Identification of a Putative Coreceptor on Vero Cells That Participates in Dengue 4 Virus Infection

Martı́nez-Barragán, José de Jesús; Ángel, Rosa M. del

doi:10.1128/jvi.75.17.7818-7827.2001

Cited by 99 publications

(65 citation statements)

References 41 publications

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“…By this process, the antibody-virus complexes may increase the ability of the virus to bind to and internalize into cells, leading to maximum productive infection. Host molecules involved in virus entry share some properties, such as an ability to bind with high affinity to the virus and a location on the target cell surface (32). Collectively, the results support the notion that dengue virus utilizes multiple cell surface molecules for binding to and infection of target cells, although some receptors may be common to all cells and may be shared among several virus serotypes (4).…”

supporting

confidence: 70%

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

Smith

2004

J Virol

219

155

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Dengue virus, the causative agent of dengue fever, dengue shock syndrome, and dengue hemorrhagic fever, infects susceptible cells by initially binding to a receptor(s) located on the host cell surface. Evidence to date suggests that receptor usage may be cell and serotype specific, and this study sought to identify dengue virus serotype 1 binding proteins on the surface of liver cells, a known target organ. By using a virus overlay protein binding assay (VOPBA), in both nondenaturing and denaturing gel systems, a putative dengue virus serotype 1 binding protein of approximately 37 kDa expressed on the surface of liver (HepG2) cells was identified. Mass spectrometry analysis identified a candidate protein, the 37/67-kDa high-affinity laminin receptor. Entry of the dengue virus serotype 1 was significantly inhibited in a dose-dependent manner by both antibodies directed against the 37/67-kDa high-affinity laminin receptor and soluble laminin. No inhibition of virus entry was seen with dengue virus serotypes 2, 3, or 4, demonstrating that the 37/67-kDa high-affinity laminin receptor is a serotype-specific receptor for dengue virus entry into liver cells.

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supporting

confidence: 70%

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

Smith

2004

J Virol

219

155

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“…The 74KDa protein possibly constitutes part of a putative receptor complex for dengue virus infection of Vero cells (Martinez-Barragan and del Angel, 2001). …”

Section: -103mentioning

confidence: 99%

Molecular mechanism of pathogenesis of dengue virus: Entry and fusion with target cell

Seema

Jain

2005

Indian J Clin Biochem

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Dengue fever is one of the major health problems in India. Interaction with specific receptor(s) at the cell surface is one of the first events in the pathogenesis of Dengue virus. However, relatively little is known about these receptors. Cellular receptors in human monocytes and mouse neural cells are main target for the viral infection. The envelope protein of the virus (E-protein) plays important role in attachment of virus to target cells and their interaction with cellular receptors. The modulation of receptor gene(s) and/or protein(s) can be used as a method for interfering with virus entry and can thus become a new method for disease prevention. The receptors can be purified by affinity chromatography using E-protein as ligand. It has been reported that addition of highly sulfated heparan sulfate prevents E-protein binding to target cells suggesting that heparan sulfate is utilized by dengue envelope protein to bind to target cells.

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“…The second type of molecules are proteins with different molecular masses that have been described as putative DEN virus receptors in several cell lines. Among them, a 45-kDa glycoprotein in C6/36 cells (33), a 74-kDa protein present in Vero cells (23), two proteins of approximately 40 to 45 kDa and 70 to 75 kDa from a B-cell line and a myelomonocytic cell line (6), a 105-kDa protein in erythroleukemia cells (32), and proteins of 29 and 43 kDa from an endothelial cell line (44) have been described. In monocytes/ macrophages, membrane proteins of 27, 45, 67, and 87 kDa were described also as putative receptors for DEN virus by using an affinity chromatography approach (26).…”

mentioning

confidence: 99%

Heat Shock Protein 90 and Heat Shock Protein 70 Are Components of Dengue Virus Receptor Complex in Human Cells

Valle

Chávez-Salinas

Medina

et al. 2005

J Virol

Self Cite

324

185

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Dengue virus requires the presence of an unidentified cellular receptor on the surface of the host cell. By using a recently published affinity chromatography approach, an 84-kDa molecule, identified as heat shock protein 90 (HSP90) by matrix-assisted laser desorption ionization-time of flight mass spectrometry, was isolated from neuroblastoma and U937 cells. Based on the ability of HSP90 (84 kDa) to interact with HSP70 (74 kDa) on the surface of monocytes during lipopolysaccharide (LPS) signaling and evidence that LPS inhibits dengue virus infection, the presence of HSP70 was demonstrated in affinity chromatography eluates and by pull-down experiments. Infection inhibition assays support the conclusion that HSP90 and HSP70 participate in dengue virus entry as a receptor complex in human cell lines as well as in monocytes/macrophages. Additionally, our results indicate that both HSPs are associated with membrane microdomains (lipid rafts) in response to dengue virus infection. Moreover, methyl-␤-cyclodextrin, a raft-disrupting drug, inhibits dengue virus infection, supporting the idea that cholesterol-rich membrane fractions are important in dengue virus entry.Dengue (DEN) virus, the most important arthropod-borne human pathogen, represents a serious public health threat. DEN virus is transmitted to humans by the bite of the domestic mosquito, Aedes aegypti, and circulates in nature as four distinct serological types (DEN-1 to -4). DEN virus has been recognized in over 100 countries, and 2.5 billion people live in areas where DEN virus is endemic (16). The clinical manifestations of DEN virus infection range in severity from a simple self-limited febrile illness known as dengue fever to a hemorrhagic fever (DHF) and potentially fatal hemorrhagic shock syndrome. Each year, more than 50 million cases of dengue fever and several hundred thousand cases of DHF occur. During the past 8 years the incidence of dengue has grown in areas of endemicity, particularly in the American region. A specific treatment or vaccine is not yet available.DEN virus is an enveloped virus that belongs to the Flaviviridae family. Mature virions are icosahedral, 50 nm in diameter, and contain a single-strand and positive-polarity RNA as genome of about 10.7 kb (21). The DEN virus genome encodes three structural proteins (envelope glycoprotein, E; membrane, M; and capsid, C) and seven nonstructural proteins (NS1, NS2a, NS2b, NS3, NS4a, NS4b, and NS5). E protein is the major structural protein exposed on the surface of the particle, and it arrays in homodimers, parallel to viral surface. Recently, the structure of DEN virus E protein has been determined by X-ray crystallography (24). Each monomer consists of three domains: the structurally central amino-terminal domain I that organizes the structure; the dimerization domain II that contains the hydrophobic fusion peptide essential for virus-cell fusion; and finally the carboxy-terminal immunoglobulin (Ig)-like domain III, which has been proposed to function as the binding site for cellular re...

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Identification of a Putative Coreceptor on Vero Cells That Participates in Dengue 4 Virus Infection

Cited by 99 publications

References 41 publications

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

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

Molecular mechanism of pathogenesis of dengue virus: Entry and fusion with target cell

Heat Shock Protein 90 and Heat Shock Protein 70 Are Components of Dengue Virus Receptor Complex in Human Cells

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