Extended low-resolution structure of a Leptospira antigen offers high bactericidal antibody accessibility amenable to vaccine design.

ABSTRACT: Pathogens rely on proteins embedded on their surface to perform tasks essential for host infection. These obligatory structures exposed to the host immune system provide important targets for rational vaccine design. Here, we use a systematically designed series of multi-domain constructs in combination with small angle X-ray scattering (SAXS) to determine the structure of the main immunoreactive region from a major antigen from Leptospira interrogans, LigB. An anti-LigB monoclonal antibody library exhibits cell binding and bactericidal activity with extensive domain coverage complementing the elongated architecture observed in the SAXS structure. Combining antigenic motifs in a single-domain chimeric immunoglobulin-like fold generated a vaccine that greatly enhances leptospiral pro

SUBMITTER: Hsieh CL 

PROVIDER: S-EPMC5749957 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature