Host cell proteins bind specifically to the capsid-cleaved 5' end of Leishmaniavirus RNA

Margarita Saiz, Young Tae Ro, Dyann F. Wirth, Jean L. Patterson

    Research output: Contribution to journalArticlepeer-review

    3 Scopus citations


    Leishmaniavirus (LRV) is a double-stranded RNA (dsRNA) virus that persistently infects some strains of the protozoan parasite, Leishmania. LRV generates a short transcript, corresponding to the 5' end of the positive-sense RNA (320 nt), via a cleavage event mediated by the viral capsid protein on the full-length positive sense RNA transcript. To address the possibility that the RNA cleavage represents a regulatory mechanism for maintaining persistent infection, the interactions between Leishmania cytoplasmic proteins and in vitro synthesized viral transcripts were studied. In gel mobility shift experiments, three specific RNA/protein complexes were formed between cellular proteins and the cleaved viral transcript, and three major proteins were labeled by UV cross-linking. No protein binding activity was observed for either the short (320 nt) or full-length RNA transcripts. However, the two cleavage reaction products were able to form stable RNA/RNA complexes. We present a model in which the virus is targeting its own transcript for cleavage to promote binding of host factors to cryptic domains inaccessible in the full-length transcript.

    Original languageEnglish (US)
    Pages (from-to)538-544
    Number of pages7
    JournalJournal of Biochemistry
    Issue number3
    StatePublished - 1999


    • Gel mobility shift
    • Leishmaniavirus
    • RNA transcript cleavage
    • RNA/protein complex

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology


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