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Mutations within a proposed packaging signal did not significantly affect relative packaging efficiency. The insertion of various fragments derived from the RUBV genome into Sindbis virus replicons revealed that there are several regions within the RUBV genome capable of enhancing encapsidation of heterologous replicon RNAs. Secondly, the <jats:italic>trans<\/jats:italic>-encapsidation system was used to analyse the effect of alterations within the capsid protein (CP) on release of VRPs and subsequent initiation of replication in newly infected cells. Deletion of the N-terminal eight amino acids of the CP reduced VRP titre significantly, which could be partially complemented by native CP provided <jats:italic>in trans<\/jats:italic>, indicating that this mutation affected an entry or post-entry event in the replication cycle. To test this hypothesis, the <jats:italic>trans<\/jats:italic>-encapsidation system was used to demonstrate the rescue of a lethal deletion within P150, one of the virus replicase proteins, by CP contained within the virus particle. This novel finding substantiated the functional role of CP in early post-entry replication.<\/jats:p>","DOI":"10.1099\/vir.0.038984-0","type":"journal-article","created":{"date-parts":[[2011,11,24]],"date-time":"2011-11-24T06:01:05Z","timestamp":1322114465000},"page":"516-525","source":"Crossref","is-referenced-by-count":5,"title":["Rubella virus-like replicon particles: analysis of encapsidation determinants and non-structural roles of capsid protein in early post-entry replication"],"prefix":"10.1099","volume":"93","author":[{"given":"Claudia","family":"Claus","sequence":"first","affiliation":[{"name":"Institute of Virology, University of Leipzig, Leipzig, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wen-Pin","family":"Tzeng","sequence":"additional","affiliation":[{"name":"Department of Biology, Georgia State University, Atlanta, GA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"U. 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