REVIEW: Antibodies as Specific Chaperones

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D. N. Ermolenko, A. V. Zherdev, and B. B. Dzantiev^*

Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia; fax: (7-095) 954-2804; E-mail: dzantiev@inbi.ras.ru

^* To whom correspondence should be addressed.

Received July 6, 2004

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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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KEY WORDS: antibodies, protein aggregation, folding, chaperones, inclusion bodies

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