期刊
VIROLOGY
卷 410, 期 1, 页码 170-180出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2010.11.006
关键词
Dengue virus; Precursor membrane; Virus-like particles; Assembly; Entry
类别
资金
- National Science Council Taiwan [NSC95-2320-B-002- 084-MY3]
- JABSOM
- National Center for Research Resources of the National Institutes of Health [2P20RR018727-06A1]
The role of the alpha-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. (C) 2010 Elsevier Inc. All rights reserved.
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