TY - JOUR
T1 - Anti-idiotypic antibodies
T2 - Biological function and structural studies
AU - Pan, Ying
AU - Yuhasz, Stacieann C.
AU - Amzel, L. Mario
PY - 1995
Y1 - 1995
N2 - Under a variety of circumstances antibodies can be elicited against the variable region of other antibody molecules (anti-idotypic antibodies, anti- ids). Some of the antibodies are directed against the binding sites of the eliciting antibodies. Of particular interest are the antibodies that recognize epitopes of the original antibody that are in contact with antigen. Antibodies of this kind have been produced and used in a variety of situations including attempts at using them as therapeutic agents. In recent years structural data at the atomic level have emerged for anti-idiotypic antibodies from X-ray diffraction studies. These studies provided structural basis for molecular mimicry of anti-ids. For a large globular antigen (lysozyme), where epitope is noncontinuguous, molecular mimicry is not present at the atomic level. In this case, idiotopes are largely composed of CDR residues, but framework residues are also used. For an epitope that is sequence-specific (anti-FIPV system), molecular mimicry appears to be present as evidenced by the sequence homology between the CDR loops of the anti-id and the epitope of the original antigen. In the case of a small hormone antigen (angiotensin II), an internal image of the eliciting antigen appears to be represented in a single CDR loop of the antiiodiotypic antibody.
AB - Under a variety of circumstances antibodies can be elicited against the variable region of other antibody molecules (anti-idotypic antibodies, anti- ids). Some of the antibodies are directed against the binding sites of the eliciting antibodies. Of particular interest are the antibodies that recognize epitopes of the original antibody that are in contact with antigen. Antibodies of this kind have been produced and used in a variety of situations including attempts at using them as therapeutic agents. In recent years structural data at the atomic level have emerged for anti-idiotypic antibodies from X-ray diffraction studies. These studies provided structural basis for molecular mimicry of anti-ids. For a large globular antigen (lysozyme), where epitope is noncontinuguous, molecular mimicry is not present at the atomic level. In this case, idiotopes are largely composed of CDR residues, but framework residues are also used. For an epitope that is sequence-specific (anti-FIPV system), molecular mimicry appears to be present as evidenced by the sequence homology between the CDR loops of the anti-id and the epitope of the original antigen. In the case of a small hormone antigen (angiotensin II), an internal image of the eliciting antigen appears to be represented in a single CDR loop of the antiiodiotypic antibody.
KW - anti-idotype
KW - epitopes
KW - mimicry
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UR - http://www.scopus.com/inward/citedby.url?scp=0028798101&partnerID=8YFLogxK
U2 - 10.1096/fasebj.9.1.7821758
DO - 10.1096/fasebj.9.1.7821758
M3 - Review article
C2 - 7821758
AN - SCOPUS:0028798101
SN - 0892-6638
VL - 9
SP - 43
EP - 49
JO - FASEB Journal
JF - FASEB Journal
IS - 1
ER -