The cell wall binding domain of <i>Listeria</i> bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid

Eugster, Marcel R.; Haug, Martina C.; Huwiler, Simona G.; Loessner, Martin J.

doi:10.1111/j.1365-2958.2011.07774.x

Cited by 93 publications

(115 citation statements)

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“…to gastrointestinal listeriosis in mice (Faith et al, 2009) (Table 1). In agreement with these findings the cell wall binding domain (CBD) of Listeria phage endolysin PlyP35 was found to recognize the GlcNAc residues on WTA (Eugster et al, 2011) (Table 1). However, this property does not seem to be a common feature of all Listeria phage endolysins (Eugster and Loessner, 2012).…”

Section: Role Of Wta Glycosylation In Other Gram-positive Bacteriasupporting

confidence: 71%

“…In particular tarM seems to be an ancient feature of S. aureus because the very early branching S. aureus clonal complex (CC) 75, sequence type (ST) 1850 strain MSHR1132 bears both, tarS and tarM in its genome (Holt et al, 2011) (Table 2) (Eugster et al, 2011), phage resistance (Tran et al, 1999) L. monocytogenes serotype 4b…”

Section: Tarm Is Absent In Several S Aureus Clonal Complexesmentioning

confidence: 99%

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Pathways and roles of wall teichoic acid glycosylation in Staphylococcus aureus

Winstel

Xia

Peschel

2014

International Journal of Medical Microbiology

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a b s t r a c tThe thick peptidoglycan layers of Gram-positive bacteria are connected to polyanionic glycopolymers called wall teichoic acids (WTA). Pathogens such as Staphylococcus aureus, Listeria monocytogenes, or Enterococcus faecalis produce WTA with diverse, usually strain-specific structure. Extensive studies on S. aureus WTA mutants revealed important functions of WTA in cell division, growth, morphogenesis, resistance to antimicrobials, and interaction with host or phages. While most of the S. aureus WTA-biosynthetic genes have been identified it remained unclear for long how and why S. aureus glycosylates WTA with ␣-or ␤-linked N-acetylglucosamine (GlcNAc). Only recently the discovery of two WTA glycosyltransferases, TarM and TarS, yielded fundamental insights into the roles of S. aureus WTA glycosylation. Mutants lacking WTA GlcNAc are resistant towards most of the S. aureus phages and, surprisingly, TarS-mediated WTA ␤-O-GlcNAc modification is essential for ␤-lactam resistance in methicillin-resistant S. aureus. Notably, S. aureus WTA GlcNAc residues are major antigens and activate the complement system contributing to opsonophagocytosis. WTA glycosylation with a variety of sugars and corresponding glycosyltransferases were also identified in other Gram-positive bacteria, which paves the way for detailed investigations on the diverse roles of WTA modification with sugar residues.

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Section: Role Of Wta Glycosylation In Other Gram-positive Bacteriasupporting

confidence: 71%

Section: Tarm Is Absent In Several S Aureus Clonal Complexesmentioning

confidence: 99%

Pathways and roles of wall teichoic acid glycosylation in Staphylococcus aureus

Winstel

Xia

Peschel

2014

International Journal of Medical Microbiology

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“…In addition to MurA and MurZ, there are three more UDP-GlcNAcconsuming enzymes present in L. monocytogenes (Fig. 6): (i) the essential MnaA protein (encoded by the lmo2537 gene) for the conversion of UDP-GlcNAc into UDP-N-acetylmannosamine, which is part of the teichoic acid linkage unit (26,27); (ii) the wall teichoic acid glycosylation protein GtcA (encoded by lmo2549) (28,29); and (iii) the glycosyltransferase encoded by the lmo2550 gene which is-as GtcAalso required for decoration of wall teichoic acids with GlcNAc (29). We assumed that-for the reasons described above-deletion of gtcA or lmo2550 possibly suppresses the ΔgpsB growth defects as well.…”

Section: Resultsmentioning

confidence: 99%

“…Inactivation of both genes suppressed the ΔgpsB growth defects, even though only partially. Both proteins consume UDP-GlcNAc for decoration of wall teichoic acids with GlcNAc (29), and their inactivation could cause an excess of intracellular UDP-GlcNAc. We assume that increased UDP-GlcNAc levels would have effects on peptidoglycan biosynthesis in ΔgpsB cells similar to those seen with induction of the UDP-GlcNAc 1-carboxyvinyltransferase MurA.…”

Section: Discussionmentioning

confidence: 99%

Suppressor Mutations LinkinggpsBwith the First Committed Step of Peptidoglycan Biosynthesis in Listeria monocytogenes

2017

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The cell division protein GpsB is a regulator of the penicillin binding protein A1 (PBP A1) in the Gram-positive human pathogen Listeria monocytogenes. Penicillin binding proteins mediate the last two steps of peptidoglycan biosynthesis as they polymerize and cross-link peptidoglycan strands, the main components of the bacterial cell wall. It is not known what other processes are controlled by GpsB. L. monocytogenes gpsB mutants are unable to grow at 42°C, but we observed that spontaneous suppressors correcting this defect arise on agar plates with high frequency. We here describe a first set of gpsB suppressors that mapped to the clpC and murZ genes. While ClpC is the ATPase component of the Clp protease, MurZ is a paralogue of the listerial UDP-N-acetylglucosamine (UDPGlcNAc) 1-carboxyvinyltransferase MurA. Both enzymes catalyze the enolpyruvyl transfer from phosphoenolpyruvate to UDP-GlcNAc, representing the first committed step of peptidoglycan biosynthesis. We confirmed that clean deletion of the clpC or murZ gene suppressed the ΔgpsB phenotype. It turned out that the absence of either gene leads to accumulation of MurA, and we show that artificial overexpression of MurA alone was sufficient for suppression. Inactivation of other UDP-GlcNAcconsuming pathways also suppressed the heat-sensitive growth of the ΔgpsB mutant, suggesting that an increased influx of precursor molecules into peptidoglycan biosynthesis can compensate for the lack of GpsB. Our results support a model according to which PBP A1 becomes misregulated and thus toxic in the absence of GpsB due to unproductive consumption of cell wall precursor molecules. IMPORTANCEThe late cell division protein GpsB is important for cell wall biosynthesis in Gram-positive bacteria. GpsB of the human pathogen L. monocytogenes interacts with one of the key enzymes of this pathway, penicillin binding protein A1 (PBP A1), and influences its activity. PBP A1 catalyzes the last two steps of cell wall biosynthesis, but it is unknown how GpsB controls PBP A1. We observed that a L. monocytogenes gpsB mutant forms spontaneous suppressors and have mapped their mutations to genes mediating and influencing the first step of cell wall biosynthesis, likely stimulating the influx of metabolites into this pathway. We assume that GpsB is important to ensure productive incorporation of cell wall precursors into the peptidoglycan sacculus by PBP A1.KEYWORDS GpsB, MurA, UDP-N-acetylglucosamine, PBP A1, peptidoglycan, UDP-N-acetylglucosamine T he cell wall represents the outmost layer of the bacterial envelope in Gram-positive bacteria. It confers rigidity and shape to their cells and provides a platform for incorporation of many molecules, e.g., proteins and wall teichoic acids, which need to be presented on the bacterial surface (1-3). The Gram-positive cell wall consists of a

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“…32 Cell wall binding of the endolysin is often necessary for bacteriolytic activity, 29,32,33 and endolysins often exhibit near species-specificity. 34,35 In rare cases endolysins can be serovar-specific, such as the L. monocytogenes phage endolysins Ply118 and Ply500 each unique to different serovars. 36,37 Endolysins with an intact CBD can also have a broad host range, such as with the streptococcal phage endolysin PlyC, which lyses several streptococcal species.…”

Section: Endolysins -Peptidoglycan Degrading Enzymesmentioning

confidence: 99%