What does this research mean for the field?

The multiply substituted G-H loop peptide from foot-and-mouth disease virus binds the neutralizing antibody 4C4 with a conformation similar to its unsubstituted counterpart via compensatory mechanisms stabilized by key water molecules. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

June 1, 2000Journal of General VirologyOpen Access

A multiply substituted G–H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules

Q: What is the clinical evidence from this study?

Study design: Other. Population: Foot-and-mouth disease virus (FMDV). Intervention: 15 amino acid synthetic peptide (G-H loop of VP1) complexed with Fab fragment of monoclonal antibody 4C4 vs. Unsubstituted synthetic peptide antigen. Primary outcome: Crystal structure at 2.3 A resolution and molecular-dynamic simulations.

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Key result

Multiply substituted FMDV G-H loop peptide binds antibody 4C4 like unsubstituted counterpart, stabilized by water.

Why the study?

The constancy of the structure of an antigenic domain despite multiple amino acid substitutions has implications for vaccine design.

Population

15 amino acid synthetic peptide from FMDV subtype C(1)

Comparison

Multiply substituted peptide vs unsubstituted synthetic peptide antigen

Design

Structural study with molecular-dynamic simulations

Authors

WOWendy F. OchoaNational University SKSusana G. KalkoVall d'Hebron Institut de Recerca PGPaula GomesUniversidade de São Paulo

Discussion

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Implication

Supports FMDV vaccine design via water-stabilized epitopes; leaves open broader applicability pending further validation.

Structured PICO

Population

15 amino acid synthetic peptide corresponding to the sequence of the major antigenic site A (G-H loop of VP1) from a multiple variant of foot-and-mouth disease virus (FMDV) subtype C(1)

Intervention

Complexation with the Fab fragment of the neutralizing monoclonal antibody 4C4

Comparator

Unsubstituted synthetic peptide antigen

Outcome

Crystal structure at 2.3 A resolutionsurrogate

The constancy of the structure of an antigenic domain despite multiple amino acid substitutions, facilitated by water molecules, has implications for vaccine design.

Cite This Study

Ochoa et al. (2000) studied Foot-and-mouth disease virus (FMDV). 15 amino acid synthetic peptide (G-H loop of VP1) complexed with Fab fragment of monoclonal antibody 4C4 vs. Unsubstituted synthetic peptide antigen was evaluated on Crystal structure at 2.3 A resolution and molecular-dynamic simulations. The multiply substituted G-H loop peptide from FMDV binds the neutralizing antibody 4C4 with a conformation similar to its unsubstituted counterpart, stabilized by a key water molecule.

synapsesocial.com/papers/6aaf2e2f84c19a519ba5efd5 https://doi.org/10.1099/0022-1317-81-6-1495

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A multiply substituted G–H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules

Discussion

Member takes

Implication

Structured PICO

Cite This Study

A multiply substituted G–H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider