Key result
5' S-isobutyl-adenosine reversibly blocks HSV-1 multiplication by inhibiting viral protein synthesis and mRNA methylation.
SIBA inhibits HSV-1 multiplication by blocking mRNA methylation, suggesting capping is essential for efficient viral translation.
Answers are grounded in this paper and cite their sources.
No clinical role for SIBA; leaves open whether mRNA cap inhibition merits antiviral development.
5' S-isobutyl-adenosine (SIBA), a structural analogue of S-adenosylhomocysteine, reversibly blocks the multiplication of herpes simplex type 1 virus. In the presence of SIBA, viral protein synthesis is inhibited. After removing SIBA the synthesis of proteins starts rapidly again. The new polypeptides are mainly alpha proteins (Honess and Roizman, J. Virol. 14:8-19, 1974,), normally the first to be synthesized after infection. The rapid synthesis of proteins after release of inhibition seems to be directed by mRNA formed in the presence of SIBA as indicated by experiments using actinomycin D but which was undermethylated as shown by analysis of methyl groups on RNA. SIBA inhibits the methylation of mRNA and especially that of the 5' cap. Capping of mRNA thus seems to be essential for efficient translation. The analogue affected various methylations to different extents.
No takes yet. Share an insight, caveat, or question.
Jacquemont et al. (1977) studied Herpes simplex virus type 1 infection (in vitro). 5' S-isobutyl-adenosine (SIBA) was evaluated on Viral protein synthesis and RNA methylation. 5' S-isobutyl-adenosine reversibly blocked the multiplication of herpes simplex type 1 virus by inhibiting viral protein synthesis and mRNA methylation, particularly of the 5' cap.
Synapse has enriched 10 related papers. Consider them for comparative context: