Time-resolved DNA release from an O-antigen–specific Salmonella bacteriophage with a contractile tail
| Autor: | Udo Heinemann, Mareike S. Stephan, Dorothee Andres, Nina K. Broeker, Joachim Koetz, Angelo Valleriani, Stefanie Barbirz, Yvette Roske |
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| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Salmonella 030102 biochemistry & molecular biology biology Cell Biology biology.organism_classification Cleavage (embryo) medicine.disease_cause Biochemistry In vitro Bacteriophage 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology Structural biology chemistry Salmonella enterica ddc:570 medicine Biophysics Receptor Molecular Biology Institut für Biochemie und Biologie DNA |
| Zdroj: | Journal of Biological Chemistry. 294:11751-11761 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.ra119.008133 |
| Popis: | Myoviruses, bacteriophages with T4-like architecture, must contract their tails prior to DNA release. However, quantitative kinetic data on myovirus particle opening are lacking, although they are promising tools in bacteriophage-based antimicrobial strategies directed against Gram-negative hosts. For the first time, we show time-resolved DNA ejection from a bacteriophage with a contractile tail, the multi-O-antigen-specific Salmonella myovirus Det7. DNA release from Det7 was triggered by lipopolysaccharide (LPS) O-antigen receptors and notably slower than in noncontractile-tailed siphoviruses. Det7 showed two individual kinetic steps for tail contraction and particle opening. Our in vitro studies showed that highly specialized tailspike proteins (TSPs) are necessary to attach the particle to LPS. A P22-like TSP confers specificity for the Salmonella Typhimurium O-antigen. Moreover, crystal structure analysis at 1.63 angstrom resolution confirmed that Det7 recognized the Salmonella Anatum O-antigen via an E15-like TSP, DettilonTSP. DNA ejection triggered by LPS from either host showed similar velocities, so particle opening is thus a process independent of O-antigen composition and the recognizing TSP. In Det7, at permissive temperatures TSPs mediate O-antigen cleavage and couple cell surface binding with DNA ejection, but no irreversible adsorption occurred at low temperatures. This finding was in contrast to short-tailed Salmonella podoviruses, illustrating that tailed phages use common particle-opening mechanisms but have specialized into different infection niches. |
| Databáze: | OpenAIRE |
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