A putative receptor for dengue virus in mosquito tissues: localization of a 45-kDa glycoprotein.

Mendoza, María Yazi; Salas-Benito, Juan Santiago; Lanz‐Mendoza, Humberto; Hernández‐Martínez, Salvador; Ángel, Rosa M. del

doi:10.4269/ajtmh.2002.67.76

Cited by 57 publications

(43 citation statements)

References 33 publications

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“…The simplest explanation is that DV of each serotype binds to different molecules on C6/36 cells. Indeed, 40-to 45-kDa cell surface proteins were observed to bind DEN-4 in C6/36 cells, whereas proteins of 67 and 80 kDa in size were reported to bind DEN-2 (60,72,83). Alternatively, it is possible that EIII has a different affinity for the same molecule on C6/36 cells, depending on the exact core sequence of the loop region in DEN-1 to -4.…”

Section: Discussionmentioning

confidence: 99%

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An External Loop Region of Domain III of Dengue Virus Type 2 Envelope Protein Is Involved in Serotype-Specific Binding to Mosquito but Not Mammalian Cells

Hung

Hsieh

Young

et al. 2004

J Virol

212

156

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Dengue virus (DV) is a flavivirus and infects mammalian cells through mosquito vectors. This study investigates the roles of domain III of DV type 2 envelope protein (EIII) in DV bindingDengue virus (DV) is an arthropod-borne human pathogen that causes a serious public health threat in tropical and subtropical regions of the world (58). The World Health Organization reports that there are approximately 500,000 cases of dengue fever per year and that the infection rate is approximately 50 million per year (see reference 15 and literature cited therein). DV has four serotypes (DEN-1 to DEN-4) that cause diseases ranging from mild dengue fever to severe symptoms such as dengue hemorrhagic fever and dengue shock syndrome (17,25,27,70).The dengue viral genome is a single-stranded, positivestrand RNA with genome organization similar to those of other flaviviruses (47). DV infects a broad range of mammalian cell lines from several species in vitro but is transmitted to humans in vivo by mosquito vectors such as Aedes aegypti and Aedes albopictus (7). Primary human cells such as peripheral blood leukocytes, blood monocytes/macrophages, dendritic cells, and B lymphocytes could also be infected by DV (9,12,13,28,32,33,46,53,55,75,76,82).Previous studies indicate that cell surface heparan sulfates (HS) are involved in attachment of DV to mammalian cells including Vero, CHO, and human hepatoma cells (11,23,31,35,44,54). HS are repeating disaccharides composed of uronic acid or L-iduronic acid and a derivative of glucosamine that is variably O-sulfated (21). Extensive sulfate modification causes cell surface HS to be highly negatively charged. The biological roles of HS are quite diverse, including cell attachment and migration, compressive resilience of cartilage, control of fibrinogenesis, cell signaling, and virus infection (3). Many pathogenic microorganisms, including viruses, gram-positive and gram-negative bacteria, and parasites, attach to HS during entry into host cells (14,69,74). Since HS is ubiquitously expressed on many cell types and is commonly used by other pathogens to gain access into cells, an additional coreceptor has been postulated to explain the limited cell tropism of DV. This coreceptor may be related to a trypsin-sensitive protein or protein complex that was shown to play a role in virion binding to mammalian cells (18,52). Several candidate coreceptor proteins for DV have been suggested for many mammalian cell lines. These proteins are between 20 to 40 kDa and 60 to 90 kDa in size and bind to dengue virions in vitro (5,31,56,59,66). Recently, DC-SIGN, a dendritic cell surface lectin, was shown to mediate DV infection to primary dendritic cells (61,81). Nevertheless, the molecular mechanism by which DV enters these cells remains poorly characterized.Besides mammalian cells, mosquito cell lines that express cell surface proteins capable of binding to DV were also reported. In C6/36 cells, 40-to 45-kDa cell surface proteins were identified to bind 83). Additional candidate coreceptors on C6/36 cells w...

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Section: Discussionmentioning

confidence: 99%

“…In C6/36 cells, 40-to 45-kDa cell surface proteins were identified to bind DEN-4 (72,83). Additional candidate coreceptors on C6/36 cells were reported to be 67 and 80 kDa (60).…”

mentioning

confidence: 99%

An External Loop Region of Domain III of Dengue Virus Type 2 Envelope Protein Is Involved in Serotype-Specific Binding to Mosquito but Not Mammalian Cells

Hung

Hsieh

Young

et al. 2004

J Virol

212

156

View full text Add to dashboard Cite

show abstract

“…Although tubulin/tubulin-like protein and prohibitin were described as putative DENV receptors in mosquitoes [15,16], these studies utilized virus overlay protein binding assay (VOPBA), a technique that was not designed for direct in vivo biological interaction. Furthermore, the capability of the VOPBA method is very limited, as most of the identified proteins can only be reported as molecular weights [17][18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%

Protein-protein interactions between A. aegypti midgut and dengue virus 2: two-hybrid screens using the midgut cDNA library

Tham

Balasubramaniam

Chew

et al. 2015

J Infect Dev Ctries

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Introduction: Dengue virus (DENV) is principally transmitted by the Aedes aegypti mosquito. To date, mosquito population control remains the key strategy for reducing the continuing spread of DENV. The focus on the development of new vector control strategies through an understanding of the mosquito-virus relationship is essential, especially targeting the midgut, which is the first mosquito organ exposed to DENV infection. Methodology: A cDNA library derived from female adult A. aegypti mosquito midgut cells was established using the switching mechanism at the 5' end of the RNA transcript (SMART), in combination with a highly potent recombination machinery of Saccharomyces cerevisiae. Gal4-based yeast two-hybrid (Y2H) assays were performed against DENV-2 proteins (E, prM, M, and NS1). Mammalian two-hybrid (M2H) and double immunofluorescence assays (IFA) were conducted to validate the authenticity of the three selected interactions.Results: The cDNA library was of good quality based on its transformation efficiency, cell density, titer, and the percentage of insert size. A total of 36 midgut proteins interacting with DENV-2 proteins were identified, some involved in nucleic acid transcription, oxidoreductase activity, peptidase activity, and ion binding. Positive outcomes were obtained from the three selected interactions validated using M2H and double IFA assays. Conclusions: The identified proteins have different biological activities that may aid in the virus replication pathway. Therefore, the midgut cDNA library is a valuable tool for identifying DENV-2 interacting proteins. The positive outcomes of the three selected proteins validated supported the quality of the cDNA library and the robustness of the Y2H mechanisms.

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“…Additionally, a protein (40-kDa) with homology to protein disulfide isomerase (PDI) was also identified among the C6/ 36 molecules that interacted with DENV4 by affinity chromatography [83•]. Interestingly, PDI has been implicated in DENV entry to endothelial cells [38•] and is also a putative [92]. Other groups reported molecules with weights of 67 and 80 kDa important for DENV2 entry [93,94].…”

Section: Dengue Virus Receptors In Mosquitoesmentioning

confidence: 99%

Dengue Virus Cellular Receptors and Tropism

et al. 2014

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Viral entry into host cells primordially defines tropism and represents an attractive target to counteract infection either by antiviral agents or by immune mediated mechanisms. Research on Dengue virus entry presents interesting challenges. Whatever the mechanism dengue virus exploits to gain entry into cells, this had to be evolutionarily conserved, so that it is now present in arthropod and human cells. Until now, dengue cellular receptors were not completely unraveled. However, we have clues about the key steps dengue virus is relying on. Initially a group of factors that interact with the virus through carbohydrate interaction assure its adherence and further contact with a protein receptor complex, which is held together thanks to its special interaction with cell membrane lipidic platforms. This interaction may be so intimate that it may trigger not only viral entry through receptormediated endocytosis, but also activation of cell signaling pathways that the virus is going to subvert to its advantage.

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A putative receptor for dengue virus in mosquito tissues: localization of a 45-kDa glycoprotein.

Cited by 57 publications

References 33 publications

An External Loop Region of Domain III of Dengue Virus Type 2 Envelope Protein Is Involved in Serotype-Specific Binding to Mosquito but Not Mammalian Cells

An External Loop Region of Domain III of Dengue Virus Type 2 Envelope Protein Is Involved in Serotype-Specific Binding to Mosquito but Not Mammalian Cells

Protein-protein interactions between A. aegypti midgut and dengue virus 2: two-hybrid screens using the midgut cDNA library

Dengue Virus Cellular Receptors and Tropism

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