Evidence that the 45-kD Glycoprotein, Part of a Putative Dengue Virus Receptor Complex in the Mosquito Cell Line C6/36, Is a Heat-Shock–Related Protein

Salas-Benito, Juan Santiago; Valle, Jorge Reyes-del; Ceballos-Olvera, Ivonne; Mosso, Clemente; Ángel, Rosa M. del

doi:10.4269/ajtmh.2007.77.283

Cited by 58 publications

(44 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More recent future science group www.futuremedicine.com investigations have identified more accurately some cellular proteins with DENV-binding ability in mosquito cells, including a laminin-binding protein, a Hsp90-related protein, prohibitin and a tubulin-like protein [54][55][56][57][58]. Finally, as also shown in mammalian cells, glycosphingolipids specific for mosquito cells were found reactive with DENV-2 [45].…”

Section: Receptors In Mosquito Cellsmentioning

confidence: 83%

“…Hsp-related protein 45 kD 4 [55] Tubulin-like protein 48 kD 2 [56] Laminin receptor 3, 4 [54] C6/36, CCl-125 (A. aegypti), adult A. aegypti Prohibitin 2 [57,58] AP-61 (A. pseudoculterallis) Glycosphingolipid 2 [45] C6/36, midgut A. aegypti Unknown protein 67-80 kD 1-4 [52] Salivary glands A. aegypti and A. polynesiensis Unknown protein 48-77 kD 1-4 [53] Salivary glands, midgut, ovary A. aegypti Unknown protein 45 kD 4 [51] DC-SIGN: Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin; GRP-78: Glucose-regulated protein 78; Hsp: Heat-shock protein; TAM: Tyro3, Axl and Mer; TIM: T-cell immunoglobulin and mucin domain containing proteins. Macrophages are also major targets of human infection with DENV and another lectin, the mannose receptor, was identified as a DENV receptor for the four DENV serotypes through binding and functional analyses [33].…”

Section: C6/36 (A Albopictus)mentioning

confidence: 99%

See 1 more Smart Citation

Dengue Virus Entry and Trafficking: Perspectives as Antiviral Target for Prevention and Therapy

2015

View full text Add to dashboard Cite

Dengue virus (DENV) is the etiological agent of the most important human viral infection transmitted by mosquitoes in the world. In spite of the serious health threat that dengue represents, at present there are no vaccine or antiviral agents available and treatment of patients consists of supportive therapy. This review will focus on the process of DENV entry into the host cell as a potential target for antiviral therapy. The recent advances in the knowledge of viral and cellular molecules and mechanisms involved in binding, internalization and trafficking of DENV into the host cell until virion uncoating are discussed, together with an overview of the strategies and compounds evaluated for development of antiviral agents targeted to DENV entry. KeywordsDengue is currently the most widespread arbovirosis in the world, with a particularly high prevalence in diverse tropical and subtropical regions of America and Asia [1]. The WHO estimates an occurrence of 50-100 million annual infections, but more recent modelling evaluations increased the number of new possible infections to 390 million per year [2]. There are four serotypes of dengue viruses (DENV), designated DENV-1 to DENV-4, that cocirculate and are transmitted to humans by the bites of the mosquitoes Aedes aegypti and Aedes albopictus. Precisely, the failure in the programs for control of the mosquito vector is one of the reasons for the explosive re-emergence and global spread of dengue in the last few decades in >100 countries, resulting in a serious public health challenge.All serotypes can produce either an inapparent infection or a wide spectrum of clinical outcomes ranging from a mild febrile illness known as dengue fever (DF) to the more severe and life-threatening forms of dengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS) [3]. The initial infection with one DENV serotype leads to lifelong protection against homologous reinfection, but only brief and partial protection against infection with other serotypes. In fact, the secondary infection with a heterologous serotype is considered a risk factor for developing DHF and DSS. These severe clinical manifestations have been associated to the phenomenon known as antibody-dependent enhancement (ADE) [3]. In this process, the antibodies elicited by the primary infection bind to the heterotypic virus without neutralization of viral infectivity, and these immune complexes are opsonized into Fc-receptor positive cells leading to an increase in DENV replication and pathogenesis [4,5].DENV is a member of the genus Flavivirus in the family Flaviviridae. The virion is a small spherical particle, 40-50 nm in diameter, containing a single-stranded positive sense RNA included in an inner nucleocapsid and surrounded by a lipid envelope. The virus genome codes for a single polyprotein that is cleaved into three structural proteins (the capsid protein C,

show abstract

Section: Receptors In Mosquito Cellsmentioning

confidence: 83%

Section: C6/36 (A Albopictus)mentioning

confidence: 99%

Dengue Virus Entry and Trafficking: Perspectives as Antiviral Target for Prevention and Therapy

2015

View full text Add to dashboard Cite

show abstract

“…Where a more viral rapid replication rate was observed in the mammalian cells after infection with D2-16681, the C6/36 cell line supported a more sustained infection from days 3-7 after infection. The sustained infection may be due to the fact that C6/36 cells harbor a specific laminin-binding protein receptor that may enhance the entry of dengue viruses into the cell (22,23). Furthermore, MMP-2 and MMP-9 were able to enhance viral entry into cells and have been correlated with the pathogenesis of infection (24,25).…”

Section: Discussionmentioning

confidence: 99%

Relationship between MMP Expression and Virulence of Dengue Virus Type-2 in Infected Mosquito and Mammalian Cells

et al. 2016

View full text Add to dashboard Cite

SUMMARY:Dengue virus infections are mostly asymptomatic but can produce a mild, self-limiting acute febrile illness, dengue fever, or a life threatening severe illness, dengue hemorrhagic fever. Dengue hemorrhagic fever is associated with increased vascular permeability partly as a result of elevated levels of matrix metalloproteinases (MMPs). We characterized MMP-2 and MMP-9 production in mosquito and mammalian cells after infection with three strains of dengue virus type-2 (D2-) ranging in virulence: 16681, the prototype New Guinea C (NGC), and PDK-53 vaccine strain. These strains were used to test variations in viral properties in vaccine candidates and confirm the production of MMP as a possible marker for virulence. A zymogram gelatinolytic activity assay was used to assess MMP-2 and MMP-9 production. We found that dengue-infected mosquito and mammalian cell lines had unique MMP-2 and MMP-9 production patterns depending on the virulence of the infecting dengue strain and the duration infection. MMP levels were highest after infection with the most virulent strain D2-16681, followed by the prototype NGC strain, in both cell lines. The MMP levels appeared to correspond with the relative amounts of infectious virions produced later in infection. Our findings improve our understanding of dengue pathogenesis and may facilitate the selection of markers to further the development of dengue vaccines.

show abstract

“…Other cell surface proteins involved in DENV entry include APO B100 (Guevara et al, 2010), the chemokine receptors CXCR3 and CXCL10 (Ip and Liao, 2010), and stress proteins related to the heat shock family such as GRP78/Bip (Jindadamrongwech and Smith, 2004) and heat-shock protein 70 and 90 (HSP70/90) (Reyes-Del Valle et al, 2005;Reyes-del Valle and del Angel, 2004). In insect C6/36 cells, prohibitin (Kuadkitkan et al, 2010) and the 45-kD heat-shock related glycoprotein (Salas-Benito et al, 2007) have been shown involved in DENV entry. Nevertheless, the exact cell surface proteins serving as receptors/co-receptors for DENV entry is still not well defined.…”

Section: Introductionmentioning

confidence: 99%

The interaction between claudin-1 and dengue viral prM/M protein for its entry

Che

Tang

2013

Virology

View full text Add to dashboard Cite

Dengue disease is becoming a huge public health concern around the world as more than one-third of the world's population living in areas at risk of infection. In an effort to assess host factors interacting with dengue virus, we identified claudin-1, a major tight junction component, as an essential cell surface protein for dengue virus entry. When claudin-1 was knocked down in Huh 7.5 cells via shRNA, the amount of dengue virus entering host cells was reduced. Consequently, the progeny virus productions were decreased and dengue virus-induced CPE was prevented. Furthermore, restoring the expression of claudin-1 in the knockdown cells facilitated dengue virus entry. The interaction between claudin-1 and dengue viral prM protein was further demonstrated using the pull-down assay. Deletion of the extracellular loop 1 (ECL1) of claudin-1 abolished such interaction, so did point mutations C54A, C64A and I32M on ECL1. These results suggest that the interaction between viral protein prM and host protein claudin-1 was essential for dengue entry. Since host and viral factors involved in virus entry are promising therapeutic targets, determining the essential role of claudin-1 could lead to the discovery of entry inhibitors with attractive therapeutic potential against dengue disease.

show abstract

Evidence that the 45-kD Glycoprotein, Part of a Putative Dengue Virus Receptor Complex in the Mosquito Cell Line C6/36, Is a Heat-Shock–Related Protein

Cited by 58 publications

References 36 publications

Dengue Virus Entry and Trafficking: Perspectives as Antiviral Target for Prevention and Therapy

Dengue Virus Entry and Trafficking: Perspectives as Antiviral Target for Prevention and Therapy

Relationship between MMP Expression and Virulence of Dengue Virus Type-2 in Infected Mosquito and Mammalian Cells

The interaction between claudin-1 and dengue viral prM/M protein for its entry

Contact Info

Product

Resources

About