Tick-borne encephalitis virus interaction with the target cells

Mal'dov, D G; Karganova, Galina G.; Timofeev, A.

doi:10.1007/bf01309594

Cited by 17 publications

(5 citation statements)

References 8 publications

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“…There are two major receptor candidates for TBEV in mammalian cells, laminin-binding protein (LBP) and the αVβ3 integrin but no receptor candidates in tick cells have been identified so far [ 61 , 62 , 63 ]. Studies using anti-idiotypic antibodies suggested that there could be other receptor candidates of as yet unknown identity [ 61 , 64 , 65 ]. In addition, under certain conditions it is possible to fuse TBEV with liposomes, hence, lipids could also be involved in binding [ 66 , 67 ].…”

Section: Life Cyclementioning

confidence: 99%

Tick-Borne Encephalitis Virus: A Structural View

Pulkkinen

Butcher

Anastasina

2018

Viruses

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Tick-borne encephalitis virus (TBEV) is a growing health concern. It causes a severe disease that can lead to permanent neurological complications or death and the incidence of TBEV infections is constantly rising. Our understanding of TBEV’s structure lags behind that of other flaviviruses, but has advanced recently with the publication of a high-resolution structure of the TBEV virion. The gaps in our knowledge include: aspects of receptor binding, replication and virus assembly. Furthermore, TBEV has mostly been studied in mammalian systems, even though the virus’ interaction with its tick hosts is a central part of its life cycle. Elucidating these aspects of TBEV biology are crucial for the development of TBEV antivirals, as well as the improvement of diagnostics. In this review, we summarise the current structural knowledge on TBEV, bringing attention to the current gaps in our understanding, and propose further research that is needed to truly understand the structural-functional relationship of the virus and its hosts.

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Section: Life Cyclementioning

confidence: 99%

Tick-Borne Encephalitis Virus: A Structural View

Pulkkinen

Butcher

Anastasina

2018

Viruses

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“…Most flaviviruses replicate in vertebrate and arthropod cells and exhibit a wide species and tissue tropism. Numerous candidate receptor proteins with a molecular mass of 40 to 80 kDa have been found to associate with flaviviruses in binding assays (19,22,27,36,44). Furthermore, an important role of heparan sulfate has also been demonstrated for the attachment of dengue-2 virus to vertebrate cells (7).…”

mentioning

confidence: 99%

Substitutions at the Putative Receptor-Binding Site of an Encephalitic Flavivirus Alter Virulence and Host Cell Tropism and Reveal a Role for Glycosaminoglycans in Entry

Lee

Lobigs

2000

J Virol

142

124

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The flavivirus receptor-binding domain has been putatively assigned to a hydrophilic region (FG loop) Virus attachment to the host cell is the first stage of the virus replication cycle. It requires the molecular interaction between the virion surface and a host cell receptor and is often the basis for viral species and tissue tropisms as well as virulence properties. The cellular receptors for some viruses have been defined and reveal diverse strategies for virus attachment, ranging from binding to specific cell surface proteins to attachment via widely distributed carbohydrate moieties, such as sialic acid and heparan sulfate (for a review, see reference 48). For a large number of viruses, however, specific host cell receptors have not been identified. The use of multiple receptors on individual or different cells could be one reason for this lack of knowledge. This scenario has been proposed for the attachment of flaviviruses (35), a genus of approximately 70 mainly arthropod-borne, enveloped RNA viruses. Most flaviviruses replicate in vertebrate and arthropod cells and exhibit a wide species and tissue tropism. Numerous candidate receptor proteins with a molecular mass of 40 to 80 kDa have been found to associate with flaviviruses in binding assays (19,22,27,36,44). Furthermore, an important role of heparan sulfate has also been demonstrated for the attachment of dengue-2 virus to vertebrate cells (7). Interestingly, cell surface glycosaminoglycans (GAGs) are exploited as attachment molecules by other viruses in a process thought to concentrate virus particles at the cell surface for subsequent binding to high-affinity receptors (for a review, see reference 2). No experimental evidence on the use or nature of a high-affinity receptor for any of the flaviviruses exists at present.Flavivirus attachment and entry are mediated by the envelope (E) protein (ϳ50 kDa), the major glycoprotein on the flavivirus particle (for reviews, see references 6 and 33). The E protein forms an oligomer with the small membrane (M) protein (ϳ8 kDa) and constitutes most of the accessible virion surface; this is reflected in the dominance of the E protein as target antigen for virus-neutralizing and protective antibodies (33). The definition of the crystal structure of the ectodomain of the E protein of the flavivirus tick-borne encephalitis virus (TBE) (37), in combination with phenotypic analyses of E protein variants, has shed light on functional domains and mechanisms involved in flavivirus attachment and entry (for a review, see reference 33). An investigation by one of us on genotypic changes associated with host cell adaptation of the encephalitic flavivirus Murray Valley encephalitis virus (MVE) suggested an important role for residue 390 in the E protein in cell tropism and virulence (25). Asp 390 found in the prototype virus was altered to His, Gly, Ala, or Asn after passage of MVE in a human adenocarcinoma (SW13) cell line, resulting in improved growth in the human cell line as well as virulence attenuation in mice. Resi...

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“…The direct relation between the number of virus receptor molecules and the susceptibility to Sindbis virus infection has been shown on BHK cells transfected with the high affinity laminin receptor gene [17]. Only one paper reports the identification of TBE virus receptor using anti-ID antibodies [35]. By trypsin treatment of virus-susceptible cells, the authors showed that at least one of the putative cellular receptors for TBE virus includes a protein component.…”

Section: Discussionmentioning

confidence: 99%

A Putative Host Cell Receptor for Tick-Borne Encephalitis Virus Identified by Anti-Idiotypic Antibodies and Virus Affinoblotting

et al. 1999

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Anti-idotypic monoclonal antibodies (anti-ID MAbs) were made against two mouse MAbs that neutralize the infectivity of the tick-borne encephalitis (TBE) virus. Three of the anti-ID MAbs (1) inhibited the binding of respective idiotypic MAb to the TBE virus antigen, (2) inhibited the infectivity of TBE virus when preincubated with virus-susceptible cells, and (3) bound to the surface of virus-susceptible but not virus-nonsusceptible cells. They recognized a 35-kD protein in immunoblotting analysis. Identification of this protein as a component of a putative TBE virus receptor was supported by the viroblot technique. In this assay, two polypeptide signals of 35 and 18 kD were obtained after incubation of blotted cell membrane proteins with the TBE virion antigen.

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Tick-borne encephalitis virus interaction with the target cells

Abstract: The binding of tick-borne encephalitis virus to porcine kidney embryo cells was studied. Anti-idiotypic antibodies against TBE virus E protein precipitated gp110 kDa which is predicted to be a cellular receptor for TBE virus.

Cited by 17 publications

References 8 publications

Tick-Borne Encephalitis Virus: A Structural View

Tick-Borne Encephalitis Virus: A Structural View

Substitutions at the Putative Receptor-Binding Site of an Encephalitic Flavivirus Alter Virulence and Host Cell Tropism and Reveal a Role for Glycosaminoglycans in Entry

A Putative Host Cell Receptor for Tick-Borne Encephalitis Virus Identified by Anti-Idiotypic Antibodies and Virus Affinoblotting

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