Recombinant truncated AniA of pathogenic Neisseria elicits a non-native immune response and functional blocking antibodies.

ABSTRACT: AniA of the pathogenic Neisseria is glycosylated in its C-terminal repeat region by the pilin glycosylation (pgl) pathway. AniA appears to be unique among bacterial nitrite reductases as it contains an N-terminal extension that includes a lipid modification site as well as a C-terminal extension that is glycosylated. Immunising with various glycoforms of the AniA protein demonstrated a strong humoral immune response to the basal monosaccharide. In addition, when animals were immunised with a truncated form of AniA, completely lacking the glycosylated C-terminal region, the antibody response was directed against AniA regardless of the glycosylation state of the protein. Immuno-SEM confirmed that AniA is expressed on the cell surface in Neisseria gonorrhoeae. Antisera generated against a tru

SUBMITTER: Shewell LK 

PROVIDER: S-EPMC4326246 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature