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Antibodies as specific chaperones

Journal

BIOCHEMISTRY-MOSCOW
Volume 69, Issue 11, Pages 1233-1238

Publisher

MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1007/s10541-005-0069-4

Keywords

excitation-contraction coupling; ryanodine receptor; voltage-gated L-type Ca2+ channel; electron cryomicroscopy; single particle reconstruction

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Protein folding is often accompanied by formation of non-native conformations leading to protein aggregation. A number of reports indicate that antibodies can facilitate folding and prevent aggregation of protein antigens. The influence of antibodies on folding is strictly antigen specific. Chaperone-like antibody activity may be due to the stabilization of native antigen conformations or folding transition states, or screening of aggregating hydrophobic surfaces. Taking advantage of chaperone-like activity of antibodies for immunotherapy may prove to be a promising approach to the treatment of Alzheimer's and prion-related diseases. Antibody-assisted folding may enhance renaturation of recombinant proteins from inclusion bodies.

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