ArticleVirology2011
The C-terminal helical domain of dengue virus precursor membrane protein is involved in virus assembly and entry.
Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Identification and characterization of key residues in Zika virus envelope protein for virus assembly and entry.Emerging microbes & infections · 2022Article
- Sites of vulnerability in HCV E1E2 identified by comprehensive functional screening.Cell reports · 2022Article
- Impact of yellow fever virus envelope protein on wild-type and vaccine epitopes and tissue tropism.NPJ vaccines · 2022Article
- Relative contribution of nonstructural protein 1 in dengue pathogenesis.The Journal of experimental medicine · 2020Article
- A Molecular Determinant of West Nile Virus Secretion and Morphology as a Target for Viral Attenuation.Journal of virology · 2020Article
- Structure-guided paradigm shifts in flavivirus assembly and maturation mechanisms.Advances in virus research · 2020Review
- Dengue Virus M Protein Promotes NLRP3 Inflammasome Activation To Induce Vascular Leakage in Mice.Journal of virology · 2019Article
- The Conserved Molecular Determinants of Virulence in Dengue Virus.International journal of medical sciences · 2019Review
- Membrane dynamics associated with viral infection.Reviews in medical virology · 2016Review
- A Single Amino Acid Substitution in the M Protein Attenuates Japanese Encephalitis Virus in Mammalian Hosts.Journal of virology · 2015Article
- Dengue epidemiology and pathogenesis: images of the future viewed through a mirror of the past.Virologica Sinica · 2015Review
- Highly conserved residues in the helical domain of dengue virus type 1 precursor membrane protein are involved in assembly, precursor membrane (prM) protein cleavage, and entry.The Journal of biological chemistry · 2014Article
- Glutamic acid at residue 125 of the prM helix domain interacts with positively charged amino acids in E protein domain II for Japanese encephalitis virus-like-particle production.Journal of virology · 2014Article
- Development of a novel DNA-launched dengue virus type 2 infectious clone assembled in a bacterial artificial chromosome.Virus research · 2014Article
- Distribution of fitness in populations of dengue viruses.PloS one · 2014Article
- Article
- Functional analysis of two cavities in flavivirus NS5 polymerase.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
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.
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Registered trials
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