OVA 257-264 scrambled (FILKSINE) – Ovalbumin peptide 257-264 scrambled
SB-PEPTIDE offers the scrambled version of OVA 257-264: OVA 257-264 scrambled (FILKSINE). FILKSINE can be used as a negative control of OVA 257-264 studies.
SB-PEPTIDE offers also OVA 257-264 (see section OVA 257-264).
OVA 257-264 (H-2Kb) is an epitope of interest of the egg white albumen, ovalbumin. Ovalbumin is a glycoprotein that is sufficiently large and complex to be mildly immunogenic. Indeed, it has been demonstrated that Ovalbumin contains B-cell epitopes which are recognized by specific IgE antibodies and CD4 T cell epitopes restricted by the MHC I-Ad molecule in mice and by HLA-D molecule in human.
Applications of OVA 257-264
OVA 257-264 is used to stimulate T cells in PBMCs and to quantify peptide epitope specificity and IFN-γ releasing effector cells by ELISPOT assay. OVA 257-264 is also used to test new adjuvant in immunotherapeutic vaccine development. OVA 257-264 can form a stable hydrogel and stimulate a immune response. This reaction seems to be linked with OVA 257-264 property to self-assemble into a hydrogel.
|Sequence : FILKSINE|
|MW : 963.13 g/mol (C45H74N10O13)|
|Purity : > 95%|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in propylene 2mL microtubes|
|Peptide Solubility Guideline|
|Bulk peptide quantities available|
|Product catalog||Size||Price € HT||Price $ USD|
1- Kamalov M., Kählig H., Rentenberger C., Mullner A. R. M., Peterlik H. and Becker C. F. W. Sci Rep. 9(1):2696 (2019)
Ovalbumin Epitope SIINFEKL Self-Assembles into a Supramolecular Hydrogel
Here we show that the well-known ovalbumin epitope SIINFEKL that is routinely used to stimulate ovalbumin-specific T cells and to test new vaccine adjuvants can form a stable hydrogel. We investigate properties of this hydrogel by a range of spectroscopic and imaging techniques demonstrating that the hydrogel is stabilized by self-assembly of the peptide into nanofibres via stacking of β-sheets. As peptide hydrogels are known to stimulate an immune response as adjuvants, the immunoactive properties of the SIINFEKL peptide may also originate from its propensity to self-assemble into a hydrogel. This finding requires a re-evaluation of this epitope in adjuvant testing.
2- Harms J. S., Khan M., Hall C., Splitter G. A., Homan E. J., Bremel R. D. and Smith A. J. Infect Immun. 86(7):e00281 (2018)
Brucella Peptide Cross-Reactive Major Histocompatibility Complex Class I Presentation Activates SIINFEKL-Specific T Cell Receptor-Expressing T Cells
Brucella spp. are intracellular pathogenic bacteria remarkable in their ability to escape immune surveillance and therefore inflict a state of chronic disease within the host. To enable further immune response studies, Brucella was engineered to express the well-characterized chicken ovalbumin (OVA). Surprisingly, we found that CD8 T cells bearing T cell receptors (TCR) nominally specific for the OVA peptide SIINFEKL (OT-1) reacted to parental Brucella-infected targets as well as OVA-expressing Brucella variants in cytotoxicity assays. Furthermore, splenocytes from Brucella-immunized mice produced gamma interferon (IFN-γ) and exhibited cytotoxicity in response to SIINFEKL-pulsed target cells.To determine if the SIINFEKL-reactive OT-1 TCR could be cross-reacting to Brucella peptides, we searched the Brucella proteome using an algorithm to generate a list of near-neighbor nonamer peptides that would bind to H2Kb Selecting five Brucella peptide candidates, along with controls, we verified that several of these peptides mimicked SIINFEKL, resulting in T cell activation through the « SIINFEKL-specific » TCR. Activation was dependent on peptide concentration as well as sequence. Our results underscore the complexity and ubiquity of cross-reactivity in T cell recognition. This cross-reactivity may enable microbes such as Brucella to escape immune surveillance by presenting peptides similar to those of the host and may also lead to the activation of autoreactive T cells.
3- Warger T. et al. Blood. 108(2):544-550 (2006)
Synergistic activation of dendritic cells by combined Toll-like receptor ligation induces superior CTL responses in vivo
Toll-like receptors (TLRs) are able to interact with pathogen-derived products and their signals induce the coordinated activation of innate and adaptive immune mechanisms. Dendritic cells (DCs) play a central role in these events. As the different TLRs are able to trigger MyD88/TRIF-dependent and -independent signaling pathways, we wondered if the simultaneous activation of these signaling cascades would synergize with respect to DC activation and induce superior cytotoxic T-lymphocyte (CTL) activity in vivo. We observed that indeed the combined activation of MyD88-dependent and -independent signaling induced by TLR7 and TLR3 ligands provoked a more rapid and more sustained bone marrow-derived DC (BMDC) activation with regard to the secretion of proinflammatory cytokines, like IL-6 and IL-12p70, and the expression of costimulatory molecules like CD40, CD70, and CD86. Furthermore, in the presence of combined TLR ligand-stimulated DCs, CD4(+) and CD8(+) T cells were insensitive toward the inhibitory effects of regulatory T cells. Most importantly, peptide-loaded BMDCs stimulated by TLR ligand combinations resulted in a marked increase of CTL effector functions in wild-type mice in vivo. Thus, our results provide evidence that unlocking the full potential of DCs by advanced activation protocols will boost their immunogenic potential and improve DC-based vaccination strategies.