ArticleThe Journal of biological chemistry2014
Molecular dissection of phage endolysin: an interdomain interaction confers host specificity in Lysin A of Mycobacterium phage D29.
Article in The Journal of biological chemistry, 2014. 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, 50 citations in OpenAlex.
- Transmembrane delivery of antimicrobial peptides by engineered eCIS into macrophages for intracellular mycobacteria elimination.Science advances · 2026Article
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- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Elucidating the molecular properties and anti-mycobacterial activity of cysteine peptidase domain of D29 mycobacteriophage endolysin.Journal of virology · 2024Article
- Deciphering the molecular mechanism and regulation of formaldehyde detoxification inApplied and environmental microbiology · 2024Article
- An intramolecular cross-talk in D29 mycobacteriophage endolysin governs the lytic cycle and phage-host population dynamics.Science advances · 2024Article
- Isolation of a bacteriophage targeting Pseudomonas aeruginosa and exhibits a promising in vivo efficacy.AMB Express · 2023Article
- Bacteriophages of Mycobacterium tuberculosis, their diversity, and potential therapeutic uses: a review.BMC infectious diseases · 2022Review
- Molecular dissection of a dedicated formaldehyde dehydrogenase from Mycobacterium smegmatis.Protein science : a publication of the Protein Society · 2022Article
- Decoding the molecular properties of mycobacteriophage D29 Holin provides insights into Holin engineering.Journal of virology · 2021Article
- A positive SelectionFrontiers in bioengineering and biotechnology · 2021Article
- The GH19 Engineering Database: Sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19.PloS one · 2021Article
- Endolysins from AntarcticMarine drugs · 2020Article
- Functional characterization of the endolysins derived from mycobacteriophage PDRPxv.World journal of microbiology & biotechnology · 2020Article
- Deciphering the Role of Holin in Mycobacteriophage D29 Physiology.Frontiers in microbiology · 2020Article
- Separation ofFrontiers in microbiology · 2020Article
- Article
- Insights into the Physiology and Metabolism of a Mycobacterial Cell in an Energy-Compromised State.Journal of bacteriology · 2019Article
- MnoSR Is a Bona Fide Two-Component System Involved in Methylotrophic Metabolism in Mycobacterium smegmatis.Applied and environmental microbiology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis has always been recognized as one of the most successful pathogens. Bacteriophages that attack and kill mycobacteria offer an alternate mechanism for the curtailment of this bacterium. Upon infection, mycobacteriophages produce lysins that catalyze cell wall peptidoglycan hydrolysis and mycolic acid layer breakdown of the host resulting in bacterial cell rupture and virus release. The ability to lyse bacterial cells make lysins extremely significant. We report here a detailed molecular dissection of the function and regulation of mycobacteriophage D29 Lysin A. Several truncated versions of Lysin A were constructed, and their activities were analyzed by zymography and by expressing them in both Escherichia coli and Mycobacterium smegmatis. Our experiments establish that Lysin A harbors two catalytically active domains, both of which show E. coli cell lysis upon their expression exclusively in the periplasmic space. However, the expression of only one of these domains and the full-length Lysin A caused M. smegmatis cell lysis. Interestingly, full-length protein remained inactive in E. coli periplasm. Our data suggest that the inactivity is ensued by a C-terminal domain that interacts with the N-terminal domain. This interaction was affirmed by surface plasmon resonance. Our experiments also demonstrate that the C-terminal domain of Lysin A selectively binds to M. tuberculosis and M. smegmatis peptidoglycans. Our methodology of studying E. coli cell lysis by Lysin A and its truncations after expressing these proteins in the bacterial periplasm with the help of signal peptide paves the way for a large scale identification and analysis of such proteins obtained from other bacteriophages.
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Registered trials
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.