Reply to Kascsak: Definition of the PrP 3F4 Epitope Revisited
Year: 2010
Type: letter
Abstract: This is a response to a letter by Kascsak (1) We appreciate the comments of Richard Kascsak on our new study (2) and regret the omission of a paper by him and co-workers (3) in our references.The fundamental importance of their work on the 3F4 antibody was recognized by our citation of two of their other relevant papers (4,5).This reagent has greatly facilitated research on PrP and prion diseases.We fully agree with Dr. Kascsak that PrP residues Met 109 and Met 112 are contributory to the 3F4 epitope based on all observations including ours.We also offer the following responses to his other comments.Based on the absence of reactivity of 3F4 with 109 MKHM 112 and 107 TNMKHM 112 as observed by Lund et al. (6), we respectfully question whether TNMKHM is the "currently accepted" 3F4 epitope.We show that there is 3F4 immunoreactivity with 106 KTNMK 110 that lacks Met 112 (2), suggesting that these 5 residues constitute a minimal 3F4 epitope.In the Rubenstein paper from 1999 (3), the KTNMK reactivity might have been missed since peptides were evaluated only with low 3F4 concentrations.Nevertheless, Lys 106 proved to be a critical residue as evidenced by a marked reduction of 3F4 binding following its deletion in the 12-mer PrP peptide 107 (see Fig. 3 of Rubenstein et al. (3)), corroborating the conclusions of our study (2) as well as that of Lund et al. (6).
Source: Journal of Biological Chemistry
Authors: Wen-Quan Zou, Jan Langeveld, Xiangzhu Xiao, Shugui Chen, Patrick L. McGeer, Jue Yuan, Michael C. Payne, Hae-Eun Kang, John McGeehan, Man-Sun Sy, Neil S. Greenspan, David Kaplan, Gong-Xian Wang, Piero Parchi, Edward Hoover, Geoff Kneale, Glenn Telling, Witold K. Surewicz, Qingzhong Kong, Jian-Ping Guo
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2052222752