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A disordered region retains the full protease inhibitor activity and the capacity to induce CD8⁺ T cells in vivo of the oral vaccine adjuvant U-Omp19.

ABSTRACT: U-Omp19 is a bacterial protease inhibitor from Brucella abortus that inhibits gastrointestinal and lysosomal proteases, enhancing the half-life and immunogenicity of co-delivered antigens. U-Omp19 is a novel adjuvant that is in preclinical development with various vaccine candidates. However, the molecular mechanisms by which it exerts these functions and the structural elements responsible for these activities remain unknown. In this work, a structural, biochemical, and functional characterization of U-Omp19 is presented. Dynamic features of U-Omp19 in solution by NMR and the crystal structure of its C-terminal domain are described. The protein consists of a compact C-terminal beta-barrel domain and a flexible N-terminal domain. The latter domain behaves as an intrinsically disorde

SUBMITTER: Laura Darriba M

PROVIDER: S-EPMC9486555 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Dataset Information

A disordered region retains the full protease inhibitor activity and the capacity to induce CD8⁺ T cells in vivo of the oral vaccine adjuvant U-Omp19.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

A disordered region retains the full protease inhibitor activity and the capacity to induce CD8+ T cells in vivo of the oral vaccine adjuvant U-Omp19.

OmicsDI is part of the ELIXIR infrastructure

Tweets

A disordered region retains the full protease inhibitor activity and the capacity to induce CD8⁺ T cells in vivo of the oral vaccine adjuvant U-Omp19.