scholarly journals Lipid Intermediates in the Biosynthesis of Bacterial Peptidoglycan

2007 ◽  
Vol 71 (4) ◽  
pp. 620-635 ◽  
Author(s):  
Jean van Heijenoort
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Cytoplasmic Membrane ◽  
Monomer Unit ◽  
Mechanisms Of Action ◽  
Lipid Ii ◽  
Glycan Chain ◽  
Bacterial Peptidoglycan ◽  
Modified Forms ◽  
Enzymatic Methods

SUMMARY This review is an attempt to bring together and critically evaluate the now-abundant but dispersed data concerning the lipid intermediates of the biosynthesis of bacterial peptidoglycan. Lipid I, lipid II, and their modified forms play a key role not only as the specific link between the intracellular synthesis of the peptidoglycan monomer unit and the extracytoplasmic polymerization reactions but also in the attachment of proteins to the bacterial cell wall and in the mechanisms of action of antibiotics with which they form specific complexes. The survey deals first with their detection, purification, structure, and preparation by chemical and enzymatic methods. The recent important advances in the study of transferases MraY and MurG, responsible for the formation of lipids I and II, are reported. Various modifications undergone by lipids I and II are described, especially those occurring in gram-positive organisms. The following section concerns the cellular location of the lipid intermediates and the translocation of lipid II across the cytoplasmic membrane. The great efforts made since 2000 in the study of the glycosyltransferases catalyzing the glycan chain formation with lipid II or analogues are analyzed in detail. Finally, examples of antibiotics forming complexes with the lipid intermediates are presented.

scholarly journals The ColM Family, Polymorphic Toxins Breaching the Bacterial Cell Wall

mBio ◽  
2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Maarten G. K. Ghequire ◽  
Susan K. Buchanan ◽  
René De Mot
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Cytoplasmic Membrane ◽  
Catalytic Domain ◽  
Gram Negative Bacteria ◽  
Antibacterial Peptides ◽  
Gram Negative ◽  
Lipid Ii ◽  
Associated Proteins ◽  
Colicin M

ABSTRACT Bacteria host an arsenal of antagonism-mediating molecules to combat for ecologic space. Bacteriocins represent a pivotal group of secreted antibacterial peptides and proteins assisting in this fight, mainly eliminating relatives. Colicin M, a model for peptidoglycan-interfering bacteriocins in Gram-negative bacteria, appears to be part of a set of polymorphic toxins equipped with such a catalytic domain (ColM) targeting lipid II. Diversifying recombination has enabled parasitism of different receptors and has also given rise to hybrid bacteriocins in which ColM is associated with another toxin module. Remarkably, ColM toxins have recruited a diverse array of immunity partners, comprising cytoplasmic membrane-associated proteins with different topologies. Together, these findings suggest that different immunity mechanisms have evolved for ColM, in contrast to bacteriocins with nuclease activities.

scholarly journals Visualizing Conformation Transitions of the Lipid Flippase MurJ

2019 ◽  
Author(s):  
Alvin C. Y. Kuk ◽  
Aili Hao ◽  
Ziqiang Guan ◽  
Seok-Yong Lee
Keyword(s):  
Mass Spectrometry ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Structural Information ◽  
Conformational Transitions ◽  
Cell Wall Synthesis ◽  
Lipid Ii ◽  
Bacterial Peptidoglycan ◽  
Lipid Flippase ◽  
Conformation Transitions

AbstractThe biosynthesis of many polysaccharides, including bacterial peptidoglycan and eukaryotic N-linked glycans, requires transport of lipid-linked oligosaccharide (LLO) precursors across the membrane by specialized flippases. MurJ is the flippase for the lipid-linked peptidoglycan precursor Lipid II, a key player in bacterial cell wall synthesis, and a target of recently discovered antibacterials. However, the flipping mechanism of LLOs including Lipid II remains poorly understood due to a dearth of structural information. Here we report crystal structures of MurJ captured in inward-closed, inward-open, inward-occluded and outward-facing conformations. Together with cysteine accessibility, mass spectrometry, and complementation studies, we elucidate the conformational transitions in MurJ that mediate lipid flipping, identified the key ion for function, and provide a framework for the development of inhibitors.

scholarly journals Lipid Flippases for Bacterial Peptidoglycan Biosynthesis

2015 ◽  
Vol 8s1 ◽  
pp. LPI.S31783 ◽  
Author(s):  
Natividad Ruiz
Keyword(s):  
Cell Wall ◽  
The Body ◽  
Cellular Compartment ◽  
Peptidoglycan Biosynthesis ◽  
Lipid Ii ◽  
Common Strategy ◽  
Nucleotide Sugars ◽  
Membrane Bound ◽  
The Subject ◽  
Bacterial Peptidoglycan

The biosynthesis of cellular polysaccharides and glycoconjugates often involves lipid-linked intermediates that need to be translocated across membranes. Essential pathways such as N-glycosylation in eukaryotes and biogenesis of the peptidoglycan (PG) cell wall in bacteria share a common strategy where nucleotide-sugars are used to build a membrane-bound oligosaccharide precursor that is linked to a phosphorylated isoprenoid lipid. Once made, these lipid-linked intermediates must be translocated across a membrane so that they can serve as substrates in a different cellular compartment. How translocation occurs is poorly understood, although it clearly requires a transporter or flippase. Identification of these transporters is notoriously difficult, and, in particular, the identity of the flippase of lipid II, an intermediate required for PG biogenesis, has been the subject of much debate. Here, I will review the body of work that has recently fueled this controversy, centered on proposed flippase candidates FtsW, MurJ, and AmJ.

scholarly journals Specific Interaction of the Unmodified Bacteriocin Lactococcin 972 with the Cell Wall Precursor Lipid II

2008 ◽  
Vol 74 (15) ◽  
pp. 4666-4670 ◽  
Author(s):  
Beatriz Martínez ◽  
Tim Böttiger ◽  
Tanja Schneider ◽  
Ana Rodríguez ◽  
Hans-Georg Sahl ◽  
...  
Keyword(s):  
Cell Wall ◽  
Molecular Basis ◽  
Pore Formation ◽  
Cytoplasmic Membrane ◽  
Specific Interaction ◽  
Whole Cells ◽  
Lipid Ii ◽  
Inhibitory Spectrum

ABSTRACT Lactococcin 972 (Lcn972) is a nonlantibiotic bacteriocin that inhibits septum biosynthesis in Lactococcus lactis rather than forming pores in the cytoplasmic membrane. In this study, a deeper analysis of the molecular basis of the mode of action of Lcn972 was performed. Of several lipid cell wall precursors, only lipid II antagonized Lcn972 inhibitory activity in vivo. Likewise, Lcn972 only coprecipitated with lipid II micelles. This bacteriocin inhibited the in vitro polymerization of lipid II by the recombinant S. aureus PBP2 and the addition to lipid II of the first glycine catalyzed by FemX. These experiments demonstrate that Lcn972 specifically interacts with lipid II, the substrate of both enzymes. In the presence of Lcn972, nisin pore formation was partially hindered in whole cells. However, binding of Lcn972 to lipid II could not compete with nisin in lipid II-doped 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) liposomes, possibly indicating a distinct binding site. The existence of a putative cotarget for Lcn972 activity is discussed in the context of its narrow inhibitory spectrum and the localized action at the division septum. To our knowledge, this is the first unmodified bacteriocin that binds to the cell wall precursor lipid II.

scholarly journals Effect of a small molecule Lipid II binder on bacterial cell wall stress

2017 ◽  
Vol Volume 10 ◽  
pp. 69-73 ◽  
Author(s):  
Jakob Malin ◽  
Amol Shetty ◽  
Sean Daugherty ◽  
Erik de Leeuw
Keyword(s):  
Cell Wall ◽  
Small Molecule ◽  
Bacterial Cell ◽  
Wall Stress ◽  
Bacterial Cell Wall ◽  
Cell Wall Stress ◽  
Lipid Ii

scholarly journals Dissecting the Binding Interactions of Teixobactin with the Bacterial Cell‐Wall Precursor Lipid II

ChemBioChem ◽  
2019 ◽  
Vol 21 (6) ◽  
pp. 789-792 ◽  
Author(s):  
Sorina Chiorean ◽  
Isaac Antwi ◽  
Daniel W. Carney ◽  
Ioli Kotsogianni ◽  
Andrew M. Giltrap ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Binding Interactions ◽  
Lipid Ii

scholarly journals Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

2004 ◽  
Vol 186 (10) ◽  
pp. 3259-3261 ◽  
Author(s):  
Imke Wiedemann ◽  
Roland Benz ◽  
Hans-Georg Sahl
Keyword(s):  
Cell Wall ◽  
Pore Formation ◽  
Cytoplasmic Membrane ◽  
Lipid Membrane ◽  
Specific Interaction ◽  
Peptide Antibiotic ◽  
Black Lipid Membrane ◽  
Lipid Ii ◽  
Antibiotic Peptide

ABSTRACT The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.

scholarly journals Characterization of the Bifunctional Glycosyltransferase/Acyltransferase Penicillin-Binding Protein 4 of Listeria monocytogenes

2006 ◽  
Vol 188 (5) ◽  
pp. 1875-1881 ◽  
Author(s):  
Joanna Zawadzka-Skomiał ◽  
Zdzislaw Markiewicz ◽  
Martine Nguyen-Distèche ◽  
Bart Devreese ◽  
Jean-Marie Frère ◽  
...  
Keyword(s):  
Cell Wall ◽  
Listeria Monocytogenes ◽  
Chain Elongation ◽  
Lipid Ii ◽  
Food Borne ◽  
Glycan Chain ◽  
Chain Polymerization ◽  
Hydrolysis Of

ABSTRACT Multimodular penicillin-binding proteins (PBPs) are essential enzymes responsible for bacterial cell wall peptidoglycan (PG) assembly. Their glycosyltransferase activity catalyzes glycan chain elongation from lipid II substrate (undecaprenyl-pyrophosphoryl-N-acetylglucosamine-N-acetylmuramic acid-pentapeptide), and their transpeptidase activity catalyzes cross-linking between peptides carried by two adjacent glycan chains. Listeria monocytogenes is a food-borne pathogen which exerts its virulence through secreted and cell wall PG-associated virulence factors. This bacterium has five PBPs, including two bifunctional glycosyltransferase/transpeptidase class A PBPs, namely, PBP1 and PBP4. We have expressed and purified the latter and have shown that it binds penicillin and catalyzes in vitro glycan chain polymerization with an efficiency of 1,400 M−1 s−1 from Escherichia coli lipid II substrate. PBP4 also catalyzes the aminolysis (d-Ala as acceptor) and hydrolysis of the thiolester donor substrate benzoyl-Gly-thioglycolate, indicating that PBP4 possesses both transpeptidase and carboxypeptidase activities. Disruption of the gene lmo2229 encoding PBP4 in L. monocytogenes EGD did not have any significant effect on growth rate, peptidoglycan composition, cell morphology, or sensitivity to β-lactam antibiotics but did increase the resistance of the mutant to moenomycin.

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