Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus.

Rieder, Elizabeth; Berinstein, Analía; Baxt, Barry; Kang, Angray S.; Mason, Peter W.

doi:10.1073/pnas.93.19.10428

Cited by 50 publications

(31 citation statements)

References 42 publications

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“…Using CLPs as a model system for cell binding, VP7 mutants were assessed for their cell attachment capability and the data obtained demonstrated clearly that mutated CLPs either did not bind to Culicoides-derived cells at all or bound at much reduced level compared to the wt CLPs, suggesting a role for RGD in core uptake by the insect cells. MAbs specific for integrins that recognize the RGD sequences of viral proteins block virus attachment and infectivity of other viruses (33,52,61,62). In our study we have used the VP7 MAbs that are RGD site specific (e.g., H1.5 and CLPIII) to block the CLP attachment and have demonstrated that such MAbs interfere with CLP binding to KC cells.…”

Section: Vol 75 2001mentioning

confidence: 89%

RGD Tripeptide of Bluetongue Virus VP7 Protein Is Responsible for Core Attachment to Culicoides Cells

Tan

Nason²,

Staeuber

et al. 2001

J Virol

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Bluetongue virus (BTV) is an arthropod-borne virus transmitted by Culicoides species to vertebrate hosts.The double-capsid virion is infectious for Culicoides vector and mammalian cells, while the inner core is infectious for only Culicoides-derived cells. The recently determined crystal structure of the BTV core has revealed an accessible RGD motif between amino acids 168 to 170 of the outer core protein VP7, whose structure and position would be consistent with a role in cell entry. To delineate the biological role of the RGD sequence within VP7, we have introduced point mutations in the RGD tripeptide and generated three recombinant baculoviruses, each expressing a mutant derivative of VP7 (VP7-AGD, VP7-ADL, and VP7-AGQ). Each expressed mutant protein was purified, and the oligomeric nature and secondary structure of each was compared with those of the wild-type (wt) VP7 molecule. Each mutant VP7 protein was used to generate empty core-like particles (CLPs) and were shown to be biochemically and morphologically identical to those of wt CLPs. However, when mutant CLPs were used in an in vitro cell binding assay, each showed reduced binding to Culicoides cells compared to wt CLPs. Twelve monoclonal antibodies (MAbs) was generated using purified VP7 or CLPs as a source of antigen and were utilized for epitope mapping with available chimeric VP7 molecules and the RGD mutants. Several MAbs bound to the RGD motif on the core, as shown by immunogold labeling and cryoelectron microscopy. RGD-specific MAb H1.5, but not those directed to other regions of the core, inhibited the binding activity of CLPs to the Culicoides cell surface. Together, these data indicate that the RGD motif present on BTV VP7 is responsible for Culicoides cell binding activity.Orbiviruses (within the family Reoviridae), are vectored to vertebrate species by arthropods (e.g., gnats, mosquitoes and ticks) and are able to replicate in both hosts. Bluetongue virus (BTV) is the prototype virus of the genus and is transmitted by gnats (Culicoides species), causing diseases of economic importance in ruminants in many parts of the world. Vector-virus interactions play a crucial role in vector-borne disease epidemiology. The spread of Culicoides species from BTV-endemic to non-BTV (or related African horsesickness virus, AHSV, and epizootic hemorrhagic disease virus EHDV, of deer) regions of the world in the past highlights the concern that these viruses are a threat to regions of the world that are presently free from them.The initiation of a virus infection involves virus binding to ligands on the cell surface prior to cell entry by a number of mechanisms (depending on the virus). Like many other viruses, BTV appears to utilize a protein molecule(s) of mammalian cells as a receptor (20); however, it is also possible that alternative receptors may be utilized in different tissues and in different species and as accessory molecules.BTV has a genome composed of 10 segments of doublestranded RNA packaged within a double icosahedral capsid. The outer capsi...

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Section: Vol 75 2001mentioning

confidence: 89%

RGD Tripeptide of Bluetongue Virus VP7 Protein Is Responsible for Core Attachment to Culicoides Cells

Tan

Nason²,

Staeuber

et al. 2001

J Virol

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“…Adeno-associated virus type 2 can use a variety of carbohydrate or glycoprotein receptors or capsid-receptor cross-linking systems to mediate cell transduction (5,22,61,70,89,90). Foot and mouth disease virus can infect through an antiviral scFv fused to intracellular adhesion molecule 1 (62). In contrast, poliovirus requires the poliovirus receptor for infection, and binding to the N-terminal domain of the receptor leads to the changes in the capsid structure required for infection, including the loss of the VP4 protein and exposure of hydrophobic portions of VP1 (80).…”

Section: Discussionmentioning

confidence: 99%

Parvovirus Infection of Cells by Using Variants of the Feline Transferrin Receptor Altering Clathrin-Mediated Endocytosis, Membrane Domain Localization, and Capsid-Binding Domains

Hueffer

Palermo

Parrish

2004

J Virol

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The feline and canine transferrin receptors (TfRs) bind canine parvovirus to host cells and mediate rapid capsid uptake and infection. The TfR and its ligand transferrin have well-described pathways of endocytosis and recycling. Here we tested several receptor-dependent steps in infection for their role in virus infection of cells. Deletions of cytoplasmic sequences or mutations of the Tyr-Thr-Arg-Phe internalization motif reduced the rate of receptor uptake from the cell surface, while polar residues introduced into the transmembrane sequence resulted in increased degradation of transferrin. However, the mutant receptors still mediated efficient virus infection. In contrast, replacing the cytoplasmic and transmembrane sequences of the feline TfR with those of the influenza virus neuraminidase (NA) resulted in a receptor that bound and endocytosed the capsid but did not mediate viral infection. This chimeric receptor became localized to detergent-insoluble membrane domains. To test the effect of structural virus receptor interaction on infection, two chimeric receptors were prepared which contained antibody-variable domains that bound the capsid in place of the TfR ectodomain. These chimeric receptors bound CPV capsids and mediated uptake but did not result in cell infection. Adding soluble feline TfR ectodomain to the virus during that uptake did not allow infection.

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“…Interaction with integrin receptor molecules is not required for FMDV uncoating, and the virus can infect cells by an antibody-dependent pathway [153,154,184]. This suggests that expression at the cell surface of particular molecules, which can act as receptors or coreceptors for the virus, may exert an important selective pressure on FMDV.…”

Section: Rgd-independent Mechanisms Of Cell Recognitionmentioning

confidence: 99%

Foot-and-mouth disease virus: a long known virus, but a current threat

et al. 2001

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-Foot-and-mouth disease virus (FMDV) was the first animal virus identified. Since then, FMDV has become a model system in animal virology and a considerable amount of information on its structure, biology and vaccinology has been obtained. However, the disease that this virus produces (FMD) still constitutes one of the main animal health concerns. In this review, we have attempted to summarise the state of the knowledge in different basic and applied areas of FMDV research, with emphasis on those aspects relevant to the control of the disease. FMDV / structure / immunity / vaccine / variability / diagnosisRésumé -Le virus de la fièvre aphteuse : un virus connu de longue date, qui demeure une menace. Le virus de la fièvre aphteuse a été le premier virus animal identifié. Depuis lors, il est devenu un système modèle en virologie animale, et une quantité importante d'informations sur sa structure, sa biologie et sa vaccinologie a été obtenue. Cependant la maladie provoquée par ce virus constitue encore une inquiétude majeure en santé animale. Dans cette revue, nous avons tenté de résumer l'état des connaissances dans différents domaines de recherche, à la fois fondamentaux et appliqués, sur le virus de la fièvre aphteuse, en mettant l'accent sur les aspects relatifs au contrôle de la maladie. virus de la fièvre aphteuse / immunité / vaccin / variabilité / diagnostic

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Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus.

Cited by 50 publications

References 42 publications

RGD Tripeptide of Bluetongue Virus VP7 Protein Is Responsible for Core Attachment to Culicoides Cells

RGD Tripeptide of Bluetongue Virus VP7 Protein Is Responsible for Core Attachment to Culicoides Cells

Parvovirus Infection of Cells by Using Variants of the Feline Transferrin Receptor Altering Clathrin-Mediated Endocytosis, Membrane Domain Localization, and Capsid-Binding Domains

Foot-and-mouth disease virus: a long known virus, but a current threat

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