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Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda.

Campbell PL, Duda RL, Nassur J, Conway JF, Huet A
J Mol Biol 432 384-395 (2020)
Cited: 13 times
EuropePMC logo PMID: 31711962

Abstract

The long flexible tail tube of bacteriophage lambda connects its capsid to the tail tip. On infection, a DNA ejection signal is passed from the tip, along the tube to the capsid that triggers passage of the DNA down the tube and into the host bacterium. The tail tube is built from repeating units of the major tail protein, gpV, which has two distinctive domains. Its N-terminal domain has the same fold as proteins that form the rigid inner tubes of contractile tail phages, such as T4, and its C-terminal domain adopt an Ig-like fold of unknown function. We determined structures of the lambda tail tube in free tails and in virions before and after DNA ejection using cryoelectron microscopy. Modeling of the density maps reveals how electrostatic interactions and a mobile loop participate in assembly and also impart flexibility to the tube while maintaining its integrity. We also demonstrate how a common protein fold produces rigid tubes in some phages but flexible tubes in others.

Reviews - 6p3e mentioned but not cited (1)

  1. Major tail proteins of bacteriophages of the order Caudovirales. Zinke M, Schröder GF, Lange A. J Biol Chem 298 101472 (2022)

Articles - 6p3e mentioned but not cited (2)

  1. Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda. Campbell PL, Duda RL, Nassur J, Conway JF, Huet A. J Mol Biol 432 384-395 (2020)
  2. Tall tails: cryo-electron microscopy of phage tail DNA ejection conduits. Hardy JM, Dunstan RA, Lithgow T, Coulibaly F. Biochem Soc Trans 50 459-22W (2022)


Reviews citing this publication (1)

  1. Bacteriophages in nature: recent advances in research tools and diverse environmental and biotechnological applications. Bisen M, Kharga K, Mehta S, Jabi N, Kumar L. Environ Sci Pollut Res Int (2024)

Articles citing this publication (9)

  1. Architecture of the flexible tail tube of bacteriophage SPP1. Zinke M, Sachowsky KAA, Öster C, Zinn-Justin S, Ravelli R, Schröder GF, Habeck M, Lange A. Nat Commun 11 5759 (2020)
  2. Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation. Linares R, Arnaud CA, Effantin G, Darnault C, Epalle NH, Boeri Erba E, Schoehn G, Breyton C. Sci Adv 9 eade9674 (2023)
  3. A Mycobacteriophage-Based Vaccine Platform: SARS-CoV-2 Antigen Expression and Display. Freeman KG, Wetzel KS, Zhang Y, Zack KM, Jacobs-Sera D, Walters SM, Barbeau DJ, McElroy AK, Williams JV, Hatfull GF. Microorganisms 9 2414 (2021)
  4. A novel multifunctional anti-PD-L1-CD16a-IL15 induces potent cancer cell killing in PD-L1-positive tumour cells. Li Y, Wu L, Liu Y, Ma S, Huang B, Feng X, Wang H. Transl Oncol 21 101424 (2022)
  5. Structural Studies of the Phage G Tail Demonstrate an Atypical Tail Contraction. González B, Li D, Li K, Wright ET, Hardies SC, Thomas JA, Serwer P, Jiang W. Viruses 13 2094 (2021)
  6. Conformational dynamics control assembly of an extremely long bacteriophage tail tube. Agnello E, Pajak J, Liu X, Kelch BA. J Biol Chem 299 103021 (2023)
  7. In Situ Structures of the Ultra-Long Extended and Contracted Tail of Myoviridae Phage P1. Yang F, Wang L, Zhou J, Xiao H, Liu H. Viruses 15 1267 (2023)
  8. AT-specific DNA visualization revisits the directionality of bacteriophage λ DNA ejection. Bong S, Park CB, Cho SG, Bae J, Hapsari ND, Jin X, Heo S, Lee JE, Hashiya K, Bando T, Sugiyama H, Jung KH, Sung BJ, Jo K. Nucleic Acids Res 51 5634-5646 (2023)
  9. Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly. Xiao H, Tan L, Tan Z, Zhang Y, Chen W, Li X, Song J, Cheng L, Liu H. PLoS Biol 21 e3002441 (2023)


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