ジャーナル: J Virol / 年: 2025 タイトル: About bacteriophage tail terminator and tail completion proteins: structure of the proximal extremity of siphophage T5 tail. 著者: Romain Linares / Cécile Breyton / 要旨: Bacteriophages are viruses infecting bacteria. The vast majority of them bear a tail, allowing host recognition, cell wall perforation, and DNA injection into the host cytoplasm. Using electron cryo- ...Bacteriophages are viruses infecting bacteria. The vast majority of them bear a tail, allowing host recognition, cell wall perforation, and DNA injection into the host cytoplasm. Using electron cryo-microscopy (cryo-EM) and single particle analysis, we determined the organization of the tail proximal extremity of siphophage T5 that possesses a long flexible tail and solved the structure of its tail terminator protein p142 (TrP). It allowed us to confirm the common evolutionary origin between T5 TrP and other known or putative TrPs from siphophages, myophages, and bacterial tail-like machines, despite very poor sequence conservation. By also determining the structure of the T5 tail proximal extremity after interaction with T5 bacterial receptor FhuA, we showed that no conformational changes occur in TrP and confirmed that the infection signal transduction is not carried by the tube itself. We also investigated the location of T5 Neck1 or tail completion protein p143 (TCP) and showed, thanks to a combination of cryo-EM and structure prediction using Alphafold2, that it is not located at the capsid-to-tail interface as suggested by its position in the genome, but instead, very unexpectedly, on the side of T5 tail tip, and that it appears to be monomeric. Based on structure comparison with other putative TCPs predicted structures, this feature could not be shared by other TCPs and questions the affiliation of p143 to this family of protein.IMPORTANCEBacteriophages, viruses infecting bacteria, are the most abundant living entities on Earth. They are present in all ecosystems where bacteria develop and are instrumental in the regulation, diversity, evolution, and pathogeny of microbial populations. Moreover, with the increasing number of pathogenic strains resistant to antibiotics, virulent phages are considered a serious alternative or complement to classical treatments. 96% of all phages present a tail that allows host recognition and safe channeling of the DNA to the host cytoplasm. We present the atomic model of the proximal extremity of the siphophage T5 tail, confirming structural similarities with other phages. This structure, combined with results previously published and further explored, also allowed a review and a discussion on the role and localization of a mysterious tail protein, the tail completion protein, which is known to be present in the phage tails, but that was never identified in a phage structure.
凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 293.15 K / 装置: FEI VITROBOT MARK IV 詳細: 3 uL of T5 tails sample were deposited on a freshly glow discharged EM grid and plunge-frozen in nitrogen-cooled liquid ethane using a ThermoFisher Mark IV Vitrobot device (100 percent ...詳細: 3 uL of T5 tails sample were deposited on a freshly glow discharged EM grid and plunge-frozen in nitrogen-cooled liquid ethane using a ThermoFisher Mark IV Vitrobot device (100 percent humidity, 20 Celsius degrees, 5 s blotting time, blot force 0).
詳細
Pure T5 tails obtained by infecting E. coli F strain with the amber mutant phage T5D20am30d
ムービー
コントローラー
データを開く
基本情報
マップデータ
試料
キーワード
Escherichia phage T5 (ファージ)
データ登録者
フランス, 2件 
引用
構造の表示
ダウンロードとリンク
EMDBマップデータ形式
emd_51232.png
http://ftp.pdbj.org/pub/emdb/structures/EMD-51232
Z (Sec.)
Y (Row.)
X (Col.)
試料の構成要素
Escherichia coli (大腸菌) / 株: F
解析
電子顕微鏡法
FIELD EMISSION GUN
