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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Elliott, S Articles by Hesterberg, L Search for Related Content PubMed PubMed Citation Articles by Elliott, S Articles by Hesterberg, L Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Fine-structure epitope mapping of antierythropoietin monoclonal antibodies reveals a model of recombinant human erythropoietin structure S Elliott, T Lorenzini, D Chang, J Barzilay, E Delorme, J Giffin and L Hesterberg Amgen Inc, Thousand Oaks, CA, USA. We have isolated and mapped the rHuEPO epitopes for three noncompeting anti-EPO monoclonal antibodies (MoAbs). The MoAb 9G8A recognizes a linear epitope that includes amino acids 13, 16, and 17. MoAb F12 recognizes a conformational epitope that includes amino acids 31 through 33, 86 through 91, and 138. MoAb D11 recognizes a conformational epitope that includes amino acids 64 through 78 and 99 through 110. MoAb D11 neutralizes rHuEPO activity which suggests that its epitope may contain the receptor binding domain. Analysis of the effect of mutations on folding allowed the identification of buried residues, alpha-helical, and non alpha-helical regions. This data along with epitope mapping data of anti rHuEPO monoclonals was used to model rHuEPO protein structure. A model consistent with the data is a 4-helix bundle with short and long interconnecting loops. Volume 87, Issue 7, pp. 2702-2713, 04/01/1996 Copyright © 1996 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: H. F. Bunn New agents that stimulate erythropoiesis Blood, February 1, 2007; 109(3): 868 - 873. [Abstract] [Full Text] [PDF] S. Tangri, B. R. Mothe, J. Eisenbraun, J. Sidney, S. Southwood, K. Briggs, J. Zinckgraf, P. Bilsel, M. Newman, R. Chesnut, et al. Rationally Engineered Therapeutic Proteins with Reduced Immunogenicity J. Immunol., March 15, 2005; 174(6): 3187 - 3196. [Abstract] [Full Text] [PDF] S. Elliott, D. Chang, E. Delorme, T. Eris, and T. Lorenzini Structural Requirements for Additional N-Linked Carbohydrate on Recombinant Human Erythropoietin J. Biol. Chem., April 16, 2004; 279(16): 16854 - 16862. [Abstract] [Full Text] [PDF] H. Qiu, A. Belanger, H.-W. P. Yoon, and H. F. Bunn Homodimerization Restores Biological Activity to an Inactive Erythropoietin Mutant J. Biol. Chem., May 1, 1998; 273(18): 11173 - 11176. [Abstract] [Full Text] [PDF] S. Elliott, T. Lorenzini, D. Chang, J. Barzilay, and E. Delorme Mapping of the Active Site of Recombinant Human Erythropoietin Blood, January 15, 1997; 89(2): 493 - 502. [Abstract] [Full Text] [PDF]

	Copyright © 1996 by American Society of Hematology         Online ISSN: 1528-0020