Induction of rabies virus-specific T-helper cells by synthetic peptides that carry dominant T-helper cell epitopes of the viral ribonucleoprotein

Ertl, Hildegund C. J.; Dietzschold, Bernhard; Gore, Milind M.; Ötvös, László; Larson, Jovi K.; Wunner, William H.; Koprowski, Hilary

doi:10.1128/jvi.63.7.2885-2892.1989

Cited by 113 publications

(29 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…At least three other peptides from the E glycoprotein of MVE virus have also been implicated as possible Th-cell epitope donors (21). The observation that the T-and B-cell epitopes must be linked for full activity is not new (5,6,8,9,27). It is surprising to us that this covalent linkage can apparently occur by simply mixing two peptides which contain free sulfhydryl groups.…”

Section: Discussionmentioning

confidence: 99%

“…Peptides. All of the sequences and antibody responses in BALB/c and outbred NIH-Swiss mice to the DEN virus peptides 1-2 (amino acids [aa] 1 to 30), 3-8/2 (aa 49 to 60 and 121 to 140), 4-6 (aa 72 to 91 and 93 to 105), 79 (aa 79 to 99), [5][6][7] (aa 90 to 104 and 106 to 120), 04 (aa 121 to 140), 142-1 (aa 165 to 172), 208 (aa 208 to 219), 67 (aa 255 to 274), and 17 (aa 352 to 368) and the BALB/c antibody responses to MVE virus peptides 03 (aa 77 to 97), 04 (aa 122 to 141), and 17 (aa 356 to 376) have been previously published (21,29,30). The newly synthesized or modified peptides used for determining the structural requirements of Th-cell help are shown in Table 1.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Enhancement of the antibody response to flavivirus B-cell epitopes by using homologous or heterologous T-cell epitopes

Roehrig

Johnson

Hunt

et al. 1992

J Virol

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Enhancement of the antibody response to flavivirus B-cell epitopes by using homologous or heterologous T-cell epitopes

Roehrig

Johnson

Hunt

et al. 1992

J Virol

View full text Add to dashboard Cite

show abstract

“…Several T-cell epitopes identified on pathogens to date were shown to be located within hypervariable regions of antigens, suggesting that not only antibodies but also T cells might contribute to the selection of antigenic variants (9,24). Amino acid substitutions in the antigenic regions of viral antigens are known to enable viruses to evade recognition by antibodies and T cells.…”

Section: Hplc Fractionsmentioning

confidence: 99%

Posttranslational side chain modification of a viral epitope results in diminished recognition by specific T cells

Larson

Ötvös

Ertl

1992

J Virol

Self Cite

View full text Add to dashboard Cite

A stretch of 16 amino acid residues within the nominal phosphoprotein of rabies virus was shown to carry an immunodominant epitope for class I-and class II-restricted T cells. The nominal phosphoprotein of rabies virus is thought to be heterogeneously phosphorylated at multiple serine and threonine residues. The synthetic peptide that expressed the T-cell epitope contained a single serine residue corresponding to position 196 of the protein. Phosphorylation of this serine within the synthetic peptide caused a significant decrease of the antigenic potency of the peptide. A similar effect was seen if the serine was replaced by an alanine or if the peptide was glycosylated at its acidic residues. These data suggest that T-cell-mediated recognition of antigen presented by major histocompatibility complex class Ior II-positive cells is impaired not only by point mutations but also by posttranslational side chain modifications of residues within viral epitopes. Little is known about the effect of side chain modifications on recognition by T cells. Previous studies suggested that inhibition of glycosylation of viral antigens might influence T-cell recognition (8, 25). In recent years, numerous viral epitopes have been identified for both class I-and class II-restricted T cells (13, 18, 23). Although many of these viral proteins carry modified side chains under physiological conditions, a review of the literature reveals that, in general, the epitopes identified to date lack natural glycosylation or phosphorylation sites, suggesting that these sites might not be readily accessible for recognition by T cells. The effect of side chain modification was studied by using the nominal phosphoprotein (NS protein [this protein was initially thought to be a nonstructural protein, hence the abbreviation NS]) of rabies virus, a 297-amino-acid protein that is thought to be heterogeneously phosphorylated at multiple serine and threonine residues (4, 6), as been demonstrated for vesicular stomatitis virus, the prototype virus of the Rhabdoviridae family, which includes rabies virus. MATERIALS AND METHODS Mice. Female C3H/He mice were purchased from The Jackson Laboratories, Bar Harbor, Maine, or from Harlan Sprague-Dawley, Indianapolis, Ind. They were immunized at between 8 and 12 weeks of age. Cell lines. The murine L929 fibroblast line (H-2k) was maintained in vitro in Dulbecco's minimal essential medium (MEM) supplemented with 50 jig of gentamicin sulfate per ml, 10 U of penicillin G per ml, 10 ,ug of streptomycin sulfate per ml, and 10% heat-inactivated fetal bovine serum (FBS). BHK-21 cells and HeLa cells (ATCC CCL-2; American Type Culture Collection, Rockville, Md.) were maintained in Eagle's MEM supplemented with 5% FBS and 50 ,ug of gentamycin sulfate per ml. HT-2 cells were maintained in Dulbecco's MEM supplemented with 10% FBS, 10-5 M 2-mercaptoethanol (2-ME), and 10% rat concanavalin A (ConA) supernatant. Viruses. The rabies virus strain Evelyn-Rokitniki-Abelseth

show abstract

“…In mouse and monkey immunogenicity studies and subsequently in human clinical trials, specific CMI, as measured by interferon-␥ (IFN-␥-specific enzyme-linked immunospot (ELISPOT) analysis, was induced [28,[31][32][33][34][35][36][37]. Designing epitope-based vaccines for a general population is a labor-intensive process involving assessment of the frequency of MHC types and identification of T-cell epitopes [38][39][40][41]. Bearing in mind the number of MHC alleles within a population and the number of proteins encoded by a given virus, it would be difficult to identify most CTL epitopes for most MHC alleles.…”

Section: Introductionmentioning

confidence: 99%

Overlapping synthetic peptides as vaccines

Jiang

Song

Попов

et al. 2006

Vaccine

View full text Add to dashboard Cite

Several vaccine strategies aim to generate cell-mediated immunity (CMI) against microorganisms or tumors. While epitope-based vaccines offer advantages, knowledge of specific epitopes and frequency of major histocompatibility complex (MHC) alleles is required. Here we show that using promiscuous overlapping synthetic peptides (OSP) as immunogens generated peptide-specific CMI in all vaccinated outbred mice and in different strains of inbred mice; CMI responses also recognized viral proteins. OSP immunogens also induced CMI ex vivo in dendritic cell/T-cell cocultures involving cells from individuals with different HLA haplotypes. Thus, broad CMI was induced by OSP in different experimental settings, using different immunogens, without identifying either epitopes or MHC backgrounds of the vaccinees.

show abstract

Induction of rabies virus-specific T-helper cells by synthetic peptides that carry dominant T-helper cell epitopes of the viral ribonucleoprotein

Cited by 113 publications

References 27 publications

Enhancement of the antibody response to flavivirus B-cell epitopes by using homologous or heterologous T-cell epitopes

Enhancement of the antibody response to flavivirus B-cell epitopes by using homologous or heterologous T-cell epitopes

Posttranslational side chain modification of a viral epitope results in diminished recognition by specific T cells

Overlapping synthetic peptides as vaccines

Contact Info

Product

Resources

About