Characterization of the interaction of domain III of the envelope protein of dengue virus with putative receptors from CHO cells

Huerta, Vivian; Chinea, Glay; Fleitas, Noralvis; Sarría, Mónica; Sánchez, Jorge; Toledo, Patricia; Padrón, Gabrìel

doi:10.1016/j.virusres.2008.07.022

Cited by 39 publications

(28 citation statements)

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“…The envelope protein consists of three domains: ED1, ED2, and ED3 (38,47,48). ED3 is proposed to be the binding domain for the virus (7,9,28), attaching to as yet poorly characterized cellular receptor(s); although heparan sulfate has been implicated in the interaction (29). Indeed, in mice, anti-ED3 monoclonal antibodies are potent neutralizers of dengue virus (5,18,19,27,43,52,55,60,61); often neutralizing to greater levels than those targeting ED1 or ED2 (60).…”

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confidence: 99%

An In-Depth Analysis of Original Antigenic Sin in Dengue Virus Infection

Midgley

Bajwa-Joseph

Vasanawathana

et al. 2011

J Virol

178

168

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The evolution of dengue viruses has resulted in four antigenically similar yet distinct serotypes. Infection with one serotype likely elicits lifelong immunity to that serotype, but generally not against the other three. Secondary or sequential infections are common, as multiple viral serotypes frequently cocirculate. Dengue infection, although frequently mild, can lead to dengue hemorrhagic fever (DHF) which can be life threatening. DHF is more common in secondary dengue infections, implying a role for the adaptive immune response in the disease. There is currently much effort toward the design and implementation of a dengue vaccine but these efforts are made more difficult by the challenge of inducing durable neutralizing immunity to all four viruses. Domain 3 of the dengue virus envelope protein (ED3) has been suggested as one such candidate because it contains neutralizing epitopes and it was originally thought that relatively few cross-reactive antibodies are directed to this domain. In this study, we performed a detailed analysis of the anti-ED3 response in a cohort of patients suffering either primary or secondary dengue infections. The results show dramatic evidence of original antigenic sin in secondary infections both in terms of binding and enhancement activity. This has important implications for dengue vaccine design because heterologous boosting is likely to maintain the immunological footprint of the first vaccination. On the basis of these findings, we propose a simple in vitro enzyme-linked immunosorbent assay (ELISA) to diagnose the original dengue infection in secondary dengue cases.Dengue virus is an insect-borne flavivirus transmitted to humans by the bite of an infected mosquito, usually Aedes aegypti (20). There are four circulating serotypes of dengue (dengue serotype 1 [Den1] to Den4) that show up to 70% sequence homology across their genomes (4, 17), and it is common for multiple viral serotypes to cocirculate in countries where dengue is endemic. Most dengue infections are either asymptomatic or lead to uncomplicated dengue fever (DF). However, in 1 to 5% of cases, symptoms can be more severe with the development of plasma leakage and hemorrhage. Such dengue hemorrhagic fever (DHF) can lead to circulatory collapse, resulting in a mortality rate of around 20% if left untreated.The more frequent occurrence of DHF in secondary dengue infections in children and adults suggests a role for the acquired immune system in disease pathogenesis, and there has been considerable research into both the B-and T-cell responses. Antibody-dependent enhancement (ADE) of infection, proposed by Halstead in 1977 (24, 25), is one hypothesis for this increase in severity in secondary infections (23,36). During a primary infection, antibodies that cross-react with the remaining 3 serotypes are induced. After a few months, when heterologous protection is no longer observed (54), it is hypothesized that these cross-reactive antibodies decline to subneutralizing levels, meaning that a heterologous infecting serot...

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confidence: 99%

An In-Depth Analysis of Original Antigenic Sin in Dengue Virus Infection

Midgley

Bajwa-Joseph

Vasanawathana

et al. 2011

J Virol

178

168

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“…It has also been shown that domain III of the envelope glycoprotein is an immunoglobulin-like structure and that the main viral region interacts with receptors on the host cells [29–36]. It has been also demonstrated that EIII domain of DENV-2 inhibits infection of DV on C6/36 cells and mammalian cells, suggesting that EIII domain binds molecules on the cell membrane that may participate in receptor-mediated DV entry [37].…”

Section: Introductionmentioning

confidence: 99%

Proteomic Identification of Dengue Virus Binding Proteins inAedes aegyptiMosquitoes andAedes albopictusCells

Muñoz

Limón-Camacho

Tovar

et al. 2013

BioMed Research International

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The main vector of dengue in America is the mosquito Aedes aegypti, which is infected by dengue virus (DENV) through receptors of midgut epithelial cells. The envelope protein (E) of dengue virus binds to receptors present on the host cells through its domain III that has been primarily recognized to bind cell receptors. In order to identify potential receptors, proteins from mosquito midgut tissue and C6/36 cells were purified by affinity using columns with the recombinant E protein domain III (rE-DIII) or DENV particles bound covalently to Sepharose 4B to compare and evaluate their performance to bind proteins including putative receptors from female mosquitoes of Ae. aegypti. To determine their identity mass spectrometric analysis of purified proteins separated by polyacrylamide gel electrophoresis was performed. Our results indicate that both viral particles and rE-DIII bound proteins with the same apparent molecular weights of 57 and 67 kDa. In addition, viral particles bound high molecular weight proteins. Purified proteins identified were enolase, beta-adrenergic receptor kinase (beta-ARK), translation elongation factor EF-1 alpha/Tu, and cadherin.

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“…2B and 2C). DIII projects slightly above the general viral surface [15] and is the proposed receptor binding domain [2, 22–24]. The three E monomers per icosahedral asymmetric unit (Figs.…”

Section: The Structure Of the Flavivirus Particlementioning

confidence: 99%

Molecular mechanisms involved in the early steps of flavivirus cell entry

Kaufmann

Rossmann

2011

Microbes and Infection

121

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Flaviviruses enter their host cells by receptor-mediated endocytosis, a well-orchestrated process of receptor recognition, penetration and uncoating. Recent findings on these early steps in the life cycle of flaviviruses are the focus of this review. Keywords FLAVIVIRUS; CELL ENTRY; RECEPTOR; ENDOCYTOSIS; ENVELOPE PROTEIN; PH ENVIRONMENT; STRUCTUREThe Flaviviridae are a family of small, enveloped RNA viruses that is comprised of three genera: Flavivirus, Hepacivirus, and Pestivirus. More than 70 viruses have been classified in the genus Flavivirus [1]. The genus includes various noteworthy mosquito-and tick-borne human pathogens, such as Yellow Fever virus (YFV), dengue virus (DENV), Tick-borne Encephalitis Virus (TBEV), and West Nile virus (WNV), that are subclassified into several antigenic complexes and phylogenetic groups [2]. Flaviviruses are typically associated with mild systemic disease, but can also cause severe symptoms such as hemorrhagic fever, encephalitis or death. Many of these viruses are resurgent, are spreading to new environments and are responsible for substantial morbidity and mortality around the globe. Flaviviruses are primarily transmitted through arthropod vectors. Humans and other mammals are not known to commonly develop infectious-level viremias and thus are probably incidental hosts with the exceptions of YFV, DENV and TBEV that are sufficiently well-adapted to a mammalian host. The flavivirus lifecycleThe basic stages of the flavivirus life cycle include attachment to the cell surface, internalization into the host cell, transfer of the viral RNA genome into the cytoplasm, translation of the viral proteins, replication of the genomic RNA, assembly and maturation of the virions, and ultimately the release of progeny viruses from the cell.Flaviviruses are lipid-enveloped viruses (Fig. 1A). After recognition and attachment to specific receptor molecules on the surface of the cell, the virus is internalized into the host * Correspondence should be addressed to M.G.R. (mr@purdue.edu, Tel. 765-494-4911, FAX 765-496-1189).Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. . The polyprotein is subsequently glycosylated by cellular glycosyltransferases and cleaved by a combination of viral and host proteases to release three structural (C, prM, and E) and seven non-structural proteins (NS1, NS2a, NS2b, NS3, NS4a, NS4b, and NS5). NS3 and NS5 are the bestcharacterized non-structural proteins that assemble with several other viral and host proteins to form the replication complex. NS3 combines helicase/NTPase, serine protease, and RNA triphosphatase...

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Characterization of the interaction of domain III of the envelope protein of dengue virus with putative receptors from CHO cells

Cited by 39 publications

References 50 publications

An In-Depth Analysis of Original Antigenic Sin in Dengue Virus Infection

An In-Depth Analysis of Original Antigenic Sin in Dengue Virus Infection

Proteomic Identification of Dengue Virus Binding Proteins inAedes aegyptiMosquitoes andAedes albopictusCells

Molecular mechanisms involved in the early steps of flavivirus cell entry

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