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Trans-Encapsidation of a Poliovirus Replicon By Different Picornavirus Capsid Proteins

  1. Author:
    Jia, X. Y.
    Vaneden, M.
    Busch, M. G.
    Ehrenfeld, E.
    Summers, D. F.

  2. Author Address

    Summers DF NCI FREDERICK CANC RES & DEV CTR NIH POB B BLDG 427 ROOM 10 FREDERICK, MD 21702 USA UNIV CALIF IRVINE DEPT MICROBIOL & MOL GENET IRVINE, CA 92697 USA UNIV CALIF IRVINE DEPT MOL BIOL & BIOCHEM IRVINE, CA 92697 USA
    1. Year: 1998
  2. Journal: Journal of Virology
    1. 72
    2. 10
    3. Pages: 7972-7977
  4. Type of Article: Article
  1. Abstract:

    A trans-encapsidation assay was established to study the specificity of picornavirus RNA encapsidation. A poliovirus replicon with the luciferase gene replacing the capsid protein-coding region was coexpressed in transfected HeLa cells with capsid proteins from homologous or heterologous virus. Successful tuans-encapsidation resulted in assembly and production of virions whose replication, upon subsequent infection of HeLa cells, was accompanied by expression of luciferase activity. The amount of luciferase activity was proportional to the amount of trans-encapsidated virus produced from the cotransfection. When poliovirus capsid proteins were supplied in trans, >2 x 10(6) infectious particles/ml were produced. When coxsackievirus B3, human rhinovirus 14, mengovirus, or hepatitis A virus (HAV) capsid proteins were supplied in trans, all but HAV showed some encapsidation of the replicon. The overall encapsidation efficiency of the replicon RNA by heterologous capsid proteins was significantly lower than when poliovirus capsid was used, trans-encapsidated particles could be completely neutralized with specific antisera against each of the donor virus capsids. The results indicate that encapsidation is regulated by specific viral nucleic acid and protein sequences. [References: 37]

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