The Tape Measure Protein of the Staphylococcus aureus Bacteriophage vB_SauS-phiIPLA35 Has an Active Muramidase Domain

Rodríguez-Rubio, Lorena; Gutiérrez, Dolores; Martínez, Beatriz; Rodrı́guez, Ana; Götz, Friedrich; Garcı́a, Pilar

doi:10.1128/aem.01236-12

Cited by 25 publications

(16 citation statements)

References 19 publications

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“…In its C terminus, this predicted TMP contains a number of notable domains, including a LysM domain, which is known to bind peptidoglycan (42), and a transglycosylase (lytic transglycosylase [LT]) domain, which catalyzes peptidoglycan cleavage. The presence of peptidoglycan-binding and -degrading domains indicates that it plays an important, probably multifunctional role (in addition to determining tail length) in the phage infection process, similar to those described for coliphage T5 and Staphylococcus aureus phage vb_SauS-philPLA35 (43), where, for example, the T5 protein Pb2 performs tail length Ldl1, a New Group of L. delbrueckii Phages determination functions as well as possessing confirmed in vitro muralytic activity (44). HHPred analysis of the protein specified by ORF24 Ldl1 (located downstream of the TMP-encoding gene) reveals significant similarity to the distal tail protein (Dit) of Bacillus phage SPP1 (E value, 5.3EϪ23) and lactococcal phage TP901-1 (E value, 1.8EϪ20), and therefore, it is proposed to encode the central hub upon which the baseplate apparatus is assembled, as has been established for the Dit proteins of both the Bacillus and lactococcal phage models mentioned above.…”

Section: Resultssupporting

confidence: 57%

Novel Phage Group Infecting Lactobacillus delbrueckii subsp. lactis, as Revealed by Genomic and Proteomic Analysis of Bacteriophage Ldl1

Casey

Mahony

Neve

et al. 2015

Appl Environ Microbiol

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e Ldl1 is a virulent phage infecting the dairy starter Lactobacillus delbrueckii subsp. lactis LdlS. Electron microscopy analysis revealed that this phage exhibits a large head and a long tail and bears little resemblance to other characterized phages infecting Lactobacillus delbrueckii. In vitro propagation of this phage revealed a latent period of 30 to 40 min and a burst size of 59.9 ؎ 1.9 phage particles. Comparative genomic and proteomic analyses showed remarkable similarity between the genome of Ldl1 and that of Lactobacillus plantarum phage ATCC 8014-B2. The genomic and proteomic characteristics of Ldl1 demonstrate that this phage does not belong to any of the four previously recognized L. delbrueckii phage groups, necessitating the creation of a new group, called group e, thus adding to the knowledge on the diversity of phages targeting strains of this industrially important lactic acid bacterial species. L actobacillus delbrueckii subsp. lactis is a member of the lactic acid bacteria (LAB) and is commonly used in the production of commercial fermented milk products, such as Emmental-like cheeses, where it is employed as a starter culture contributing to the acidification and the organoleptic properties of the final product (1, 2). Bacteriophage (or phage) infection of these starter strains represents a major hurdle to their technological activity, as this may cause lysis of the starter, which in turn may lead to reduced acidification activity and a poor(er)-quality product, with a consequent negative economic impact (3).The commercial importance of L. delbrueckii fermentations has catalyzed extensive research into the occurrence, diversity, and impact of its infecting phages. Currently, L. delbrueckii phages are organized into four distinct groups (designated groups a, b, c, and d), classified based on DNA homology by hybridization (4-6) and, more recently, by comparative genome analysis (7). L. delbrueckii phages belonging to groups a and c have enjoyed considerable scientific scrutiny, with phage LL-H representing a prototype Lactobacillus phage. LL-H was originally isolated in 1972 (8), and its full genome sequence and transcriptional map, which revealed two distinct phases of transcription, have been determined (9). Furthermore, research on phage-host interactions, culminating in the identification of gp71 as the receptor-binding protein of LL-H (10) and lipoteichoic acids as the recognized receptor, have significantly advanced our understanding of this phage and the way in which it recognizes its host (11, 12). Also, the prolate-head, temperate phage JCL1032, being a member of group c L. delbrueckii phages, has been subjected to considerable scientific characterization, including genome sequencing (13), analysis of genomic integration (14), and identification of lipoteichoic acid as its receptor (12).Due to their apparent increased frequency of isolation, research has recently focused on group b phages, facilitated by the sequencing of six phages, c5 and LL-Ku (13); Ld3, Ld17, and Ld25A (7); and ph...

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Section: Resultssupporting

confidence: 57%

Novel Phage Group Infecting Lactobacillus delbrueckii subsp. lactis, as Revealed by Genomic and Proteomic Analysis of Bacteriophage Ldl1

Casey

Mahony

Neve

et al. 2015

Appl Environ Microbiol

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“…For some bacteriophages PG-hydrolysing domains have been observed in the tape measure proteins (TMPs) rather than VAPGHs (Fraser et al, 2007;Rodríguez-Rubio et al, 2012b), which suggests they might be involved in infection and DNA ejection into stationary phase cells (Piuri and Hatfull, 2006). In fact, a growing number of conserved domains are being recognized in other phage structural proteins that probably play roles in attachment to host cells through sugar binding or degradation of the polysaccharides on the cell surface (Fraser et al, 2007).…”

Section: Evolutionary Insightsmentioning

confidence: 98%

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Rodríguez-Rubio

Martínez

Donovan³

et al. 2012

Critical Reviews in Microbiology

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134

110

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Virion-associated peptidoglycan hydrolases (VAPGH) are phage-encoded lytic enzymes that locally degrade the peptidoglycan (PG) of the bacterial cell wall during infection. In contrast to endolysins, PGHs that mediate lysis of the host bacteria at the end of the lytic cycle to release of phage progeny, the action of VAPGHs generates a small hole through which the phage tail tube crosses the cell envelope to eject the phage genetic material at the beginning to the infection cycle. The antimicrobial activity of VAPGHs was first discovered through the observation of the phenomenon of 'lysis from without', in which the disruption of the bacterial cell wall occurs prior to phage production and is caused by a high number of phages adsorbed onto the cell surface. Based on a unique combination of properties of VAPGHs such as high specificity, remarkable thermostability, and a modular organization, these proteins are potential candidates as new antibacterial agents, e.g. against antibiotic-resistant bacteria in human therapy and veterinary as well as biopreservatives in food safety, and as biocontrol agents of harmful bacteria in agriculture. This review provides an overview of the different VAPGHs discovered to date and their potential as novel antimicrobials.

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“…These observations suggest that some effectors may be loaded into the Hcp tube during assembly of the T6SS structure and may be injected into target cells along with the tube. The effectors that reside in the Hcp tube in an unfolded conformation may also act analogously to phage tail “tape measure” proteins (Rodriguez-Rubio et al, 2012) and thus control the length of the extended (i.e., uncontracted) T6SS tail/tube complex.…”

Section: Effector Identification T6ss Secretion Recognition Signalsmentioning

confidence: 99%

A View to a Kill: The Bacterial Type VI Secretion System

Dong

Mekalanos

2014

Cell Host & Microbe

521

556

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The bacterial Type 6 Secretion System (T6SS) is an organelle that is structurally and mechanistically analogous to an intracellular membrane-attached contractile phage tail. Recent studies determined that a rapid conformational change in the structure of a sheath protein complex propels T6SS spike and tube components along with anti-bacterial and anti-eukaryotic effectors out of predatory T6SS+ cells and into prey cells. The contracted organelle is then recycled in an ATP-dependent process. T6SS is regulated at transcriptional and post-translational levels, the latter involving detection of membrane perturbation in some species. In addition to directly targeting eukaryotic cells, the T6SS can also target other bacteria co-infecting a mammalian host, highlighting the importance of the T6SS not only for bacterial survival in environmental ecosystems but also in the context of infection and disease. This review highlights these and other advances in our understanding of the structure, mechanical function, assembly, and regulation of the T6SS.

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The Tape Measure Protein of the Staphylococcus aureus Bacteriophage vB_SauS-phiIPLA35 Has an Active Muramidase Domain

Cited by 25 publications

References 19 publications

Novel Phage Group Infecting Lactobacillus delbrueckii subsp. lactis, as Revealed by Genomic and Proteomic Analysis of Bacteriophage Ldl1

Novel Phage Group Infecting Lactobacillus delbrueckii subsp. lactis, as Revealed by Genomic and Proteomic Analysis of Bacteriophage Ldl1

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

A View to a Kill: The Bacterial Type VI Secretion System

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