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-Structure paper
タイトル | Visualizing Adsorption of Cyanophage P-SSP7 onto Marine Prochlorococcus. |
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ジャーナル・号・ページ | Sci Rep, Vol. 7, Page 44176, Year 2017 |
掲載日 | 2017年3月10日 |
著者 | Kazuyoshi Murata / Qinfen Zhang / Jesús Gerardo Galaz-Montoya / Caroline Fu / Maureen L Coleman / Marcia S Osburne / Michael F Schmid / Matthew B Sullivan / Sallie W Chisholm / Wah Chiu / |
PubMed 要旨 | Marine cyanobacteria perform roughly a quarter of global carbon fixation, and cyanophages that infect them liberate some of this carbon during infection and cell lysis. Studies of the cyanobacterium ...Marine cyanobacteria perform roughly a quarter of global carbon fixation, and cyanophages that infect them liberate some of this carbon during infection and cell lysis. Studies of the cyanobacterium Prochlorococcus MED4 and its associated cyanophage P-SSP7 have revealed complex gene expression dynamics once infection has begun, but the initial cyanophage-host interactions remain poorly understood. Here, we used single particle cryo-electron tomography (cryo-ET) to investigate cyanophage-host interactions in this model system, based on 170 cyanophage-to-host adsorption events. Subtomogram classification and averaging revealed three main conformations characterized by different angles between the phage tail and the cell surface. Namely, phage tails were (i) parallel to, (ii) ~45 degrees to, or (iii) perpendicular to the cell surface. Furthermore, different conformations of phage tail fibers correlated with the aforementioned orientations of the tails. We also observed density beyond the tail tip in vertically-oriented phages that had penetrated the cell wall, capturing the final stage of adsorption. Together, our data provide a quantitative characterization of the orientation of phages as they adsorb onto cells, and suggest that cyanophages that abut their cellular targets are only transiently in the "perpendicular" orientation required for successful infection. |
リンク | Sci Rep / PubMed:28281671 / PubMed Central |
手法 | EM (サブトモグラム平均) |
構造データ | EMDB-3131: EMDB-6427: |