ArticleJournal of bacteriology2011
Functional analysis of the holin-like proteins of mycobacteriophage Ms6.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- The peptidoglycan-binding domain regulates antimycobacterial activity of LysB by affecting its transportation and/or catalytic activity.Communications biology · 2026Article
- A systematic overexpression screen identifies cytotoxic genes encoded by the Cluster L1 mycobacteriophage LeBron.G3 (Bethesda, Md.) · 2026Article
- Identification and analysis of the crucial holin domain and sites and the bactericidal activity of a holin-endolysin lysis cassette from phage PZL-Ah152 againstJournal of virology · 2026Article
- Characterization of novel mycobacteriophages with a focus on phage Pisa4 and its interaction with human innate immune cells.Frontiers in microbiology · 2026Article
- Article
- Genome-wide screen overexpressing mycobacteriophage Amelie genes identifies multiple inhibitors of mycobacterial growth.G3 (Bethesda, Md.) · 2025Article
- Characterization of the novel cross-genus phage vB_SmaS_QH3 and evaluation of its antibacterial efficacy againstFrontiers in microbiology · 2025Article
- An intramolecular cross-talk in D29 mycobacteriophage endolysin governs the lytic cycle and phage-host population dynamics.Science advances · 2024Article
- Systematic overexpression of genes encoded by mycobacteriophage Waterfoul reveals novel inhibitors of mycobacterial growth.G3 (Bethesda, Md.) · 2022Article
- Getting Outside the Cell: Versatile Holin Strategies Used by Distinct Phages to Leave Their Bacillus thuringiensis Host.Journal of virology · 2022Article
- Article
- Decoding the molecular properties of mycobacteriophage D29 Holin provides insights into Holin engineering.Journal of virology · 2021Article
- Isolation and Characterization of vB_MsmS_Celfi: A NewPHAGE (New Rochelle, N.Y.) · 2021Article
- Application of a Novel Phage LPSEYT for Biological Control ofMicroorganisms · 2020Article
- Deciphering the Role of Holin in Mycobacteriophage D29 Physiology.Frontiers in microbiology · 2020Article
- Phage therapy as a renewed therapeutic approach to mycobacterial infections: a comprehensive review.Infection and drug resistance · 2019Article
- Phage Lysis: Multiple Genes for Multiple Barriers.Advances in virus research · 2019Review
- Review
- Enzymes and Mechanisms Employed by Tailed Bacteriophages to Breach the Bacterial Cell Barriers.Viruses · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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(Δgp4)) caused slightly accelerated lysis, whereas an Ms6(Δgp5) 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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.