@article{oai:u-ryukyu.repo.nii.ac.jp:02015914,
 author = {Arakaki, Sakae and Makino, Yoshihiro and Tadano, Masayuki and Fukunaga, Toshihiko},
 issue = {1},
 journal = {琉球医学会誌 = Ryukyu Medical Journal},
 month = {},
 note = {We have constructed C-terminally truncated Japanese encephalitis virus envelope (E) proteins that ranged in length from 260 amino acids (a. a.) to 380 a. a. of the N-terminal sequence, using the baculovirus expression system, to analyze antigenic sites and examine basic conditions to keep a proper configuration of E protein. Truncated E proteins longer than 304 a. a. residues reacted with patients sera with sequential flavivirus infection, but failed to react with sera with primary flavivirus, even JE virus, infection. The E proteins of 279 a. a. or shorter residues did not react with sera from both patients with primary and sequential flavivirus infection. These results suggest that the main epitopes recognized during the secondary flavivirus infection are different from those recognized during the primary flavivirus infection, and also that existence of the fifth disulphide bond (a. a. #190 and a. a. #287) is involved in the reactivity of recombinant E proteins with patient sera in sequential flavivirus infection. Analysis of the length of expressed membrane (M) protein combined with E protein revealed that M proteins shorter than 37 a. a. residues failed to react with any of patient sera. This suggests that at least the C-terminal 37 a.a. residues of M protein is needed for the proper cleavage between M and E proteins., 論文},
 pages = {25--32},
 title = {[原著］Expression of Japanese Encephalitis Virus Envelope Protein by Baculovirus Expression System for the Analysis of Immunopathogenesis},
 volume = {14},
 year = {1994}
}