| Literature DB >> 26458390 |
Verónica A González-García1, Rebeca Bocanegra2, Mar Pulido-Cid1, Jaime Martín-Benito1, Ana Cuervo1, José L Carrascosa2.
Abstract
A specialized complex, the tail, is the most common strategy employed by bacterial viruses to deliver their genome without disrupting cell integrity. T7 has a short, non-contractile tail formed by a tubular structure surrounded by fibers. Recent studies showed that incubation of the virus with Escherichia coli lipopolysaccharides (LPS) resulted in complete delivery of the viral genome, demonstrating for the first time that LPS are the T7 receptor. Further screening of the bacterial envelope for proteinaceous compounds that affect T7 ejection showed that porins OmpA and OmpF affect viral particle adsorption and infection kinetics, suggesting that these proteins play a role in the first steps of virus-host interaction. Comparison of the structures before and after ejection showed the conformational changes needed in the tail for genome delivery. Structural similarities between T7 and other viruses belonging to the Podoviridae family suggests that they could also follow a similar DNA ejection mechanism.Entities:
Keywords: DNA ejection; Podoviridae; cryo-electron m; protein structure; tail complex
Year: 2015 PMID: 26458390 PMCID: PMC4589982 DOI: 10.1080/21597081.2015.1056904
Source DB: PubMed Journal: Bacteriophage ISSN: 2159-7073