>false</is_claimable><name>NS2B/3 proteolysis at the C-prM junction of the tick-borne encephalitis virus polyprotein is highly membrane dependent.</name><description>The replication of tick-borne encephalitis virus (TBEV), like that of all flaviviruses, is absolutely dependent on proteolytic processing. Production of the mature proteins C and prM from their common precursor requires the activity of the viral NS2B/3 protease (NS2B/3(pro)) at the C-terminus of protein C and the host signal peptidase I (SPaseI) at the N-terminus of protein prM. Recently, we have shown in cell culture that the cleavage of protein C and the subsequent production of TBEV particles can be made dependent on the activity of the foot-and-mouth disease virus 3C protease, but not on the activity of the HIV-1 protease (HIV1(pro)) (Schrauf et al., 2012). To investigate this failure, we developed an in vitro cleavage assay to assess the two cleavage reactions performed on the C-prM p</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Sep</publication><modification>2026-04-29T11:43:40.613Z</modification><creation>2019-03-27T00:57:43Z</creation></dates><accession>S-EPMC3437442</accession><cross_references><pubmed>22727684</pubmed><doi>10.1016/j.virusres.2012.06.012</doi></cross_references></HashMap>