Shih HH, Tu C, Cao W, Klein A, Ramsey R, Fennell BJ, Lambert M, Ní Shúilleabháin D, Autin B, Kouranova E, Laxmanan S, Braithwaite S, Wu L, Ait-Zahra M, Milici AJ, Dumin JA, LaVallie ER, Arai M, Corcoran C, Paulsen JE, Gill D, Cunningham O, Bard J, Mosyak L, Finlay WJ. An ultra-specific avian antibody to phosphorylated tau protein reveals a unique mechanism for phosphoepitope recognition. J Biol Chem. 2012 Dec 28;287(53):44425-34. PubMed.
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CNRS
The authors describe the generation of novel avian antibodies against several phospho-epitopes of tau. Notably, they go far in the molecular characterization of an antibody recognizing the pThr231-Pro epitope. This antibody recognizes the tangles in AD-derived brain slices. A most interesting aspect of this paper is that it shows the conformation of the pThr231-Pro bond recognized by the Fab fragment. The conformation is in trans, thereby challenging the idea that this bond would be specifically in cis in AD tau, as proposed through the use of a cis-specific antibody (Nakamura et al., 2012).
References:
Nakamura K, Greenwood A, Binder L, Bigio EH, Denial S, Nicholson L, Zhou XZ, Lu KP. Proline isomer-specific antibodies reveal the early pathogenic tau conformation in Alzheimer's disease. Cell. 2012 Mar 30;149(1):232-44. PubMed.
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