Epitope-specific focusing of the immune response to a minimized human chorionic gonadotropin analog.
Minimized proteins have long been used to elicit an immune response to particular regions of a protein antigen. Most efforts to derive minimized proteins have employed synthetic peptide fragments. This approach works well for linear epitopes but poorly for conformational epitopes. Here we describe a homodimeric human chorionic gonadotropin (hCG) analog that retains the conformation of related parts of hCG and elicits high affinity specific antibodies. This novel immunogen displays the tertiary structure of selected loops of the protein but lacks structures that could elicit potentially undesirable antibodies.
Ehrlich
P H
PH
Department of OBGYN, Department of Neuroscience and Cell Biology, Robert Wood Johnson (Rutgers) Medical School, 675 Hoes Lane, Piscataway, New Jersey, 08854, USA.
Bernard
M P
MP
Myers
R V
RV
Macdonald
G J
GJ
Moyle
W R
WR
D000595:Amino Acid Sequence; D000818:Animals; D000915:Antibody Affinity; D000917:Antibody Formation; D000918:Antibody Specificity; D006063:Chorionic Gonadotropin / Q000737:chemistry / Q000276:immunology*; D019281:Dimerization; D000939:Epitopes / Q000737:chemistry*; D006801:Humans; D007114:Immunization; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D006063:Chorionic Gonadotropin; D000939:Epitopes