ArticleApplied and environmental microbiology2013
Mycobacteriophage Ms6 LysA: a peptidoglycan amidase and a useful analytical tool.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Transmembrane delivery of antimicrobial peptides by engineered eCIS into macrophages for intracellular mycobacteria elimination.Science advances · 2026Article
- LdtC Is a Key l,d-Transpeptidase for Peptidoglycan Assembly in Mycobacterium smegmatis.Journal of bacteriology · 2023Article
- Exploration of Synergistic Action of Cell Wall-Degrading Enzymes against Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2021Article
- Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.PloS one · 2021Article
- Exploring the Enzymatic and Antibacterial Activities of Novel Mycobacteriophage Lysin B Enzymes.International journal of molecular sciences · 2020Article
- Cell Wall Hydrolytic Enzymes Enhance Antimicrobial Drug Activity Against Mycobacterium.Current microbiology · 2019Article
- Review
- Two dd-Carboxypeptidases from Mycobacterium smegmatis Affect Cell Surface Properties through Regulation of Peptidoglycan Cross-Linking and Glycopeptidolipids.Journal of bacteriology · 2018Article
- Human NOD2 Recognizes Structurally Unique Muramyl Dipeptides from Mycobacterium leprae.Infection and immunity · 2016Article
- Antimycobacterial Activities of Endolysins Derived From a Mycobacteriophage, BTCU-1.Molecules (Basel, Switzerland) · 2015Article
- Molecular dissection of phage endolysin: an interdomain interaction confers host specificity in Lysin A of Mycobacterium phage D29.The Journal of biological chemistry · 2014Article
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
Since the peptidoglycan isolated from Mycobacterium spp. is refractory to commercially available murolytic enzymes, possibly due to the presence of various modifications found on this peptidoglycan, the utility of a mycobacteriophage-derived murolytic enzyme was assessed for an analysis of peptidoglycan from mycobacteria. We cloned, expressed, and purified the lysA gene product, a protein with homology to known peptidoglycan-degrading amidases, from bacteriophage Ms6. The recombinant protein was shown to cleave the bond between l-Ala and d-muramic acid of muramyl pentapeptide and to release up to 70% of the diaminopimelic acid present in the isolated mycobacterial cell wall. In contrast to lysozyme, which, in culture, inhibits the growth of both Mycobacterium smegmatis and Mycobacterium tuberculosis, LysA had no effect on the growth of either species. However, the enzyme is useful for solubilizing the peptide chains of isolated mycobacterial peptidoglycan for analysis. The data indicate that the stem peptides from M. smegmatis are heavily amidated, containing few free carboxylic acids, regardless of the cross-linking status.
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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.