The lytic cassette of mycobacteriophage Ms6 encodes an enzyme with lipolytic activity

Gil, Filipa; Catalão, Maria João; Moniz-Pereira, José; Leandro, Paula; McNeil, Michael; Pimentel, Madalena

doi:10.1099/mic.0.2007/014621-0

Cited by 53 publications

(86 citation statements)

References 30 publications

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“…In some phages, like and 21, the holin gene presents a dual-start motif producing two proteins by virtue of alternate translational starts, the holin and the antiholin, while in other phages these two proteins are encoded by separate genes (e.g., P1 and T4) (29,42). Such diversity is also observed in mycobacteriophages: in addition to the endolysin LysA, the majority of mycobacteriophages sequenced so far encodes an additional enzyme with lipolytic activity, LysB, that targets the outer membrane of mycobacteria (5,6). In phages belonging to cluster A2, like D29, the holin gene is positioned between lysA and lysB while in phages belonging to cluster F1, as in the Ms6 case, the holin gene is localized immediately downstream of lysB.…”

Section: Discussionmentioning

confidence: 96%

“…Even though the mechanisms underlying mycobacteriophage lysis of mycobacteria are poorly understood, recent work has contributed significantly to the progress in the field (2,5,6,14,25). Nonetheless, the exact mechanism by which the lysis effectors LysA and LysB are localized to their substrates remains elusive in the majority of the mycobacteriophages.…”

Section: Discussionmentioning

confidence: 99%

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Functional Analysis of the Holin-Like Proteins of Mycobacteriophage Ms6

et al. 2011

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The mycobacteriophage Ms6 is a temperate double-stranded DNA (dsDNA) bacteriophage which, in addition to the predicted endolysin (LysA)-holin (Gp4) lysis system, encodes three additional proteins within its lysis module: Gp1, LysB, and Gp5. Ms6 Gp4 was previously described as a class II holin-like protein. By analysis of the amino acid sequence of Gp4, an N-terminal signal-arrest-release (SAR) domain was identified, followed by a typical transmembrane domain (TMD), features which have previously been observed for pinholins. A second putative holin gene (gp5) encoding a protein with a predicted single TMD at the N-terminal region was identified at the end of the Ms6 lytic operon. Neither the putative class II holin nor the single TMD polypeptide could trigger lysis in pairwise combinations with the endolysin LysA in Escherichia coli. One-step growth curves and single-burst-size experiments of different Ms6 derivatives with deletions in different regions of the lysis operon demonstrated that the gene products of gp4 and gp5, although nonessential for phage viability, appear to play a role in controlling the timing of lysis: an Ms6 mutant with a deletion of gp4 (Ms6 ⌬gp4 ) caused slightly accelerated lysis, whereas an Ms6 ⌬gp5 deletion mutant delayed lysis, which is consistent with holin function. Additionally, cross-linking experiments showed that Ms6 Gp4 and Gp5 oligomerize and that both proteins interact. Our results suggest that in Ms6 infection, the correct and programmed timing of lysis is achieved by the combined action of Gp4 and Gp5.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Functional Analysis of the Holin-Like Proteins of Mycobacteriophage Ms6

et al. 2011

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“…In addition to the cytoplasmic membrane and the peptidoglycan cell wall, the envelope of the Rhodococcus and the other genera of the mycolata, a suprageneric taxon including Nocardia, Corynebacterium, and Mycobacterium, has a third layer comprised of an arabinogalactan polymer linked to an "outer membrane" of mycolic acid chains (70). Extrapolating from the lysis systems of mycobacteriophages, rhodococcal phages can be expected to encode not only the canonical holin and endolysin (LysA) lysis proteins but also an enzyme, LysB, that attacks this outer layer (21,22,54). The LysA and holin genes were readily identified as adjacent reading frames, gene10 and gene11 in Pepy6, and as a .…”

Section: Vol 77 2011 Genomic and Functional Analyses Of R Equi Phamentioning

confidence: 99%

Genomic and Functional Analyses of Rhodococcus equi Phages ReqiPepy6, ReqiPoco6, ReqiPine5, and ReqiDocB7

Summer

Liu

Gill

et al. 2011

Appl Environ Microbiol

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The isolation and results of genomic and functional analyses of Rhodococcus equi phages ReqiPepy6, ReqiDocB7, ReqiPine5, and ReqiPoco6 (hereafter referred to as Pepy6, DocB7, Pine5, and Poco6, respectively) are reported. Two phages, Pepy6 and Poco6, more than 75% identical, exhibited genome organization and protein sequence likeness to Lactococcus lactis phage 1706 and clostridial prophage elements. An unusually high fraction, 27%, of Pepy6 and Poco6 proteins were predicted to possess at least one transmembrane domain, a value much higher than the average of 8.5% transmembrane domain-containing proteins determined from a data set of 36,324 phage protein entries. Genome organization and protein sequence comparisons place phage Pine5 as the first nonmycobacteriophage member of the large Rosebush cluster. DocB7, which had the broadest host range among the four isolates, was not closely related to any phage or prophage in the database, and only 23 of 105 predicted encoded proteins could be assigned a functional annotation. Because of the relationship of Rhodococcus to Mycobacterium, it was anticipated that these phages should exhibit some of the features characteristic of mycobacteriophages. Traits that were identified as shared by the Rhodococcus phages and mycobacteriophages include the prevalent long-tailed morphology and the presence of genes encoding LysBlike mycolate-hydrolyzing lysis proteins. Application of DocB7 lysates to soils amended with a host strain of R. equi reduced recoverable bacterial CFU, suggesting that phage may be useful in limiting R. equi load in the environment while foals are susceptible to infection.Although the "tailed phage," or members of the virus order Caudovirales, constitute the majority of DNA diversity on the planet, the genomes of only a few hundred are known. Moreover, the genomic data that are available for bacteriophages are extremely unevenly distributed in terms of host species, with two-thirds derived from phages of only eight host genera or closely related bacterial species, including those belonging to the Staphylococcus, Mycobacterium, Pseudomonas, Lactococcus, and Burkholderia genera and the Enterobacteriaceae family (28). Nevertheless, some important themes have emerged from analyzing multiple phages that infect closely related host genera. One theme emerging is that despite rampant lateral gene transfer, there are recognizable "phage types" spanning geography and host taxa. Casjens (11a) was able to group 73 tailed-enterophage genomes into 13 phage types, the members of which were more closely related to each other by a number of criteria than they were to any member of another type. It should be noted that the classic enterophages do not include representatives of all phage types. When groups of phages from other host clades are sequenced, new phages and new phage types are identified. For example, among the sequenced phages of Burkholderia, there are members of the established , Mu, and P2 temperate phage types, as well as entirely new virulent phage types, such a...

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“…The lysis cassette of Marvin is coded near the middle of the genome, a common location for mycobacteriophage genomes, and includes lysin A (gp51), the holin protein (gp54), and a putative lysin B (gp53) (16,42) (Fig. 3).…”

Section: Resultsmentioning

confidence: 99%

Mycobacteriophage Marvin: a New Singleton Phage with an Unusual Genome Organization

Mageeney

Pope

Harrison

et al. 2012

J Virol

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bMycobacteriophages represent a genetically diverse group of viruses that infect mycobacterial hosts. Although more than 80 genomes have been sequenced, these still poorly represent the likely diversity of the broader population of phages that can infect the host, Mycobacterium smegmatis mc 2 155. We describe here a newly discovered phage, Marvin, which is a singleton phage, having no previously identified close relatives. The 65,100-bp genome contains 107 predicted protein-coding genes arranged in a noncanonical genomic architecture in which a subset of the minor tail protein genes are displaced about 20 kbp from their typical location, situated among nonstructural genes anticipated to be expressed early in lytic growth. Marvin is not temperate, and stable lysogens cannot be recovered from infections, although the presence of a putative xis gene suggests that Marvin could be a relatively recent derivative of a temperate parent. The Marvin genome is replete with novel genes not present in other mycobacteriophage genomes, and although most are of unknown function, the presence of amidoligase and glutamine amidotransferase genes suggests intriguing possibilities for the interactions of Marvin with its mycobacterial hosts.

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The lytic cassette of mycobacteriophage Ms6 encodes an enzyme with lipolytic activity

Cited by 53 publications

References 30 publications

Functional Analysis of the Holin-Like Proteins of Mycobacteriophage Ms6

Functional Analysis of the Holin-Like Proteins of Mycobacteriophage Ms6

Genomic and Functional Analyses of Rhodococcus equi Phages ReqiPepy6, ReqiPoco6, ReqiPine5, and ReqiDocB7

Mycobacteriophage Marvin: a New Singleton Phage with an Unusual Genome Organization

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