ArticleJournal of virology2000
The phage infection process: a functional role for the distal linker region of bacteriophage protein 3.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Generation of a helper phage for the fluorescent detection of peptide-target interactions by dual-display phages.Scientific reports · 2023Article
- High-Throughput Sequencing of Phage Display Libraries Reveals Parasitic Enrichment of Indel Mutants Caused by Amplification Bias.International journal of molecular sciences · 2021Article
- Bacteriophage-encoded virion-associated enzymes to overcome the carbohydrate barriers during the infection process.Applied microbiology and biotechnology · 2017Review
- The mechanism of bacterial infection by filamentous phages involves molecular interactions between TolA and phage protein 3 domains.Journal of bacteriology · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The filamentous bacteriophage infects Escherichia coli by interaction with the F pilus and the TolQRA complex. The virus-encoded protein initiating this process is the gene 3 protein (g3p). The g3p molecule can be divided into three different domains separated by two glycine-rich linker regions. Though there has been extensive evaluation of the importance of the diverse domains of g3p, no proper function has so far been assigned to these linker regions. Through the design of mutated variants of g3p that were displayed on the surface of bacteriophage, we were able to elucidate a possible role for the distal glycine-rich linker region. A phage that displayed a g3p comprised of only the N1 domain, the first linker region, and the C-terminal domain was able to infect cells at almost the same frequency as the wild-type phage. This infection was proven to be dependent on the motif between amino acid residues 68 and 86 (i.e., the first glycine-rich linker region of g3p) and on F-pilus expression.
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Registered trials
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