<scp>X</scp>‐ray structure of a superinfection exclusion lipoprotein from phage <scp>TP</scp>‐<scp>J</scp>34 and identification of the tape measure protein as its target

Bebeacua, Cecilia; Fajardo, Juan Carlos Lorenzo; Blangy, Stéphanie; Spinelli, S.; Bollmann, Stefanie; Neve, Horst; Cambillau, Christian; Heller, Knut J.

doi:10.1111/mmi.12267

Cited by 47 publications

(55 citation statements)

References 53 publications

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“…This large conformational change is probably somehow coupled to a signal to the stopper to open (26), releasing the dsDNA from the phage capsid. The dsDNA would in turn push out the TMP, which is suspected to guide delivery to the cytoplasm (54,63,64). In a majority of phages, the Tal protein harbors at its C terminus endolysin activity to digest the peptidoglycan and form a hole permitting the passage of the MTP and dsDNA at the onset of infection.…”

Section: Discussionmentioning

confidence: 99%

Structure, Adsorption to Host, and Infection Mechanism of Virulent Lactococcal Phage p2

Bebeacua

Tremblay

Farenc

et al. 2013

J Virol

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g Lactococcal siphophages from the 936 and P335 groups infect the Gram-positive bacterium Lactococcus lactis using receptor binding proteins (RBPs) attached to their baseplate, a large multiprotein complex at the distal part of the tail. We have previously reported the crystal and electron microscopy (EM) structures of the baseplates of phages p2 (936 group) and TP901-1 (P335 group) as well as the full EM structure of the TP901-1 virion. Here, we report the complete EM structure of siphophage p2, including its capsid, connector complex, tail, and baseplate. Furthermore, we show that the p2 tail is characterized by the presence of protruding decorations, which are related to adhesins and are likely contributed by the major tail protein C-terminal domains. This feature is reminiscent of the tail of Escherichia coli phage and Bacillus subtilis phage SPP1 and might point to a common mechanism for establishing initial interactions with their bacterial hosts. Comparative analyses showed that the architecture of the phage p2 baseplate differs largely from that of lactococcal phage TP901-1. We quantified the interaction of its RBP with the saccharidic receptor and determined that specificity is due to lower k off values of the RBP/saccharidic dissociation. Taken together, these results suggest that the infection of L. lactis strains by phage p2 is a multistep process that involves reversible attachment, followed by baseplate activation, specific attachment of the RBPs to the saccharidic receptor, and DNA ejection.

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Section: Discussionmentioning

confidence: 99%

Structure, Adsorption to Host, and Infection Mechanism of Virulent Lactococcal Phage p2

Bebeacua

Tremblay

Farenc

et al. 2013

J Virol

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“…Further Sie systems include the ltp gene of the Streptococcus thermophilus temperate phage TP-J34. This gene encodes a lipoprotein that inhibits DNA release into the host cell during infection with a lytic phage, presumably by targeting the phage-encoded tape measure protein (TMP), which is necessary for channel formation to allow DNA passage into the cell (20,21).…”

Section: Superinfection Exclusionmentioning

confidence: 99%

Evolutionary Ecology of Prokaryotic Immune Mechanisms

Houte

Buckling

Westra

2016

Microbiol Mol Biol Rev

217

177

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SUMMARYBacteria have a range of distinct immune strategies that provide protection against bacteriophage (phage) infections. While much has been learned about the mechanism of action of these defense strategies, it is less clear why such diversity in defense strategies has evolved. In this review, we discuss the short- and long-term costs and benefits of the different resistance strategies and, hence, the ecological conditions that are likely to favor the different strategies alone and in combination. Finally, we discuss some of the broader consequences, beyond resistance to phage and other genetic elements, resulting from the operation of different immune strategies.

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confidence: 99%

“…Another good example is the botulinum toxin encoded by Clostridium botulinum phages CE␤ and CE␥ (17). Yet some phages express membrane-associated or periplasmic proteins, such as Imm encoded by the Escherichia coli phage T4 (18) or LTP encoded by the S. thermophilus phage TP-J34 (19), that function as phage superinfection exclusion systems (for a review, see reference 20).Phage-host interactions have been extensively studied for E.coli and other species during a productive lytic infection, and multiple proteins have been shown to interfere with transcription, translation, or DNA replication (2,(21)(22)(23)(24)(25). On the other hand, phage-host interactions during lysogeny and the influence of prophages on host genes have not been investigated extensively (3,4,25,26).…”

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Global Transcriptional Response of Clostridium difficile Carrying the ϕCD38-2 Prophage

Sekulović

Fortier

2015

Appl Environ Microbiol

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Clostridium difficile is one of the most dangerous pathogens in hospital settings. Most strains of C. difficile carry one or more prophages, and some of them, like CD38-2 and CD119, can influence the expression of toxin genes. However, little is known about the global host response in the presence of a given prophage. In order to fill this knowledge gap, we used high-throughput RNA sequencing (RNA-seq) to conduct a genome-wide transcriptomic analysis of the epidemic C. difficile strain R20291 carrying the CD38-2 prophage. A total of 39 bacterial genes were differentially expressed in the R20291 lysogen, 26 of them being downregulated. Several of the regulated genes encode transcriptional regulators and phosphotransferase system (PTS) subunits involved in glucose, fructose, and glucitol/sorbitol uptake and metabolism. CD38-2 also upregulated the expression of a group of regulatory genes located in phi-027, a resident prophage common to most ribotype 027 isolates. The most differentially expressed gene was that encoding the conserved phase-variable cell wall protein CwpV, which was upregulated ϳ20-fold in the lysogen. Quantitative PCR and immunofluorescence showed that the increased cwpV expression results from a greater proportion of cells actively transcribing the gene. Indeed, ϳ95% of lysogenic cells express cwpV, as opposed to only ϳ5% of wild-type cells. Furthermore, the higher proportion of cells expressing cwpV results from a higher frequency of recombination of the genetic switch controlling phase variation, which we confirmed to be dependent on the host-encoded recombinase RecV. In summary, CD38-2 interferes with phase variation of the surface protein CwpV and the expression of metabolic genes. Bacteriophages (or simply phages) are the most abundant biological entities in the biosphere (1). Temperate phages have the ability to kill their host via a lytic replication cycle, but they can also establish a stable parasitic relationship with their host through a lysogenic cycle (2). Some phages, like , integrate into the chromosomes of their host via the expression of a phage-encoded integrase, while other prophages, like c-st and N15, are maintained as self-replicating circular or linear plasmids that are partitioned into dividing cells (3, 4). The maintenance of lysogeny has been extensively studied for and relies on the expression of a limited number of phage genes. For example, the CI repressor is constitutively expressed at low levels and plays a central role by repressing the initiation of transcription of lytic genes, thereby maintaining the prophage in a quiescent state (5).In principle, only a few genes should be required to maintain lysogeny, and therefore, most of the remaining prophage genome should be silent. Several studies with Lactobacillus, Bifidobacterium, and Streptococcus thermophilus support this (6-9). However, prophages are not always completely silent, and their transcriptional activity may depend on the growth conditions (10). In addition, several prophages encode "extra" genes that ar...

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X‐ray structure of a superinfection exclusion lipoprotein from phage TP‐J34 and identification of the tape measure protein as its target

Cited by 47 publications

References 53 publications

Structure, Adsorption to Host, and Infection Mechanism of Virulent Lactococcal Phage p2

Structure, Adsorption to Host, and Infection Mechanism of Virulent Lactococcal Phage p2

Evolutionary Ecology of Prokaryotic Immune Mechanisms

Global Transcriptional Response of Clostridium difficile Carrying the ϕCD38-2 Prophage

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