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ds2 vaccine  (Moderna)

 
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    Structured Review

    Moderna ds2 vaccine
    (A) Schematic diagram and design rationale of monomer A. The design of monomer A was outlined (top). Substitutions unique to monomer A and <t>DS2</t> are labeled in black and gray, respectively. Substitutions shared among DS-Cav1, DS2, and monomer A are colored in red, and those shared between DS2 and monomer A are colored in blue. The dashed squares indicated the deleted residues. In the pre-F structure (PDB: 5k6i), Epitope I, II, III, IV, V, and Ø were labeled in magenta, green, purple, red, yellow, and blue, respectively and their neutralizing sensitivities are indicated. (B) Binding affinities of monomer A (top) and scDimer AA (bottom) with MAbs targeting six epitopes. Actual and fitted curves were represented by red and black lines, respectively. K D values were listed as mean ± SD of three experiments. (C) Endpoint titers of immunized antigen-binding IgG in murine sera were measured by ELISA. Groups of mice (n=4∼5) were intramuscularly immunized with 3 or 10 µg of monomer A or scDimer AA at 0, 3, and 6 weeks with Alhydrogel ® adjuvant. Serum samples were collected on day 56 (two weeks after the 3 rd immunization) and subjected for ELISA test. (D) Neutralization of RSV A2 strain in murine sera on day 56 was assessed. (E) Design of scDimer AA. Two truncated monomers A were tandemly linked, with the latter one starting at N27 residue. (F) Crystal structure of scDimer AA, with epitopes labeled as in panel A. Dotted lines represented areas with uncharacterized structures due to the flexibility of the regions. In (C) and (D), dotted lines indicated the lower limit of detection (LLD). Any value less than the LLD was assigned a value of 1⁄2 the LLD. Data were derived from two technical replicates of a single experiment, with bars indicating mean ± SD. P values were determined using Two-way ANOVA (ns indicated P > 0⋅05; * indicated P < 0⋅05; ** indicated P < 0⋅01, *** indicated P < 0⋅001, **** indicated P < 0⋅0001).
    Ds2 Vaccine, supplied by Moderna, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ds2+vaccine/ds2+vaccine/bio_rxiv__2025__05__31__655981-63-26-37
    Average 90 stars, based on 1 article reviews
    ds2 vaccine - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms"

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms

    Journal: bioRxiv

    doi: 10.1101/2025.05.31.655981

    (A) Schematic diagram and design rationale of monomer A. The design of monomer A was outlined (top). Substitutions unique to monomer A and DS2 are labeled in black and gray, respectively. Substitutions shared among DS-Cav1, DS2, and monomer A are colored in red, and those shared between DS2 and monomer A are colored in blue. The dashed squares indicated the deleted residues. In the pre-F structure (PDB: 5k6i), Epitope I, II, III, IV, V, and Ø were labeled in magenta, green, purple, red, yellow, and blue, respectively and their neutralizing sensitivities are indicated. (B) Binding affinities of monomer A (top) and scDimer AA (bottom) with MAbs targeting six epitopes. Actual and fitted curves were represented by red and black lines, respectively. K D values were listed as mean ± SD of three experiments. (C) Endpoint titers of immunized antigen-binding IgG in murine sera were measured by ELISA. Groups of mice (n=4∼5) were intramuscularly immunized with 3 or 10 µg of monomer A or scDimer AA at 0, 3, and 6 weeks with Alhydrogel ® adjuvant. Serum samples were collected on day 56 (two weeks after the 3 rd immunization) and subjected for ELISA test. (D) Neutralization of RSV A2 strain in murine sera on day 56 was assessed. (E) Design of scDimer AA. Two truncated monomers A were tandemly linked, with the latter one starting at N27 residue. (F) Crystal structure of scDimer AA, with epitopes labeled as in panel A. Dotted lines represented areas with uncharacterized structures due to the flexibility of the regions. In (C) and (D), dotted lines indicated the lower limit of detection (LLD). Any value less than the LLD was assigned a value of 1⁄2 the LLD. Data were derived from two technical replicates of a single experiment, with bars indicating mean ± SD. P values were determined using Two-way ANOVA (ns indicated P > 0⋅05; * indicated P < 0⋅05; ** indicated P < 0⋅01, *** indicated P < 0⋅001, **** indicated P < 0⋅0001).
    Figure Legend Snippet: (A) Schematic diagram and design rationale of monomer A. The design of monomer A was outlined (top). Substitutions unique to monomer A and DS2 are labeled in black and gray, respectively. Substitutions shared among DS-Cav1, DS2, and monomer A are colored in red, and those shared between DS2 and monomer A are colored in blue. The dashed squares indicated the deleted residues. In the pre-F structure (PDB: 5k6i), Epitope I, II, III, IV, V, and Ø were labeled in magenta, green, purple, red, yellow, and blue, respectively and their neutralizing sensitivities are indicated. (B) Binding affinities of monomer A (top) and scDimer AA (bottom) with MAbs targeting six epitopes. Actual and fitted curves were represented by red and black lines, respectively. K D values were listed as mean ± SD of three experiments. (C) Endpoint titers of immunized antigen-binding IgG in murine sera were measured by ELISA. Groups of mice (n=4∼5) were intramuscularly immunized with 3 or 10 µg of monomer A or scDimer AA at 0, 3, and 6 weeks with Alhydrogel ® adjuvant. Serum samples were collected on day 56 (two weeks after the 3 rd immunization) and subjected for ELISA test. (D) Neutralization of RSV A2 strain in murine sera on day 56 was assessed. (E) Design of scDimer AA. Two truncated monomers A were tandemly linked, with the latter one starting at N27 residue. (F) Crystal structure of scDimer AA, with epitopes labeled as in panel A. Dotted lines represented areas with uncharacterized structures due to the flexibility of the regions. In (C) and (D), dotted lines indicated the lower limit of detection (LLD). Any value less than the LLD was assigned a value of 1⁄2 the LLD. Data were derived from two technical replicates of a single experiment, with bars indicating mean ± SD. P values were determined using Two-way ANOVA (ns indicated P > 0⋅05; * indicated P < 0⋅05; ** indicated P < 0⋅01, *** indicated P < 0⋅001, **** indicated P < 0⋅0001).

    Techniques Used: Labeling, Binding Assay, Enzyme-linked Immunosorbent Assay, Adjuvant, Neutralization, Residue, Derivative Assay

    Related Articles

    Labeling:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).

    Binding Assay:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).

    Enzyme-linked Immunosorbent Assay:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).

    Adjuvant:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).

    Neutralization:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).

    Residue:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).

    Derivative Assay:

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms
    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Article Title: Group IIC self-splicing intron-derived novel circular RNA vaccine elicits superior immune response against RSV
    Article Snippet: Based on DS-Cav1 design, an additional disulfide bond was incorporated to generate DS2, which has been used in Moderna’s mRNA vaccine ( ).



    Similar Products

    ds2 vaccine  (Moderna)
    90
    Moderna ds2 vaccine
    (A) Schematic diagram and design rationale of monomer A. The design of monomer A was outlined (top). Substitutions unique to monomer A and <t>DS2</t> are labeled in black and gray, respectively. Substitutions shared among DS-Cav1, DS2, and monomer A are colored in red, and those shared between DS2 and monomer A are colored in blue. The dashed squares indicated the deleted residues. In the pre-F structure (PDB: 5k6i), Epitope I, II, III, IV, V, and Ø were labeled in magenta, green, purple, red, yellow, and blue, respectively and their neutralizing sensitivities are indicated. (B) Binding affinities of monomer A (top) and scDimer AA (bottom) with MAbs targeting six epitopes. Actual and fitted curves were represented by red and black lines, respectively. K D values were listed as mean ± SD of three experiments. (C) Endpoint titers of immunized antigen-binding IgG in murine sera were measured by ELISA. Groups of mice (n=4∼5) were intramuscularly immunized with 3 or 10 µg of monomer A or scDimer AA at 0, 3, and 6 weeks with Alhydrogel ® adjuvant. Serum samples were collected on day 56 (two weeks after the 3 rd immunization) and subjected for ELISA test. (D) Neutralization of RSV A2 strain in murine sera on day 56 was assessed. (E) Design of scDimer AA. Two truncated monomers A were tandemly linked, with the latter one starting at N27 residue. (F) Crystal structure of scDimer AA, with epitopes labeled as in panel A. Dotted lines represented areas with uncharacterized structures due to the flexibility of the regions. In (C) and (D), dotted lines indicated the lower limit of detection (LLD). Any value less than the LLD was assigned a value of 1⁄2 the LLD. Data were derived from two technical replicates of a single experiment, with bars indicating mean ± SD. P values were determined using Two-way ANOVA (ns indicated P > 0⋅05; * indicated P < 0⋅05; ** indicated P < 0⋅01, *** indicated P < 0⋅001, **** indicated P < 0⋅0001).
    Ds2 Vaccine, supplied by Moderna, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ds2+vaccine/ds2+vaccine/bio_rxiv__2025__05__31__655981-63-26-37
    Average 90 stars, based on 1 article reviews
    ds2 vaccine - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) Schematic diagram and design rationale of monomer A. The design of monomer A was outlined (top). Substitutions unique to monomer A and DS2 are labeled in black and gray, respectively. Substitutions shared among DS-Cav1, DS2, and monomer A are colored in red, and those shared between DS2 and monomer A are colored in blue. The dashed squares indicated the deleted residues. In the pre-F structure (PDB: 5k6i), Epitope I, II, III, IV, V, and Ø were labeled in magenta, green, purple, red, yellow, and blue, respectively and their neutralizing sensitivities are indicated. (B) Binding affinities of monomer A (top) and scDimer AA (bottom) with MAbs targeting six epitopes. Actual and fitted curves were represented by red and black lines, respectively. K D values were listed as mean ± SD of three experiments. (C) Endpoint titers of immunized antigen-binding IgG in murine sera were measured by ELISA. Groups of mice (n=4∼5) were intramuscularly immunized with 3 or 10 µg of monomer A or scDimer AA at 0, 3, and 6 weeks with Alhydrogel ® adjuvant. Serum samples were collected on day 56 (two weeks after the 3 rd immunization) and subjected for ELISA test. (D) Neutralization of RSV A2 strain in murine sera on day 56 was assessed. (E) Design of scDimer AA. Two truncated monomers A were tandemly linked, with the latter one starting at N27 residue. (F) Crystal structure of scDimer AA, with epitopes labeled as in panel A. Dotted lines represented areas with uncharacterized structures due to the flexibility of the regions. In (C) and (D), dotted lines indicated the lower limit of detection (LLD). Any value less than the LLD was assigned a value of 1⁄2 the LLD. Data were derived from two technical replicates of a single experiment, with bars indicating mean ± SD. P values were determined using Two-way ANOVA (ns indicated P > 0⋅05; * indicated P < 0⋅05; ** indicated P < 0⋅01, *** indicated P < 0⋅001, **** indicated P < 0⋅0001).

    Journal: bioRxiv

    Article Title: Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms

    doi: 10.1101/2025.05.31.655981

    Figure Lengend Snippet: (A) Schematic diagram and design rationale of monomer A. The design of monomer A was outlined (top). Substitutions unique to monomer A and DS2 are labeled in black and gray, respectively. Substitutions shared among DS-Cav1, DS2, and monomer A are colored in red, and those shared between DS2 and monomer A are colored in blue. The dashed squares indicated the deleted residues. In the pre-F structure (PDB: 5k6i), Epitope I, II, III, IV, V, and Ø were labeled in magenta, green, purple, red, yellow, and blue, respectively and their neutralizing sensitivities are indicated. (B) Binding affinities of monomer A (top) and scDimer AA (bottom) with MAbs targeting six epitopes. Actual and fitted curves were represented by red and black lines, respectively. K D values were listed as mean ± SD of three experiments. (C) Endpoint titers of immunized antigen-binding IgG in murine sera were measured by ELISA. Groups of mice (n=4∼5) were intramuscularly immunized with 3 or 10 µg of monomer A or scDimer AA at 0, 3, and 6 weeks with Alhydrogel ® adjuvant. Serum samples were collected on day 56 (two weeks after the 3 rd immunization) and subjected for ELISA test. (D) Neutralization of RSV A2 strain in murine sera on day 56 was assessed. (E) Design of scDimer AA. Two truncated monomers A were tandemly linked, with the latter one starting at N27 residue. (F) Crystal structure of scDimer AA, with epitopes labeled as in panel A. Dotted lines represented areas with uncharacterized structures due to the flexibility of the regions. In (C) and (D), dotted lines indicated the lower limit of detection (LLD). Any value less than the LLD was assigned a value of 1⁄2 the LLD. Data were derived from two technical replicates of a single experiment, with bars indicating mean ± SD. P values were determined using Two-way ANOVA (ns indicated P > 0⋅05; * indicated P < 0⋅05; ** indicated P < 0⋅01, *** indicated P < 0⋅001, **** indicated P < 0⋅0001).

    Article Snippet: DS-Cav1, a representative pre-F stabilized by introducing a disulfide bond and two cavity-filling substitutions, is adopted in the approved GSK protein-based vaccine, Arexvy., An enhanced version, DS2, with additional disulfide bonds and substitutions, was also adopted in Moderna’s licensed mRNA vaccine (mRNA-1345, mRESVIA).

    Techniques: Labeling, Binding Assay, Enzyme-linked Immunosorbent Assay, Adjuvant, Neutralization, Residue, Derivative Assay