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

Authors: Shewell, Lucy K; Ku, Shan C; Schulz, Benjamin L; Jen, Freda E-C; Mubaiwa, Tsitsi D; Ketterer, Margaret R; Apicella, Michael A; Jennings, Michael P

Published In Biochem Biophys Res Commun, (2013 Feb 08)

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 truncated, non-glycosylated, recombinant form of the AniA protein are capable of blocking nitrite reductase function in a whole cell assay. We propose that recombinant modified AniA has potential as a vaccine antigen for N. gonorrhoeae.

PubMed ID: 23313483

MeSH Terms: No MeSH terms associated with this publication