Influence of helical organization on immunogenicity and antigenicity of synthetic peptides.
Using cooperative effects of different peptide structures synthesized in tandem, we have induced an alpha-helical structure in water solution on a peptide which, alone, is unorganized. This structure is particularly relevant in this case as the selected model protein (type 24 M protein of Streptococcus pyogenes) is an extended coiled-coil system. We were thus able to assess the importance of organization or unorganization of a unique amino acid sequence with regards to its immunogenicity and antigenicity. Although in a classical manner, antibodies cross-reacting with the protein can be obtained with the short, unorganized peptide, we demonstrate that conformation-specific antibodies are raised when longer, organized peptides are used as immunogens.
Service de Chimie des Biomolécules, Institut Pasteur de Lille, France.
H
H
Gras-Masse
M
M
Jolivet
H
H
Drobecq
J P
JP
Aubert
E H
EH
Beachey
F
F
Audibert
L
L
Chedid
A
A
Tartar
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000941:Antigens / Q000276:immunology*; D005260:Female; D051379:Mice; D010446:Peptide Fragments; D010455:Peptides / Q000276:immunology*; D011487:Protein Conformation; D014614:Vaccines, Synthetic / Q000276:immunology
D000906:Antibodies; D000941:Antigens; D010446:Peptide Fragments; D010455:Peptides; D014614:Vaccines, Synthetic