ArticleMicrobiology (Reading, England)2014
Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.
Article in Microbiology (Reading, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Elucidation of host and symbiont contributions to peptidoglycan metabolism based on comparative genomics of eight aphid subfamilies and their Buchnera.PLoS genetics · 2022Article
- Ethanol tolerance assessment in recombinant E. coli of ethanol responsive genes from Lactobacillus buchneri NRRL B-30929.World journal of microbiology & biotechnology · 2020Article
- Living the Sweet Life: HowFoods (Basel, Switzerland) · 2020Article
- Cell Wall Anchoring of a Bacterial Chitosanase inInternational journal of molecular sciences · 2020Article
- Lipoteichoic acid mediates binding of a Lactobacillus S-layer protein.Glycobiology · 2018Article
- False positives in using the zymogram assay for identification of peptidoglycan hydrolases.Analytical biochemistry · 2018Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- AcmB Is an S-Layer-Associated β-N-Acetylglucosaminidase and Functional Autolysin in Lactobacillus acidophilus NCFM.Applied and environmental microbiology · 2016Article
- The yajC gene from Lactobacillus buchneri and Escherichia coli and its role in ethanol tolerance.Journal of industrial microbiology & biotechnology · 2016Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Bacterial cell wall hydrolases are essential for peptidoglycan remodelling in regard to bacterial cell growth and division. In this study, peptidoglycan hydrolases (PGHs) of different Lactobacillus buchneri strains were investigated. First, the genome sequence of L. buchneri CD034 and L. buchneri NRRL B-30929 was analysed in silico for the presence of PGHs. Of 23 putative PGHs with different predicted hydrolytic specificities, the glycosyl hydrolase family 25 domain-containing homologues LbGH25B and LbGH25N from L. buchneri CD034 and NRRL B-30929, respectively, were selected and characterized in detail. Zymogram analysis confirmed hydrolysing activity on bacterial cell walls for both enzymes. Subsequent reversed-phase HPLC and MALDI-TOF MS analysis of the peptidoglycan breakdown products from L. buchneri strains CD034 and NRRL B-30929, and from Lactobacillus rhamnosus GG, which served as a reference, revealed that LbGH25B and LbGH25N have N-acetylmuramidase activity. Both enzymes were identified as cell wall-associated proteins by means of immunofluorescence microscopy and cellular fractionation, as well as by the ability of purified recombinant LbGH25B and LbGH25N to bind to L. buchneri cell walls in vitro. Moreover, similar secondary structures mainly composed of β-sheets and nearly identical thermal stabilities with Tm values around 49 °C were found for the two N-acetylmuramidases by far-UV circular dichroism spectroscopy. The functional and structural data obtained are discussed and compared to related PGHs. In this study, a major N-acetylmuramidase from L. buchneri was characterized in detail for the first time.
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