Journal
JOURNAL OF VIROLOGY
Volume 87, Issue 23, Pages 12745-12755Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02495-13
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Funding
- National Institutes of Health [R01GM79710]
- European Union [HEALTH-F3-2009-223101]
- National Institutes of Health/Department of Health and Human Services, Intramural Research program of the National Library of Medicine
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Although most of the 73 open reading frames (ORFs) in bacteriophage lambda have been investigated intensively, the function of many genes in host-phage interactions remains poorly understood. Using yeast two-hybrid screens of all lambda ORFs for interactions with its host Escherichia coli, we determined a raw data set of 631 host-phage interactions resulting in a set of 62 high-confidence interactions after multiple rounds of retesting. These links suggest novel regulatory interactions between the E. coli transcriptional network and lambda proteins. Targeted host proteins and genes required for lambda infection are enriched among highly connected proteins, suggesting that bacteriophages resemble interaction patterns of human viruses. Lambda tail proteins interact with both bacterial fimbrial proteins and E. coli proteins homologous to other phage proteins. Lambda appears to dramatically differ from other phages, such as T7, because of its unusually large number of modified and processed proteins, which reduces the number of host-virus interactions detectable by yeast two-hybrid screens.
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