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Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages.

Siponen M, Spinelli S, Blangy S, Moineau S, Cambillau C, Campanacci V
J Bacteriol 191 3220-5 (2009)
Cited: 23 times
EuropePMC logo PMID: 19286807

Abstract

Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry to manufacture cheeses, is subject to infection by a diverse population of virulent phages. We have previously determined the structures of three receptor binding proteins (RBPs) from lactococcal phages TP901-1, p2, and bIL170, each of them having a distinct host range. Virulent phages p2 and bIL170 are classified within the 936 group, while the temperate phage TP901-1 is a member of the genetically distinct P335 polythetic group. These RBPs comprise three domains: the N-terminal domain, binding to the virion particle; a beta-helical linker domain; and the C-terminal domain, bearing the receptor binding site used for host recognition. Here, we have designed, expressed, and determined the structure of an RBP chimera in which the N-terminal and linker RBP domains of phage TP901-1 (P335) are fused to the C-terminal RBP domain of phage p2 (936). This chimera exhibits a stable structure that closely resembles the parental structures, while a slight displacement of the linker made RBP domain adaptation efficient. The receptor binding site is structurally indistinguishable from that of native p2 RBP and binds glycerol with excellent affinity.

Articles - 3da0 mentioned but not cited (2)

  1. Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages. Siponen M, Spinelli S, Blangy S, Moineau S, Cambillau C, Campanacci V. J Bacteriol 191 3220-3225 (2009)
  2. α/β coiled coils. Hartmann MD, Mendler CT, Bassler J, Karamichali I, Ridderbusch O, Lupas AN, Hernandez Alvarez B. Elife 5 e11861 (2016)


Reviews citing this publication (8)

  1. A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries. Veesler D, Cambillau C. Microbiol Mol Biol Rev 75 423-33, first page of table of contents (2011)
  2. Structures and host-adhesion mechanisms of lactococcal siphophages. Spinelli S, Veesler D, Bebeacua C, Cambillau C. Front Microbiol 5 3 (2014)
  3. Molecular Basis of Bacterial Host Interactions by Gram-Positive Targeting Bacteriophages. Dunne M, Hupfeld M, Klumpp J, Loessner MJ. Viruses 10 (2018)
  4. Phage-Host Interactions of Cheese-Making Lactic Acid Bacteria. Mahony J, McDonnell B, Casey E, van Sinderen D. Annu Rev Food Sci Technol 7 267-285 (2016)
  5. Progress in lactic acid bacterial phage research. Mahony J, Bottacini F, van Sinderen D, Fitzgerald GF. Microb Cell Fact 13 Suppl 1 S1 (2014)
  6. Bacteriophage-host interactions as a platform to establish the role of phages in modulating the microbial composition of fermented foods. White K, Yu JH, Eraclio G, Dal Bello F, Nauta A, Mahony J, van Sinderen D. Microbiome Res Rep 1 3 (2022)
  7. Biodiversity of Phages Infecting the Dairy Bacterium Streptococcus thermophilus. Hanemaaijer L, Kelleher P, Neve H, Franz CMAP, de Waal PP, van Peij NNME, van Sinderen D, Mahony J. Microorganisms 9 1822 (2021)
  8. Phage Adsorption to Gram-Positive Bacteria. Leprince A, Mahillon J. Viruses 15 196 (2023)

Articles citing this publication (13)

  1. Crystal structure of bacteriophage SPP1 distal tail protein (gp19.1): a baseplate hub paradigm in gram-positive infecting phages. Veesler D, Robin G, Lichière J, Auzat I, Tavares P, Bron P, Campanacci V, Cambillau C. J Biol Chem 285 36666-36673 (2010)
  2. Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2. Bebeacua C, Tremblay D, Farenc C, Chapot-Chartier MP, Sadovskaya I, van Heel M, Veesler D, Moineau S, Cambillau C. J Virol 87 12302-12312 (2013)
  3. Crystal structure and function of a DARPin neutralizing inhibitor of lactococcal phage TP901-1: comparison of DARPin and camelid VHH binding mode. Veesler D, Dreier B, Blangy S, Lichière J, Tremblay D, Moineau S, Spinelli S, Tegoni M, Plückthun A, Campanacci V, Cambillau C. J Biol Chem 284 30718-30726 (2009)
  4. Structure and molecular assignment of lactococcal phage TP901-1 baseplate. Bebeacua C, Bron P, Lai L, Vegge CS, Brøndsted L, Spinelli S, Campanacci V, Veesler D, van Heel M, Cambillau C. J Biol Chem 285 39079-39086 (2010)
  5. Molecular insights on the recognition of a Lactococcus lactis cell wall pellicle by the phage 1358 receptor binding protein. Farenc C, Spinelli S, Vinogradov E, Tremblay D, Blangy S, Sadovskaya I, Moineau S, Cambillau C. J Virol 88 7005-7015 (2014)
  6. Lactococcal 936-type phages and dairy fermentation problems: from detection to evolution and prevention. Mahony J, Murphy J, van Sinderen D. Front Microbiol 3 335 (2012)
  7. Solution and electron microscopy characterization of lactococcal phage baseplates expressed in Escherichia coli. Campanacci V, Veesler D, Lichière J, Blangy S, Sciara G, Moineau S, van Sinderen D, Bron P, Cambillau C. J Struct Biol 172 75-84 (2010)
  8. Expanding the molecular toolbox for Lactococcus lactis: construction of an inducible thioredoxin gene fusion expression system. Douillard FP, O'Connell-Motherway M, Cambillau C, van Sinderen D. Microb Cell Fact 10 66 (2011)
  9. Cryo-electron microscopy structure of lactococcal siphophage 1358 virion. Spinelli S, Bebeacua C, Orlov I, Tremblay D, Klaholz BP, Moineau S, Cambillau C. J Virol 88 8900-8910 (2014)
  10. Classification of lytic bacteriophages attacking dairy Leuconostoc starter strains. Ali Y, Kot W, Atamer Z, Hinrichs J, Hinrichs J, Vogensen FK, Heller KJ, Neve H. Appl Environ Microbiol 79 3628-3636 (2013)
  11. Structure and Assembly of TP901-1 Virion Unveiled by Mutagenesis. Stockdale SR, Collins B, Spinelli S, Douillard FP, Mahony J, Cambillau C, van Sinderen D. PLoS One 10 e0131676 (2015)
  12. Identification of the receptor-binding protein in lytic Leuconostoc pseudomesenteroides bacteriophages. Kot W, Hammer K, Neve H, Vogensen FK. Appl Environ Microbiol 79 3311-3314 (2013)
  13. Bacteriophage functional genomics and its role in bacterial pathogen detection. Klumpp J, Fouts DE, Sozhamannan S. Brief Funct Genomics 12 354-365 (2013)


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