ABSTRACT
Although most of the 73 open reading frames (ORFs) in bacteriophage λ 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.
FOOTNOTES
- Received 29 August 2013.
- Accepted 10 September 2013.
- Accepted manuscript posted online 18 September 2013.
- Address correspondence to Peter Uetz, peter{at}uetz.us.
↵* Present address: Stefan Wuchty, Department of Computer Science, University of Miami, Coral Gables, Florida, USA.
S.B. and S.W. contributed equally to this article.
Supplemental material for this article may be found at http://dx.doi.org/10.1128/JVI.02495-13.
- Copyright © 2013, American Society for Microbiology. All Rights Reserved.