Surface expression of an immunodominant malaria protein B cell epitope by yellow fever virus 1 1Edited by J. Karn

Bonaldo, Myrna C.; Garratt, R.C.; Caufour, Philippe; Freire, Marcos S.; Rodrigues, Maurício M.; Nussenzweig, Ruth S.; Galler, Ricardo

doi:10.1006/jmbi.2001.5258

Cited by 42 publications

(61 citation statements)

References 40 publications

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“…60,61 A number of recombinant YF17D viruses that express T cell and humoral epitopes of the Plasmodium spp CS protein inserted at the fg loop (site at amino acid 200 of the E protein) have been constructed. These viruses were stable through serial passages in cultured vertebrate cells and also retained attenuation for mice and monkeys.…”

Section: Insertion Of Foreign Epitope Coding Sequences Into the Yf Gementioning

confidence: 99%

“…These viruses were stable through serial passages in cultured vertebrate cells and also retained attenuation for mice and monkeys. 58,60,62 In addition, the recombinant virus expressing a B-cell epitope from the malarial parasite Plasmodium falciparum induced antibodies against the CS protein after mouse and monkey vaccination. 60,62 The epitope expression in the E protein is an interesting approach, since it was recently reported that this protein elicits dominant immune responses corresponding either to MHC class I or class II antigens.…”

Section: Insertion Of Foreign Epitope Coding Sequences Into the Yf Gementioning

confidence: 99%

“…58,60,62 In addition, the recombinant virus expressing a B-cell epitope from the malarial parasite Plasmodium falciparum induced antibodies against the CS protein after mouse and monkey vaccination. 60,62 The epitope expression in the E protein is an interesting approach, since it was recently reported that this protein elicits dominant immune responses corresponding either to MHC class I or class II antigens. 8,22,59 Another possibility for epitope expression was developed by means of a transposon-mediated technique to randomly insert and express influenza A virus epitopes into the yellow fever virus NS1 protein.…”

Section: Insertion Of Foreign Epitope Coding Sequences Into the Yf Gementioning

confidence: 99%

See 2 more Smart Citations

The yellow fever 17D virus as a platform for new live attenuated vaccines

Bonaldo

Sequeira

Galler³

2014

Human Vaccines & Immunotherapeutics

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Section: Insertion Of Foreign Epitope Coding Sequences Into the Yf Gementioning

confidence: 99%

Section: Insertion Of Foreign Epitope Coding Sequences Into the Yf Gementioning

confidence: 99%

Section: Insertion Of Foreign Epitope Coding Sequences Into the Yf Gementioning

confidence: 99%

See 1 more Smart Citation

The yellow fever 17D virus as a platform for new live attenuated vaccines

Bonaldo

Sequeira

Galler³

2014

Human Vaccines & Immunotherapeutics

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“…We have previously described the viability of heterologous insertions in the fg loop of the YF 17D virus E protein (1). This loop is located in domain II, distant from the receptor binding domain III.…”

mentioning

confidence: 99%

Attenuation of Recombinant Yellow Fever 17D Viruses Expressing Foreign Protein Epitopes at the Surface

Bonaldo

Garratt

Marchevsky

et al. 2005

J Virol

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The yellow fever (YF) 17D vaccine is a live attenuated virus. Three-dimensional (3D) homology modeling of the E protein structure from YF 17D virus and its comparison with that from tick-borne encephalitis virus revealed that it is possible to accommodate inserts of different sizes and amino acid compositions in the flavivirus E protein fg loop. This is consistent with the 3D structures of both the dimeric and trimeric forms in which the fg loop lies exposed to solvents. We demonstrate here that YF 17D viruses bearing foreign humoral (17D/8) and T-cell (17D/13) epitopes, which vary in sequence and length, displayed growth restriction. It is hypothesized that interference with the dimer-trimer transition and with the formation of a ring of such trimers in order to allow fusion compromises the capability of the E protein to induce fusion of viral and endosomal membranes, and a slower rate of fusion may delay the extent of virus production. This would account for the lower levels of replication in cultured cells and of viremia in monkeys, as well as for the more attenuated phenotype of the recombinant viruses in monkeys. Testing of both recombinant viruses (17D/8 and 17D/13) for monkey neurovirulence also suggests that insertion at the 17D E protein fg loop does not compromise the attenuated phenotype of YF 17D virus, further confirming the potential use of this site for the development of new live attenuated 17D virus-based vaccines.The yellow fever (YF) 17D virus is attenuated and used for human vaccination. Some of the outstanding properties of this vaccine include limited viral replication in the host but with significant expansion and dissemination of the viral mass, yielding a robust and long-lived neutralizing antibody response. The vaccine is cheap and applied as a single dose, and there are well-established production methodology and quality control procedures, which include the monkey neurovirulence test (MNVT). Altogether, the 17D virus has become very attractive as an expression vector for the development of new live attenuated vaccines.The development of infectious-clone technology has allowed the genetic manipulation of the YF 17D virus genome toward the expression of foreign genes. Different technical approaches to constructing recombinant viruses based on the YF 17D virus are possible and will differ according to the antigen to be expressed. One major approach has been the creation of chimeric viruses through the exchange of structural prM/M/E genes (reviewed in reference 10). An alternative approach used in the development of YF 17D virus as a vector for heterologous antigens is the expression of particular epitopes in the E protein. In the mature virus, the E protein forms a symmetrical network of 90 dimers. These dimers are anchored into the viral envelope and lie flat on its surface. Each monomer is composed of three domains. The central and dimerization domains (I and II, respectively) are formed of several noncontiguous stretches of the polypeptide chain, while the C-terminal domain III is a c...

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“…Fusion of the MSP1 19 123,124 have induced protective responses in animal models and are also being explored.…”

Section: Antigen Deliverymentioning

confidence: 99%