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  • 标题:A unique variant of lymphocytic choriomeningitis virus that induces pheromone binding protein MUP: Critical role for CTL
  • 本地全文:下载
  • 作者:Brian C. Ware ; Brian C. Ware ; Brian M. Sullivan
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2019
  • 卷号:116
  • 期号:36
  • 页码:18001-18008
  • DOI:10.1073/pnas.1907070116
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Lymphocytic choriomeningitis virus (LCMV) WE variant 2.2 (v2.2) generated a high level of the major mouse urinary protein: MUP. Mice infected with LCMV WE v54, which differed from v2.2 by a single amino acid in the viral glycoprotein, failed to generate MUP above baseline levels found in uninfected controls. Variant 54 bound at 2.5 logs higher affinity to the LCMV receptor α-dystroglycan (α-DG) than v2.2 and entered α-DG–expressing but not α-DG–null cells. Variant 2.2 infected both α-DG–null or –expressing cells. Variant 54 infected more dendritic cells, generated a negligible CD8 T cell response, and caused a persistent infection, while v2.2 generated cytotoxic T lymphocytes (CTLs) and cleared virus within 10 days. By 20 days postinfection and through the 80-day observation period, significantly higher amounts of MUP were found in v2.2-infected mice. Production of MUP was dependent on virus-specific CTL as deletion of such cells aborted MUP production. Furthermore, MUP production was not elevated in v2.2 persistently infected mice unless virus was cleared following transfer of virus-specific CTL..
  • 关键词:pheromones ; MUP ; cytotoxic T lymphocytes (CTL) ; lymphocytic choriomeningitis virus (LCMV)
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