Bacteriophage T5 Structure Reveals Similarities with HK97 and T4 Suggesting Evolutionary Relationships

Effantin, Grégory; Boulanger, P.; Neumann, Emmanuelle; Letellìer, Lucienne; Conway, James F.

doi:10.1016/j.jmb.2006.06.081

Cited by 111 publications

(126 citation statements)

References 45 publications

(45 reference statements)

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“…CEV2 is both morphologically and genetically very similar to T5. 48,49 The infection kinetics of CEV2 are also similar to those observed under similar conditions for T5 infecting other E. coli strains, eclipse period of ~14 min, latent period ~39 min and burst size ~350 phage cell -1 . 50,51 Restriction enzyme digests of CEV2 DNA show that like T5 (in-silico digests using Genbank AY692264.1) it is susceptible to digestion by a broad range of the same enzymes in a similar but not identical E. coli O157:H7 is a minor and transient component of the ruminant gut, with colonized cattle shedding highly variable quantities for 30-60 d. Cattle can pick up the organism from each other, the surrounding farm/pen environment and contaminated water and feed.…”

Section: Discussionsupporting

confidence: 66%

“…[55][56][57] Our finding that CEV2 is a close relative of T5 is advantageous; T5-like phages are exclusively lytic and none have been found to encode pathogenicity islands, virulence/antibiotic resistance genes or integrases. 49,58 To our knowledge, CEV2 is the first T5-like phage to be isolated that infects E. coli O157:H7. Host selectivity is another important parameter in the selection of phages to include in therapeutic cocktails.…”

Section: Discussionmentioning

confidence: 99%

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Naturally resident and exogenously applied T4-like and T5-like bacteriophages can reduceEscherichia coliO157

et al. 2011

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Section: Discussionsupporting

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Naturally resident and exogenously applied T4-like and T5-like bacteriophages can reduceEscherichia coliO157

et al. 2011

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“…Although some RBPs are located at the tip of fibers (3), others belong to an elongated structure, the tail spike (4,5). In bacteriophages infecting the Gram ϩ bacterium Lactococcus lactis such as p2 (936 group), TP901-1, and Tuc2009 (P335 group), RBPs are part of a large organelle (1-2 MDa) termed the baseplate (BP).…”

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confidence: 99%

Structure and Molecular Assignment of Lactococcal Phage TP901-1 Baseplate

Bebeacua

Bron

Lai

et al. 2010

Journal of Biological Chemistry

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P335 lactococcal phages infect the Gram؉ bacterium Lactococcus lactis using a large multiprotein complex located at the distal part of the tail and termed baseplate (BP). The BP harbors the receptor-binding proteins (RBPs), which allow the specific recognition of saccharidic receptors localized on the host cell surface. We report here the electron microscopic structure of the phage TP901-1 wild-type BP as well as those of two mutants bppL ؊ and bppU ؊ , lacking BppL (the RBPs) or both peripheral BP components (BppL and BppU), respectively. We also achieved an electron microscopic reconstruction of a partial BP complex, formed by BppU and BppL. This complex exhibits a tripod shape and is composed of nine BppLs and three BppUs. These structures, combined with lightscattering measurements, led us to propose that the TP901-1 BP harbors six tripods at its periphery, located around the central tube formed by ORF46 (Dit) hexamers, at its proximal end, and a ORF47 (Tal) trimer at its distal extremity. A total of 54 BppLs (18 RBPs) are thus available to mediate host anchoring with a large apparent avidity. TP901-1 BP exhibits an infection-ready conformation and differs strikingly from the lactococcal phage p2 BP, bearing only 6 RBPs, and which needs a conformational change to reach its activated state. The comparison of several Siphoviridae structures uncovers a close organization of their central BP core whereas striking differences occur at the periphery, leading to diverse mechanisms of host recognition.The first steps of phage infection require interactions between the phage receptor-binding proteins (RBPs) 2 (1, 2) and the receptors at the host cell surface. Although some RBPs are located at the tip of fibers (3), others belong to an elongated structure, the tail spike (4, 5). In bacteriophages infecting the Gram ϩ bacterium Lactococcus lactis such as p2 (936 group), TP901-1, and Tuc2009 (P335 group), RBPs are part of a large organelle (1-2 MDa) termed the baseplate (BP). We previously solved RBP structures of phages p2 (6, 7) and TP901-1 (8) as well as the RBP C-terminal domain ("head domain") of phage bIL170 (936 group) (9). It appeared that the RBP of phage TP901-1 (termed BppL, lower baseplate protein) was cleaved during crystallization, and the polypeptidic chain in the crystal structure starts either at residue 16 or at residue 32 (10). Proteolytic cleavage was also observed for the homologous RBP from Tuc2009 (11) as well as in the structure of a chimeric RBP comprising the N-terminal and linker domains of phage TP901-1 RBP fused to the C-terminal domain of phage p2 RBP (12). We demonstrated that individually expressed Tuc2009 BppU (upper baseplate protein) and BppL did not interact when mixed, and we attributed this to the proteolytic cleavage of the BppL N terminus that should normally plug into BppU (13). In contrast, co-expression of BppU and BppL yielded a well defined 3:9 complex (13).The BP architecture of the P335 phages TP901-1 and Tuc2009 has been investigated thoroughly using mutagenesis and immuno...

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“…1 Nowadays considered a separate genus within the Siphoviridae family, T5-like phages are characterized by a 250 nm non-contractile flexible tail, attached to a 90 nm icosahedral capsid. 2 The capsid contains an approximately 120 kbp double-stranded (ds)DNA genome, the largest of the T-odd group (T1, T3, T5, and T7). 3 Other distinguishing features of T5 are the single-stranded interruptions (nicks) that occur at well-defined positions in its genome 3 and a unique two-step genome transfer mechanism that leads to transcription of pre-early genes before the remaining phage DNA has entered the host cell.…”

Section: Introductionmentioning

confidence: 99%

“…4 Although the T5-like bacteriophages have been classified as a separate genus, recent electron microscopy work has revealed similarities to T4 as well as Lambda-like phages, suggesting unexpected evolutionary relationships. 2 Interestingly, the resemblance to T4 extends beyond the mere morphological level: like T4, bacteriophage T5 encodes an ensemble of replication and recombination factors within a dedicated section of its genome, the so-called replication module. 5 Even though only a subset of these factors show obvious homology to T4 counterparts, the co-localization of the two types of genes in the replication module strongly suggests that T5 uses a recombination-dependent replication (RDR) mechanism similar to that of T4.…”

Section: Introductionmentioning

confidence: 99%

Identification of the ssDNA-binding protein of bacteriophage T5

Werten

2013

Bacteriophage

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Bacteriophage T5 Structure Reveals Similarities with HK97 and T4 Suggesting Evolutionary Relationships

Cited by 111 publications

References 45 publications

Naturally resident and exogenously applied T4-like and T5-like bacteriophages can reduceEscherichia coliO157

Naturally resident and exogenously applied T4-like and T5-like bacteriophages can reduceEscherichia coliO157

Structure and Molecular Assignment of Lactococcal Phage TP901-1 Baseplate

Identification of the ssDNA-binding protein of bacteriophage T5

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