Japanese Journal of Infectious Diseases
Online ISSN : 1884-2836
Print ISSN : 1344-6304
ISSN-L : 1344-6304
53 巻, 2 号
選択された号の論文の16件中1~16を表示しています
Reviews
Review
  • Michiaki Takahashi
    2000 年 53 巻 2 号 p. 47-55
    発行日: 2000/06/28
    公開日: 2025/03/17
    ジャーナル フリー

    Background of the development of a live varicella vaccine, including studies on the attenuation of measles and polioviruses, and transformation experiments of cultured hamster and human cells with conditional lethal mutants of adenovirus and herpes simplex virus were described. Varicella-zoster virus (Oka strain) was passaged in guinea pig cells, and the resulting virus (vaccine virus) was found to have a higher affinity to guinea pig cells. It was recently proved that variations of base sequence occurred exclusively in gene 62 (immediate-early gene) in comparison of vaccine Oka virus and parent Oka virus. This variation is presumed to have occurred during passage in guinea pig cells. Live varicella vaccine (Oka strain) has increasingly been used throughout the world. It was also found in a preliminary study that giving the vaccine to the elderly enhanced humoral and cell-mediated immunity, leading to a prevention of post herpetic neuralgia. A large field trial is now going on in the United States to immunize the elderly for the purpose of prevention of herpes zoster, particularly post herpetic neuralgia.

  • Takashi Onodera, Keiichi Saeki
    2000 年 53 巻 2 号 p. 56-61
    発行日: 2000/06/28
    公開日: 2025/03/17
    ジャーナル フリー

    Worldwide attention has been given to scrapie, because bovine spongiform encephalopathy (BSE) could be experimentally transmitted to sheep. This ovine form of BSE was clinically identical to scrapie. In Japanese scrapie cases, a majority of the diseased sheep were from Suffolk, while 8 cases were from Corriedale. It is very likely that sheep-to-sheep transmission of scrapie has taken place in Obihiro, Hokkaido. Normal prion protein may play a role in the morphoregulatory signaling pathway, which orchestrates the specificity of a particular cellular response. Over-expression of normal prion protein in mice cause neurodegenerative disorders. Recently, Prnd was identified downstream of the mouse prion protein gene (Prnp), and encodes 179 amino acids and a prion protein (PrP)-like protein designated doppel (Dpl). Dpl was upregulated in the central nervous system of two PrP-deficient lines of mice, as well as in prionless cell lines. Dpl caused neurodegeneration similar to that caused by PrP. Linked expression of Prnp and Prnd may cause several neurodegenerative disorders.

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