Open AccessPeptide Mimotopes ofNeisseria meningitidisGroup B Capsular Polysaccharide
Author(s) -
Inho Park,
In Hong Choi,
Se Jong Kim,
Jeon-Soo Shin
Publication year - 2004
Publication title -
yonsei medical journal/yonsei medical journal
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.702
H-Index - 63
eISSN - 1976-2437
pISSN - 0513-5796
DOI - 10.3349/ymj.2004.45.4.755
Subject(s) - mimotope , neisseria meningitidis , polysialic acid , epitope , microbiology and biotechnology , phage display , monoclonal antibody , immunogenicity , virology , antigen , neisseria , antibody , biology , bacteria , biochemistry , immunology , cell adhesion , genetics , neural cell adhesion molecule , cell
The antigenic similarity between Neisseria meningitidis group B (NMGB) capsular polysaccharide (PS) and human polysialic acid (PSA) has hampered the development of a NMGB PS-based vaccine. But the possibility of a safe vaccine based on NMGB PS has been demonstrated by the existence of the NMGB PS-associated nonautoreactive epitope, which is distinct from those present on human PSA. To obtain peptide mimotopes of NMGB PS, we used HmenB3, a protective and nonautoreactive monoclonal antibody, to screen a phage library with 12 amino acids. We obtained 23 phage clones that bound to HmenB3 but not in the presence of E. coli K1 PS [which is alpha(2-8)-linked PSA like NMGB PS]. The clones contained 3 mimotopes and differed from previously described NMGB PS mimotopes. Immunization with a synthetic peptide of one mimotope elicited anti-NMGB antibodies in BALB/c mice. These mimotopes may be useful in the development of group B meningococcal vaccines.