Amyloid Form of Ovalbumin Evokes Native Antigen-specific Immune Response in the Host

Tufail, Saba; Owais, Mohammad; Kazmi, Shadab; Balyan, Renu; Khalsa, Jasneet Kaur; Syed, Farhatullah; Sherwani, Asif; Gatoo, Manzoor Ahmad; Umar, Mohd Saad; Zubair, Swaleha

doi:10.1074/jbc.m113.540989

Cited by 16 publications

(29 citation statements)

References 53 publications

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“…The presence of 20 mM trifluoroacetic acid or 30 mM trichloroacetic acid at room temperature even induces OVA aggregation as evidenced by increased ThT fluorescence and β‐sheet contents (Naeem et al., ). OVA aggregates with increased ThT fluorescence are also formed at room temperature when OVA solutions (pH 2.5) are subjected to continuous shaking for multiple days (Tufail et al., ).…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

“…Incubation of OVA (pH 2.5, room temperature) under continuous shaking for 10 days results in fibrillar structures, whereas aggregates with a suprafibrillar structure are observed after 15 days (Tufail et al., ).…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

“…Heating OVA at 40 to 90 °C and neutral pH decreases the percentage of helical structures, and increases ThT fluorescence (Azakami, Mukai, & Kato, ; Pearce, Mackintosh, & Gerrard, ). Also, incubation of OVA at room temperature (pH 7.0) under continuous shaking for up to 15 days yields aggregates with lower percentages of helical structures and higher levels of ThT fluorescence than the starting material (Tufail et al., ).…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

“…(), the structure of OVA aggregates formed during heating at 75 to 80 °C for 24 hr at neutral pH is compatible with that of semiflexible strings of monomers. Fibrillar aggregates have also been reported to result from incubation (pH 7.0) at room temperature during agitation for 15 days (Tufail et al., ). At low ionic strength, heat‐induced aggregates are weakly branched and with increasing ionic strength, the degree of branching and the flexibility increases (Pouzot et al., ).…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

“…However, Tufail et al. () found aggregation of OVA fibrils over several days to be reversible. After fibril formation (room temperature, pH 2.5 or 7.0) and suspension of the fibrils at pH 7.4, monomeric OVA was released from the fibrils in a slow and steady manner.…”

Section: Hen Egg Proteinsmentioning

confidence: 99%

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Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

Jansens

Lambrecht

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Conditions including heating mode, time, temperature, pH, moisture and protein concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes, and/or salt influence amyloid fibril (AF) formation as they can affect the accessibility of amino acid sequences prone to aggregate. As some conditions applied on model protein resemble conditions in food processing unit operations, we here hypothesize that food processing can lead to formation of protein AFs with a compact cross β‐sheet structure. This paper reviews conditions and food constituents that affect amyloid fibrillation of egg and cereal proteins. While egg and cereal proteins often coexist in food products, their impact on each other's fibrillation remains unknown. Hen egg ovalbumin and lysozyme form AFs when subjected to moderate heating at acidic pH separately. AFs can also be formed at higher pH, especially in the presence of alcohols or chaotropic/reducing agents. Tryptic wheat gluten digests can form fibrillar structures at neutral pH and maize and rice proteins do so in aqueous ethanol or at acidic pH, respectively.

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Section: Hen Egg Proteinsmentioning

confidence: 99%

Section: Hen Egg Proteinsmentioning

confidence: 99%

Section: Hen Egg Proteinsmentioning

confidence: 99%

Section: Hen Egg Proteinsmentioning

confidence: 99%

Section: Hen Egg Proteinsmentioning

confidence: 99%

See 3 more Smart Citations

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

Jansens

Lambrecht

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Minimalist Adjuvant‐Free Nano‐Vaccine Based on Antigen Self‐Assembled Amyloid‐Like Fibrils to Induce Potent Immune Response

Wang,

Xia,

et al. 2024

Adv Healthcare Materials

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The development of cancer vaccines is at the forefront of cancer immunotherapy. Most existing strategies to induce an efficient anti‐tumor immune response rely on molecular adjuvants and the incorporation of complex synthetic vectors into vaccine formulations. In contrast, this study introduces a one‐step engineering technique to assemble the model antigen, Ovalbumin (OVA), into amyloid aggregates, leveraging biomimetic folding and aggregation to create non‐fibrillar OVA globular aggregates and OVA amyloid‐like fibrils as single‐component, adjuvant‐free vaccines. Notably, the OVA amyloid‐like fibrils induced stronger immune responses compared to the native form, as evidenced by robust humoral immune reactions and the establishment of immune memory. These enhanced responses can be attributed to the self‐adjuvant effect of the unique assembled structure, which preserves antigenic epitopes, improves antigen stability, facilitates antigen internalization, prolongs retention at the injection site, enhances antigen trafficking to the lymphoid organs, and promotes increased secretion of antibodies and cytokines. Furthermore, the efficacy of the vaccine was validated in a high OVA‐expressing tumor model, demonstrating the potential of OVA amyloid‐like fibrils as an effective vaccine for cancer immunoprevention. This minimalist self‐adjuvant vaccine strategy holds promising implications for cancer immunotherapy and can inform the design of other protein antigen‐based vaccines.

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Neurodegeneration meets immunology – A chemical biology perspective

Araman

Hart

2019

Bioorganic & Medicinal Chemistry

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Amyloid Form of Ovalbumin Evokes Native Antigen-specific Immune Response in the Host

Cited by 16 publications

References 53 publications

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

Minimalist Adjuvant‐Free Nano‐Vaccine Based on Antigen Self‐Assembled Amyloid‐Like Fibrils to Induce Potent Immune Response

Neurodegeneration meets immunology – A chemical biology perspective

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