1. The C-terminal helical domain of dengue virus precursor membrane protein is involved in virus assembly and entry
- Author
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Hsieh, Szu-Chia, Zou, Gang, Tsai, Wen-Yang, Qing, Min, Chang, Gwong-Jen, Shi, Pei-Yong, and Wang, Wei-Kung
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DENGUE viruses , *MEMBRANE proteins , *VIRAL replication , *GENETIC mutation , *VIRAL genomes , *CELL culture , *VIRUS diseases , *HOST-virus relationships - Abstract
Abstract: The role of the α-helical domain (MH) of dengue virus (DENV) precursor membrane protein in replication was investigated by site-directed mutagenesis. Proline substitutions of three residues (120, 123 and 127) at the C-terminus, but not those at the N-terminus of MH domain, reduced the virus-like particles of DENV1, DENV2 and DENV4 detected in supernatants. In a DENV2 replicon trans-packaging system, these three mutations suppressed particles detected; two of them (I123P and V127P) also affected viral entry. In the context of DENV2 genome-length RNA, all three mutations reduced virion assembly and virus spreading in cell culture. Analysis of revertants showed that mutation A120P could partially support viral infection cycle; in contrast, mutations I123P and V127P were lethal, and adaptations of I123P→I123L and V127P→V127L were required to restore the viral infection cycle. These findings demonstrate that the C-terminus of the MH domain is involved in both assembly and entry of DENV. [ABSTRACT FROM AUTHOR]
- Published
- 2011
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