Foodborne Transmission of Bovine Spongiform Encephalopathy to Nonhuman Primates
Edgar Holznagel , Barbara Yutzy, Walter Schulz-Schaeffer, Carina Kruip, Uwe Hahmann, Pär Bierke, Juan-Maria Torres, Yong-Sun Kim, Achim Thomzig, Michael Beekes, Gerhard Hunsmann, and Johannes Loewer
Author affiliations: Paul-Ehrlich-Institut, Langen, Germany (E. Holznagel, B. Yutzy, C. Kruip, J. Loewer); University of Göttingen, Göttingen, Germany (W. Schulz-Schaeffer); German Primate Centre, Göttingen (U. Hahmann, G. Hunsmann); Swedish Institute for Infectious Disease Control, Solna, Sweden (P. Bierke); Centro de Investigación en Sanidad Animal, Madrid, Spain (J.-M. Torres); Hallym University, Anyang, Gyeonggi-Do, South Korea (Y.-S. Kim); Robert-Koch-Institut, Berlin, Germany (A. Thomzig, M. Beekes)
Figure 1. . Schematic diagram of the mature nonglycosylated prion protein and below amino acid sequences of the human and the simian prion polypeptide chain. Homology (198/207 aa) between human and simian mature cellular form of prion protein on the amino acid level is 96%. Large and small arrows indicate major and minor, respectively, proteinase K digestion sites (14). Open arrows indicate digestion sites in type 1 fragments; filled arrows indicate digestion sites in type 2 fragments. The epitopes recognized by the used monoclonal antibodies are shown below. OR, octarepeat region; H, α-helical structure; PK, proteinase K; M. fascicularis,Macaca fascicularis. *Swiss-Prot (www.ebi.ac.uk/swissprot/) accession numbers.
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