期刊
MOLECULAR SYSTEMS BIOLOGY
卷 8, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/msb.2011.101
关键词
bacteriophage lambda; host-virus; iron-sulfur clusters; programmed ribosomal frameshifting; tRNA modification
资金
- NIH [1DP1OD006413, 1F32GM090545]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [F32GM090545] Funding Source: NIH RePORTER
- NATIONAL LIBRARY OF MEDICINE [DP1LM011510] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [DP1OD006413] Funding Source: NIH RePORTER
Viral infection depends on a complex interplay between host and viral factors. Here, we link host susceptibility to viral infection to a network encompassing sulfur metabolism, tRNA modification, competitive binding, and programmed ribosomal frameshifting (PRF). We first demonstrate that the iron-sulfur cluster biosynthesis pathway in Escherichia coli exerts a protective effect during lambda phage infection, while a tRNA thiolation pathway enhances viral infection. We show that tRNA(Lys) uridine 34 modification inhibits PRF to influence the ratio of lambda phage proteins gpG and gpGT. Computational modeling and experiments suggest that the role of the iron-sulfur cluster biosynthesis pathway in infection is indirect, via competitive binding of the shared sulfur donor IscS. Based on the universality of many key components of this network, in both the host and the virus, we anticipate that these findings may have broad relevance to understanding other infections, including viral infection of humans. Molecular Systems Biology 8: 567; published online 31 January 2012; doi:10.1038/msb.2011.101
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