Serotype-Specific Entry of Dengue Virus into Liver Cells: Identification of the 37-Kilodalton/67-Kilodalton High-Affinity Laminin Receptor as a Dengue Virus Serotype 1 Receptor

Thepparit, Chutima; Smith, Duncan R.

doi:10.1128/jvi.78.22.12647-12656.2004

Cited by 219 publications

(166 citation statements)

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“…The increase in virus yield seen in the presence of L-Asn suggested that fusion with lysosomes resulted in a degree of virus degradation. The yield of intracellular virus, determined as described elsewhere (Thepparit & Smith, 2004), was similarly increased in the presence of L-Asn (P,0.001) and decreased in the presence of 3-MA (P50.001) (Fig. 3c).…”

mentioning

confidence: 70%

Section: Methodsmentioning

confidence: 99%

“…After 2 h, normal growth medium (with or without autophagy modulator as appropriate) was added and cells were incubated under normal conditions until harvesting of the cells or medium. Virus titres were determined by standard plaque assay as described previously (Sithisarn et al, 2003) and intracellular virus levels were determined as described elsewhere (Thepparit & Smith, 2004).Approximately 3610 4 HepG2 cells were seeded and grown on 1 cm 2 coverslips under standard conditions for 24 h, followed directly by infection with DENV-2 at 10 p.f.u. per cell for 2 h or pre-incubated for 3 h with 10 mM 3-MA in DMEM/FBS or for 1 h with 100 nM rapamycin or 30 mM L-Asn in DMEM/FBS before virus infection at 10 p.f.u.…”

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confidence: 99%

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Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes

Panyasrivanit

Khakpoor

Wikan

et al. 2009

Journal of General Virology

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Infections with dengue virus (DENV) are a significant public health concern in tropical and subtropical regions. However, little detail is known about how DENV interacts with the host-cell machinery to facilitate its translation and replication. In DENV-infected HepG2 cells, an increase in the level of LC3-II (microtubule-associated protein 1 light chain 3 form II), the autophagosomal membrane-bound form of LC3, was observed, and LC3 was found to co-localize with dsRNA and DENV NS1 protein, as well as ribosomal protein L28, indicating the presence of at least some of the DENV translation/replication machinery on autophagic vacuoles. Inhibition of fusion of autophagic vacuoles with lysosomes resulted in an increase in both intracellular and extracellular virus, and co-localization observed between mannose-6-phosphate receptor (MPR) and dsRNA and between MPR and LC3 identified the autophagic vacuoles as amphisomes. Amphisomes are formed as a result of fusion between endosomal and autophagic vacuoles, and as such provide a direct link between virus entry and subsequent replication and translation. INTRODUCTIONWith an estimated 100 million infections per year worldwide, dengue virus (DENV), which is spread to humans by the bite of female Aedes mosquitoes, represents a significant public health threat in tropical and subtropical countries (Guzman & Kouri, 2002). The DENV complex comprises four antigenically distinct viruses termed DENV serotypes 1, 2, 3 and 4 (DENV-1 to -4), all of which can cause a wide spectrum of disease presentation, from a relatively mild febrile disease to a life-threatening haemorrhagic syndrome (Malavige et al., 2004). DENV is an enveloped, positivesense, single-stranded RNA virus of approximately 11 kb that encodes three structural proteins (core, pre-membrane and envelope) and seven non-structural proteins (NS1, NS2A, NS2B, NS3, NS4A, NS4B and NS5) in one open reading frame (Chang, 1997). Entry of DENV into a susceptible cell occurs primarily through receptormediated endocytosis via clathrin-coated pits (Krishnan et al., 2007) and the virus is then trafficked to endosomes (Krishnan et al., 2007;van der Schaar et al., 2007) and fuses with the endosomal membranes (Heinz et al., 2004) through a pH-dependent conformational change in the envelope protein (Modis et al., 2004;Mukhopadhyay et al., 2005). The fate of the released nucleocapsid is largely obscure, although it is known that, after uncoating of the virus genome, the host-cell translational machinery is utilized to synthesize a polyprotein precursor that is processed co-and post-translationally by a virus-encoded protease (NS3) and host signallases (Cahour et al., 1992). Translation and subsequent replication of the DENV genome occur in tight association with intracellular membranous structures that are believed to be endoplasmic reticulum (ER)-derived (Clyde et al., 2006;Miller & Krijnse-Locker, 2008;Salonen et al., 2005), although the exact origin of these membranes remains unclear.Autophagy is a lysosomal degradation pathway involve...

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confidence: 70%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes

Panyasrivanit

Khakpoor

Wikan

et al. 2009

Journal of General Virology

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148

176

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“…Several types of cellular receptor have been identified for DENV: highly sulfated heparan sulfates (hsHS) (Chen et al, 1997), the lectins DC-SIGN and L-SIGN (Navarro-Sanchez et al, 2003;Tassaneetrithep et al, 2003) and the lamininbinding protein (Thepparit & Smith, 2004;Tio et al, 2005). The structure of the complex between DENV and the carbohydrate-recognition domain of DC-SIGN has et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus

Lisova

Hardy

Petit

et al. 2007

Journal of General Virology

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Dengue is caused by a taxonomic group of four viruses, dengue virus types 1-4 (DENV1-DENV4). A molecular understanding of the antibody-mediated protection against this disease is critical to design safe vaccines and therapeutics. Here, the energetic epitope of antibody mAb4E11, which neutralizes the four serotypes of DENV but no other flavivirus, and binds domain 3 (ED3) of their envelope glycoprotein, was characterized. Alanine-scanning mutagenesis of the ED3 domain from serotype DENV1 was performed and the affinities between the mutant domains and the Fab fragment of mAb4E11 were measured. The epitope residues (307-312, 387, 389 and 391) were at the edges of two distinct b-sheets. Four residues constituted hot spots of binding energy. They were aliphatic and contributed to form a hydrophobic pocket (Leu308, Leu389), or were positively charged (Lys307, Lys310). They may bind the diversity residues of mAb4E11, H-Trp96-Glu97. Remarkably, cyclic residues occupy and block the hydrophobic pocket in all unrelated flaviviruses. Transplanting the epitope from the ED3 domain of DENV into those of other flaviviruses restored affinity. The epitope straddles residues of ED3 that are involved in virulence, e.g. Asn/Asp390. These results define the epitope of mAb4E11 as an antigenic signature of the DENV group and suggest mechanisms for its neutralization potency. INTRODUCTIONDengue is a re-emerging viral disease. It is caused by four types of virus, dengue virus types 1-4 (DENV1-DENV4), which belong to the species Dengue virus in the genus Flavivirus (Heinz et al., 2000). They are transmitted by Aedes mosquitoes and infect between 50 million and 100 million persons each year. The disease generally takes a mild form, dengue fever, but severe forms, dengue haemorragic fever and dengue shock syndrome, have recently become epidemic (Gubler, 2002).The immune response against an infection by DENV involves both a humoral component, in the form of neutralizing antibodies, and a cell-mediated component (Guzman & Kouri, 2002). The preferential reactivation of the memory B cells that correspond to a primary infection, and an antibody-dependent enhancement of infection, might constitute triggering mechanisms of the severe forms during a secondary infection by a different viral serotype (Halstead, 2003; Mongkolsapaya et al., 2003). A molecular understanding of the events that lead to antibody neutralization, enhancement or escape is critical to the development of efficient and secure vaccines and therapeutics. DENV1-DENV4 are enveloped RNA viruses, like all flaviviruses. The structures of the whole virus and of the envelope glycoprotein E (gpE) have been solved by electron cryomicroscopy and X-ray crystallography (Modis et al., 2003(Modis et al., , 2005 Zhang et al., 2003). Ninety dimers of gpE cover the surface of the virus. Each monomer comprises three ectodomains, ED1-ED3, and a transmembrane segment. ED2 includes the dimerization interface, a glycosylation site and the peptide of fusion with the cellular membrane. ED3 is continuou...

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“…Thus, it was assumed that RPSA plays a significant role in the tumor progression (Martignone et al, 1993;Menard et al, 1997). Previous studies reported that RPSA interacted with many ligands, but the underlying interaction mechanism had not been elucidated yet (Gauczynski et al, 2001;Thepparit and Smith, 2004;Kim et al, 2005;Akache et al, 2006;Gauczynski et al, 2006). In addition, the crystal structure of the partial domain of human RPSA was discovered and it might suggest the function of RPSA and facilitate the design of novel therapeutics targeting RPSA (Jamieson et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

RPSA Gene Mutants Associated with Risk of Colorectal Cancer among the Chinese Population

Zhang

Jin²,

Liu³

et al. 2013

Asian Pacific Journal of Cancer Prevention

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Serotype-Specific Entry of Dengue Virus into Liver Cells: Identification of the 37-Kilodalton/67-Kilodalton High-Affinity Laminin Receptor as a Dengue Virus Serotype 1 Receptor

Cited by 219 publications

References 44 publications

Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes

Co-localization of constituents of the dengue virus translation and replication machinery with amphisomes

Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus

RPSA Gene Mutants Associated with Risk of Colorectal Cancer among the Chinese Population

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