Peptidoglycan

The second class of PG hydrolases is an Due north-acetylmuramoyl-50-alanine amidase, a specific amidohydrolase that cleaves a critical amide bond betwixt the glycan moiety (MurNAc) and the peptide moiety (fifty-alanine) of the PG (Fig. 1C) This activity is associated more often with bacteriophage endolysins than autolysins or exolysins.

From: Advances in Virus Research , 2012

Peptidoglycan

Waldemar Vollmer , in Molecular Medical Microbiology (Second Edition), 2015

Peptidoglycan is an essential component of the bacterial prison cell envelope and protects the cell from bursting due to turgor and maintains cell shape. Equanimous of glycan chains connected by curt peptides, peptidoglycan forms a net-like macromolecule effectually the cytoplasmic membrane. At that place is meaning structural variation in the peptidoglycans of different bacteria. Pathogens alter the peptidoglycan to go resistant to lysozyme. Peptidoglycan carries covalently fastened cell surface components like teichoic acrid, capsular polysaccharide and cell wall proteins. Peptidoglycan precursors are synthesized in the cytoplasm and linked to a polyprenyl phosphate lipid for send across the cytoplasmic membrane. Presumably, peptidoglycan synthases and hydrolases form dynamic multi-enzyme complexes which polymerize new peptidoglycan and insert it into the existing cell wall, concomitant with the release of old textile. The peptidoglycan synthesis complexes are controlled by components of the bacterial cytoskeleton. Gram-negative leaner also regulate peptidoglycan synthesis by outer-membrane proteins.

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Imaging Bacterial Molecules, Structures and Cells

Y.-P. Hsu , ... M.S. VanNieuwenhze , in Methods in Microbiology, 2016

Abstract

Peptidoglycan is a rigid envelope surrounding the cytoplasmic membrane of almost bacterial species. Information technology helps protect bacterial cells from environmental stress and helps preserve cell morphology throughout their life cycle. Peptidoglycan biosynthesis is besides an important regulator of bacterial cell division. Since the discovery of penicillin, information technology has also been an important drug target for antibacterial discovery and evolution. As a result, a pregnant effort has been directed at expanding our cognition of peptidoglycan biosynthesis and dynamics. One approach directed towards this goal enables visualization of peptidoglycan structures in either alive or fixed cells. Recent advancements in microscopy have enabled scientists to study peptidoglycan structure, morphology, and organization at high resolution. In combination with structurally defined molecular probes, scientists are now able to perform highly specific, bioorthogonal probing of peptidoglycan structure and dynamics. In this chapter, nosotros volition survey peptidoglycan imaging techniques and hash out the findings obtained past these methods.

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Bacterial cell envelope peptidoglycan

Waldemar Vollmer , Petra Born , in Microbial Glycobiology, 2010

five. Conclusions

Peptidoglycan is responsible for the osmotic stability past encasing the cytoplasmic membrane of about bacteria. It is a unique, internet-similar polymer made of glycan strands which are cross-linked by unusual peptides. There is large variability in the structure of bacterial peptidoglycan due to differences in the amino acid sequence, types of cross-links and the presence or absenteeism of secondary modifications in both the glycan strands and peptides. High-resolution techniques have revealed loftier complexity in the fine construction of peptidoglycan, as well as compositional changes that occur when newly synthesized fabric matures. Sacculi from E. coli are highly elastic and have remarkably large pores allowing free diffusion of medium-sized proteins. The architecture of peptidoglycan cannot be adamant by the bachelor methods. Biophysical data support a model of a layered architecture in which the glycan strands are arranged in parallel to the cytoplasmic membrane. Further questions to be explored are detailed in the Research Focus Box.

Enquiry FOCUS BOX

The following major questions and tasks in peptidoglycan enquiry remain to be solved:

•

What is the molecular architecture of peptidoglycan? Is at that place a preferred direction of the glycan strands and peptides relative to the cell'southward centrality? Is the compages similar in Gram-positive and Gram-negative species?

•

How are other jail cell surface polymers like teichoic acids interlaced in the peptidoglycan network in Gram-positive species?

•

What is the part of modifications in the peptidoglycan structure? Are at that place other modifications in yet uncharacterized peptidoglycan structures? The fine structure of peptidoglycan is merely known in a few model bacteria but is unknown in nearly species.

•

Many enzymes responsible for peptidoglycan synthesis, hydrolysis and modification are poorly characterized.

•

What is the molecular growth mechanism of the peptidoglycan sacculus?

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Bacteriophages, Part B

Daniel C. Nelson , ... David M. Donovan , in Advances in Virus Research, 2012

Abstruse

Peptidoglycan (PG) is the major structural component of the bacterial cell wall. Bacteria accept autolytic PG hydrolases that allow the jail cell to grow and divide. A well-studied group of PG hydrolase enzymes are the bacteriophage endolysins. Endolysins are PG-degrading proteins that allow the phage to escape from the bacterial cell during the phage lytic bicycle. The endolysins, when purified and exposed to PG externally, can cause "lysis from without." Numerous publications have described how this phenomenon can be used therapeutically every bit an constructive antimicrobial against sure pathogens. Endolysins have a feature modular construction, often with multiple lytic and/or cell wall-binding domains (CBDs). They dethrone the PG with glycosidase, amidase, endopeptidase, or lytic transglycosylase activities and have been shown to exist synergistic with fellow PG hydrolases or a range of other antimicrobials. Due to the coevolution of phage and host, information technology is thought they are much less probable to invoke resistance. Endolysin engineering has opened a range of new applications for these proteins from food safety to ecology decontamination to more than effective antimicrobials that are believed refractory to resistance development. To put phage endolysin work in a broader context, this chapter includes relevant studies of other well-characterized PG hydrolase antimicrobials.

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Crustacean immune responses and their implications for disease control

L. Cerenius , K. Söderhäll , in Infectious Disease in Aquaculture, 2012

two.v.3 Recognition of peptidoglycans (PG)

PG are present in most bacterial cell walls. The known ability of PG to specifically trigger defense force in crustaceans has been enigmatic; so far no PG recognition proteins (PGRPs) have been detected in any crustacean EST collection or the merely consummate crustacean genome so far available (i.eastward. Dapnia pulex). PGRP genes are present in many other animals from insects to mammals. A crustacean PG blueprint-recognition protein was recently identified in freshwater crayfish by its PGN-binding adequacy and the recombinant protein produced to study its characteristics (Liu et al., 2011). The poly peptide, a 46   kDa serine proteinase homologue (named Pl-SPH2) is proteolytically candy to a xxx   kDa fragment. The 30   kDa fragment binds PG together with some other proteinase homologue (Pl-SPH1) and LGBP. If any of these are removed by RNAi, PG-triggered proPO-activation is abolished. This suggests that a complex consisting of SPH1, SPH2 and LGBP bound to the PG is responsible for mediating blueprint recognition of this important bacterial cell constituent in crayfish. This means that LGBP has a central part in pattern recognition, beingness involved in recognition of microbial components present in fungi, Gram-positive also as Gram-negative bacteria.

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Chemotaxonomic Features in the Bifidobacteriaceae Family

Paola Mattarelli , Barbara Sgorbati , in The Bifidobacteria and Related Organisms, 2018

v.2.1 Peptidoglycan Structure

Peptidoglycan (referred to also as murein) is the common cell wall component of most Gram-positive bacteria (about 30%–70% of the cell walls) and Gram-negative (only a modest component of the cell wall <x%) bacteria. Peptidoglycan is substantially equanimous of glycan strands consisting of repeats of β-ane,four-linked N-acetylglucosamine and N-acetylmuramic acid disaccharide units, cross-linked past short peptides. It is very important for physiological studies involving the mechanism of resistance to the antibiotics, phage susceptibility, and serological behavior and immune response (Schumann, 2011). The composition and structure of the peptidoglycan is rather abiding among Gram-negative bacteria, but widely differ amongst Gram-positive bacteria. Therefore, the nature of the interpeptide bridge of the prison cell-wall peptidoglycan is markedly involved in bacteral taxonomy and it has been widely studied for interspecies and intraspecies variations. The determination of these features does not necessarily require the purification of the consummate jail cell wall for all groups, focusing on the interpeptide span, which is considered an important taxonomic criterion.

The analysis of peptidoglycan has been performed on the total hydrolysate of the peptidoglycan by gas chromatography/mass spectrometry. Ii-dimensional thin-layer chromatography of the peptidoglycan partial hydrolysate has been finally utilized to determine the presence of different peptides [for details, see Schumann (2011)].

The peptidoglycan construction has been examined in about Bifidobacteriaceae species (54 taxa out of 60 taxa in the Bifidobacterium genus and in all the so-called scardovial genera). Gardnerella vaginalis prison cell wall contains major amounts of alanine, glycine, glutamic acid, and lysine unlike from all Bifidobacteriaceae species (O'Donnell et al., 1984). In the genus Bifidobacterium there are species where peptidoglycan structure is unique and is not shared with other species (east.g., peptidoglycan type A11.23, A11.25, A11.37); on the other hand, there are species that share the aforementioned peptidoglycan structure (Table 5.1). Concerning the subspecies in the genus Bifidobacterium, all have the same peptidoglycan structure of the type subspecies (e.g., B. longum subsp. longum, subsp. infantis, subsp. suis, and subsp. suillum share the same A21.3 structure) (Tabular array 5.1). Moreover, in the genus Bifidobacterium, the species usually cluster co-ordinate to their source, that is, the species derived from human and nonhuman primates cluster together (peptidoglycan type A11.11, A11.32, A21.3), whereas those from other animals have peptidoglycan blazon A11.1 and A11.31 (Table 5.1). Peptydoglycan structures are rather conservative, as many enzymes are involved in their complex syntheses, simply its significance as an evolutionary biomarker is not known. New insights can be obtained past deeper knowledge of peptidoglycan structural diversity in Bifidobacteriaceae species.

Table five.1. Peptidoglycan Type in the Genus Bifidobacterium and Scardovial Genera

Species Types of cross-linkages Peptidoglycan types No. of different peptidoglycan type in the DSMZ catalogue entries
B. asteroides, B. breve, B. reuteri, B. saguini A1α l-Lys-Gly A11.i
B. catenulatum, B. magnum, B. pseudocatenulatum, B. hapali A3α l-Lys(l-Orn)-50-Ala2-l-Ser A11.11
B. gallicum A3α l-Lys-50-Ala-l-Ser A11.thirteen detected in Weissella but non in bifidobacteria so far
B. minimum, B. biavatii, TRI 7, TRI 1, MRM 8.19 A3α l-Lys-50-Ser A11.14
B. scardovii A3α l-Lys-50-Ser-l-Ala A11.xviii detected in Oenococcus and Lactococcus but not in bifidobacteria and then far
B. animalis subsp. animalis and subsp. lactis, B. choerinum, B. cuniculi, B. ruminantium, TRE H A3α l-Lys(l-Orn)-l-Ser-(l-Ala)-l-Ala2 A11.21
B. eulemuris A3α l-Lys-l-Ser-50-Thr-l-Ala A11.23 is typical of several Arthrobacter simply not found in bifidobacteria and so far
B. aerophilum A3α l-Lys-50-Thr-l-Ala A11.25 detected in lactococci and streptococci merely not in bifidobacteria and so far
B. thermophilum A3α l-Orn(l-Lys)-d-Glu A11.26 detected in Arthobacter just not in bifidobacteria and then far
B. angulatum, B. coryneforme, B. gallinarum, B. indicum, B. mongoliense, B. pullorum, B. subtile A4α l-Lys-d-Asp A11.31
B. adolescentis, B. dentium, B. merycicum, B. saeculare, B. stellenboschense, B. callitrichos A4α l-Lys(fifty-Orn)-d-Asp A11.32
B. aesculapii A4α l-Lys-d-Ser-d-Asp A11.37 is typical of several Cellulosimicrobium but non found in bifidobacteria so far
B. boum A4α l-Lys-d-Ser-d-Glu A11.38
B. avesanii A4β l-Orn(Lys)-d-Ser-d-Glu Derived from A11.38
B. pseudolongum subsp. pseudolongum and subsp. globosum A3β l-Orn(L-Lys)-50-Ala2-3 A21.two
B. longum subsp. longum, subsp. infantis, subsp. suis,subsp. suillum, B. lemurum A3β l-Orn-l-Ser-l-Ala-fifty-Thr-fifty-Ala A21.3
TRE D, TRI 5 A3β l-Orn(Lys)-l-Ser-l-Ala-50-Thr-fifty-Ala Derived from A 21.3
Bifidobacterium ramosum A3β l-Orn-l-Ser-l-Ala Not detected in any organism so far
B. bifidum, B. myosotis A4β fifty-Orn-d-Ser-d-Asp A21.7
B. tsurumiense Glu-Lys-Asp-(Ala)two Not in the list of DSMZ
B. kashiwanohense, B. myosotis, B. tissieri Glu-Ala-Lys Not in the list of DSMZ
Scardovial genera
Alloscardovia macacae, A. omnicolens, Bombiscardovia coagulans A4α l-Lys-l-Asp A11.31
Alloscardovia criceti, Scardovia inopinata A4α l-Lys-d-Ser-d-Glu A11.38
Neoscardovia arbecensis A1γ meso-Dpm-direct A31
Pseuscardovia radai A4β 50-Orn(50-Lys)-d-Ser-d-Glu A21.12
Pseudoscardovia suis A3β fifty-Orn(fifty-Lys)-l-Ser(l-Ala)-l-Alaii —
Scardovia wiggsiae fifty-(Lys-Orn)-Thr-Glu (Downes et al., 2011)
A4α fifty-Lys-l-Thr-d-Glu (in the DSMZ web site) A11.57
Other genus
Gardnerella vaginalis Ala-Gly-Glu-Lys (O'Donnell et al., 1984) Non in the list of DSMZ

*B. aquikefiri, B. actynocoloniforme, B. bohemicum, B. bombi, B. district, B. crudilactis, B. faecale, B. psycraerophilum, B. thermacidophilum, Aeriscardovia aeriphila, and Parascardovia denticolens accept not been tested for peptidoglycan structure. In bold new bifidobacterial species under description isolated from tamarins (TRE H, TRE D, TRI one, TRI 5, TRI 7) and from common marmoset (MRM 8.19).

Knowledge almost peptidoglycan structures dates back to the 1970s–80s, but systematic analytical piece of work on peptidoglycans has not been continued after sequence analyses became a more exciting topic (Schumann 2011). Nevertheless, its importance in polyphasic taxonomy remains relevant (Mattarelli et al., 2014).

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Peptidoglycan (Murein)

M.A. de Pedro , in Encyclopedia of Microbiology (Third Edition), 2009

Peptidoglycan is a polymeric macromolecule made upwardly of linear glycan strands fastened to each other by peptide bridges. Peptidoglycan is polymerized at the external side of the cytoplasmic membrane in the class of a mesh-like, covalently closed layer surrounding the prison cell, the sacculus. The sacculus responsible for the physical strength of the cell envelope, is a primary morphogenetic element, and the target for a plethora of antibiotics. Peptidoglycan metabolism is complex and can be divided into four main aspects: biosynthesis of precursors, polymerization of monomers, incorporation of nascent polymers into the preexisting sacculus, and postinsertional modifications. Each of these aspects pose specific challenges to the cell.

Monomeric precursors are synthesized in the cytoplasm past a dedicated pathway, which ends providing activated monomers linked to the external side of the cytoplasmic membrane. A complex set of peptidoglycan synthases, including PBPs and peptidoglycan hydrolases, polymerize precursors, and insert nascent polymers into the turgor pressure level stressed, net-like sacculus to promote expansion of the structure and concomitant cell growth. The sacculus is in plough subjected to farther metabolic modifications in response to environmental and physiological conditions, including maturation, turnover, recycling, and adaptive responses. Actual state of knowledge on peptidoglycan metabolism is reviewed.

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Peptidoglycan biosynthesis and remodeling revisited

Moagi Shaku , ... Bavesh D. Kana , in Advances in Applied Microbiology, 2020

1 Introduction

The peptidoglycan (PG) layer of the bacterial cell wall is a protective polymer composed of cross-linked glycan strands, further cross-linked by peptide units. The PG covers the prison cell membrane serving equally an anchor for outer jail cell wall components such every bit teichoic acids and capsular polysaccharides ( Vollmer, Blanot, & De Pedro, 2008). While maintaining a certain degree of rigidity to enable the bacterial cell to withstand sufficient osmotic turgor, the PG is besides sufficiently fluid to facilitate cell growth, allow for improvidence of nutrients into the cell, and enable the secretion of extracellular proteins (Vollmer, Blanot, & De Pedro, 2008). Gram-negative bacteria synthesize a thin unmarried PG layer covered by an outer membrane while gram-positive leaner produce a thick multi-layer PG (Fig. 1). Our understanding of the processes required for PG biosynthesis has rapidly improved as a outcome of many studies of all the enzymes required for PG precursor biosynthesis from unlike bacterial species and the elucidation of the functions of two macromolecular enzyme complexes (the elongasome and divisome)—required for the incorporation of PG precursors into the existing PG structure to allow the cell to grow and carve up, respectively (Pazos & Peters, 2019). Moreover, recent studies using novel super resolution imaging techniques reporting on the interactions between different enzymes, with the power to detect conformational changes betwixt interacting proteins, have advanced the understanding of sub-cellular localization of protein complexes necessary for key cell bike processes. The development of avant-garde alive cell imaging techniques, coupled with PG labeling using metabolic probes and loftier throughput mutagenesis techniques, has enabled real-time spatial analysis of different processes associated with PG biosynthesis and remodeling. Some contempo applications of these techniques include findings in gram-negative bacteria highlighting that PG biosynthesis enzymes are regulated past novel outer-membrane co-factors and that these enzymes form singled-out complexes such every bit SEDS-PBP complexes that modulate PG biosynthesis dynamics. Additional examples include identification of phosphorelay mechanisms in gram-positive leaner linked to PG biosynthesis and how these serve major regulators of bacterial cell growth and division (Dörr, Moynihan, & Mayer, 2019).

Fig. 1

Fig. 1. Structure of the Gram-negative and Gram-positive cell wall. Gram-negative leaner form a thin unmarried PG layer covered past an outer membrane while gram-positive bacteria produce a thick multi-layer PG.

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Microbial glycosylated components in constitute disease

Max Dow , ... Mari-Anne Newman , in Microbial Glycobiology, 2010

4. Bacterial PG as a MAMP

Peptidoglycan is an essential and unique jail cell wall component of bacteria that imparts rigidity and construction to the bacterial envelope (come across Chapter 2). The PG from Staphylococcus aureus, a Gram-positive homo pathogen, and from the Gram-negative found pathogens, X. campestris pv. campestris and Agrobacterium tumefaciens, have been shown to induce a range of defence responses in leaves or prison cell pause cultures of A. thaliana (Gust et al., 2007; Erbs et al., 2008). These findings indicate that PG acts every bit a MAMP in plants, as information technology does in animals. Many of the plant responses observed are characteristic of those induced by other MAMPs and include PR-one induction, deposition of callose, acidification of the cell culture medium and induction of the oxidative burst. However, different the action of other MAMPs, no substantial calcium influx has been observed.

Differences are seen in the ability of PG or derived muropeptides from these contrasting pathogens to activate defence responses. Muropeptides from X. campestris pv. campestris are more constructive than native PG in triggering curt-term responses, eastward.g. generation of reactive oxygen species, suggesting that they are generally recognized earlier past the plant than native PG (Erbs et al., 2008). Muropeptides from Ten. campestris pv. campestris are likewise more efficient inducers of PR1 gene transcription than PG; approximately equivalent effects take been seen with 0.one   μg ml of muropeptides and 50   μg ml of intact PG (Erbs et al., 2008). Biologically active muropeptide fragments may exist generated by the turnover of PG that occurs continuously in leaner, or past enzymatic degradation by bifunctional chitinase/lysozyme enzymes from the host (Cloud-Hansen et al., 2006). The greater activity of muropeptides than native PG for X. campestris pv. campestris contrasts markedly with perception by A. thaliana of the Southward. aureus PG, where the converse effect was seen (Gust et al., 2007).

Fundamental chemical differences in PG from Gram-positive and Gram-negative organisms may explain the disparity in MAMP activities. Of note, PG consists of glycan chains of β-(1→iv)-linked-N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc). The presence of the lactyl group of the muramic acrid allows the covalent attachment of a short peptide stem that typically contains alternating l- and d-amino acids. The structure of the sugar backbone is generally conserved in all leaner, with different degrees of acetylation the but identified chemical variation. In dissimilarity, the peptide moiety displays considerable diversity. In full general, the third position amino acid in Gram-positive bacteria is l-lysine (Lys) while in Gram-negative bacteria information technology is meso-2,6-diaminopimelic (DAP) acrid. Furthermore, Gram-positive bacteria have peptide stems ordinarily cross-linked through an inter-peptide span, mostly glycine (Gly), whereas Gram-negative bacteria peptide stems are usually straight cross-linked.

The nature of the eliciting moiety inside PG is unknown. The weaker action of degradation products of PG from S. aureus compared to the native PG has led to speculation that the glycan backbone is the active elicitor moiety (Gust et al., 2007). Culling suggestions have come up from structural comparisons of muropeptides from A. tumefaciens, which are weak elicitors, with those from X. campestris pv. campestris, which are more effective (Erbs et al., 2008). These Gram-negative muropeptides differ by the presence of a Gly balance replacing alanine (Ala) in the case of Agrobacterium PG and by the lack of an acetyl group in X. campestris pv. campestris PG. There are only a few examples in which Gly is reported as a component of PG of Gram-negative leaner and no correlation with the biological activity has been reported (Vollmer et al., 2008). These variations might explain their different eliciting activities; chemical synthesis of these and related components should let this question to be addressed.

The amending of PG in Agrobacterium to reduce its effectiveness as a MAMP is redolent of the alteration of the lipid A moiety of LPSs in this genera, which may accept a similar effect on the ability of the lipid A to induce defences responses (see higher up). Furthermore, although flagellin from many bacteria is a potent MAMP, that from A. tumefaciens is non recognized in A. thaliana (Zipfel et al., 2006). This may reverberate the lifestyle of A. tumefaciens, which is a subtle pathogen dependent on maintaining viability of host cells for transfer of T-Dna and consequent nutritional benefits from the transformed host cells.

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Taxonomy of Prokaryotes

Peter Schumann , in Methods in Microbiology, 2011

I Introduction

Peptidoglycan (less usually referred to as 'murein') forms a mesh-like layer outside the cytoplasmic membrane, is responsible for rigidity and shape of bacterial cells and protects them from osmotic disruption. It is a polymer that occurs in cell walls of both Gram-positive and Gram-negative bacteria simply has not been found in Archaea. In Gram-positive bacteria it represents ca. thirty–70% of the cell wall too polysaccharides, teichoic or teichuronic acids. It is only a pocket-size component (<10%) in Gram-negative prison cell walls that mainly consist of lipopolysaccharides and lipoproteins. Since its offset assay, the peptidoglycan structure has received wide interest from those investigating the action of antibiotics and mechanisms of resistance, phage susceptibility and serological behaviour, allowed responses, and last but not the least for the classification and identification of bacteria. The assay of the peptidoglycan is hampered by the fact that it is a 3-dimensionally cross-linked, and hence an insoluble polymer that must be either hydrolysed to amino acids, peptides, and amino sugars or digested to muropeptides (Young, 1998) in order to conclude structural information from its constituents. This analytical approach requires conscientious purification from associated polymers as well equally cytoplasmic and membrane textile because many contaminating polymers may give rise to the same degradation products as those resulting from the peptidoglycan itself.

While Gram-negative bacteria are uniform in their peptidoglycan structure (Schleifer and Kandler, 1972), there is a bewildering diversity in the structure of peptidoglycans of Gram-positive bacteria (come across Table 1). For this reason, the peptidoglycan structure is an important taxonomic criterion for their differentiation. Pioneering work on the elucidation of the peptidoglycan structure dates dorsum to the 1960s (e.yard. Ghuysen, 1968; Schleifer and Kandler, 1967). The achievements of these studies and the relevance of the peptidoglycan diversity for bacterial taxonomy were summarized in the review of Schleifer and Kandler (1972). Methods for isolation of peptidoglycan and analyses of its structure for bacterial taxonomy are compiled in additional reviews (Hancock, 1994; Komagata and Suzuki, 1987; Rosenthal and Dziarski, 1994; Schleifer, 1985; Schleifer and Seidl, 1985). Information on the peptidoglycan structure is considered a recommended criterion for the description of new taxa of Gram-positive bacteria (Tindall et al., 2010), in item of members of the suborder Micrococcineae (Schumann et al., 2009), staphylococci (Freney et al., 1999) and aerobic endospore-forming bacteria (Logan et al., 2009). As currently only few laboratories worldwide are able to fulfil these requirements in all details, the aim of this chapter is to provide a ready of detailed and viable protocols for using contemporary techniques for the analysis of the peptidoglycan structure.

Table 1. Nomenclature of peptidoglycan structures of cross-linkage types A and B

Type A of cantankerous-linkage
  A11 A1α l-Lys-direct
  A11.gly A1α fifty-Lys-straight; α-carboxyl group of d-Glu substituted by Gly
  A11.pep A2 l-Lys peptide subunit
  A11.ane A3α l-Lys-Gly
  A11.ii A3α l-Lys-Gly5–6
  A11.3 A3α 50-Lys-Glytwo–iv-l-Serone–ii-Gly
  A11.4 A3α l-Lys-l-Ala
  A11.five A3α l-Lys-l-Ala2
  A11.vi A3α fifty-Lys-fifty-Ala3
  A11.7 A3α l-Lys-l-Ala4
  A11.8 A3α l-Lys-fifty-Ala-Glyfour–5
  A11.9 A3α fifty-Lys-l-Ala-fifty-Ala(50-Ser)
  A11.10 A3α l-Lys-l-Alatwo-fifty-Ala(50-Ser)
  A11.xi A3α 50-Lys(l-Orn)-fifty-Ala2-l-Ser
  A11.12 A3α fifty-Lys-fifty-Alatwo-Gly-50-Ala
  A11.13 A3α l-Lys-50-Ala-l-Ser
  A11.14 A3α l-Lys-l-Ser
  A11.fifteen A3α l-Lys-l-Ala2-l-Ser
  A11.16 A3α fifty-Lys-l-Ala(l-Ser)-l-Ser
  A11.17 A3α l-Lys-l-Ala-l-Thr-l-Ala
  A11.xviii A3α 50-Lys-l-Ser-fifty-Ala
  A11.19 A3α l-Lys-l-Ser-50-Ser(l-Ala)
  A11.twenty A3α fifty-Lys-l-Ser-fifty-Alatwo
  A11.21 A3α l-Lys(l-Orn)-l-Ala(l-Ser)-50-Ala2
  A11.22 A3α 50-Lys-fifty-Ser-l-Ala2–3; α-carboxyl group of d-Glu substituted by glycine amide
  A11.23 A3α fifty-Lys-l-Ser-l-Thr-l-Ala
  A11.24 A3α l-Lys-l-Thr-Gly
  A11.25 A3α l-Lys-fifty-Thr-fifty-Ala
  A11.26 A3α l-Lys-l-Thr-l-Ala; α-carboxyl group of d-Glu substituted by alanine amide
  A11.27 A3α l-Lys-l-Thr-l-Alaii
  A11.28 A3α 50-Lys-fifty-Thr-l-Alathree
  A11.29 A3α l-Lys-l-Thr-l-Ser(l-Ala)
  A11.30 A3α l-Lys-fifty-Thr-fifty-Ser-l-Ala2
  A11.31 A4α l-Lys-d-Asp
  A11.32 A4α l-Lys(l-Orn)-d-Asp
  A11.33 A4α 50-Lys-d-Glu
  A11.34 A4α fifty-Lys-l-Ala-d-Asp
  A11.35 A4α l-Lys-l-Ala-l-Glu
  A11.36 A4α fifty-Lys-l-Ser-d-Asp
  A11.37 A4α l-Lys-d-Ser-d-Asp
  A11.38 A4α fifty-Lys-d-Ser-d-Glu
  A11.39 A4α 50-Lys-l-Ser2-d-Glu
  A11.forty A4α l-Lys-Gly-d-Glu
  A11.41 A3α fifty-Lys-Gly-l-Ala3
  A11.42 A4α l-Lys-Gly-d-Asp
  A11.43 A4α l-Lys-d-Glu2
  A11.44 A3α l-Lys-Gly(l-Ser)
  A11.45 A4α 50-Lys-fifty-Thr-d-Asp
  A11.46 A3α 50-Lys-fifty-Ala-Gly-fifty-Ala2
  A11.47 A3α l-Lys-l-Ala-Gly; α-carboxyl group of d-Glu substituted by alanine amide
  A11.48 A4α l-Lys-l-Ser-d-Glu
  A11.49 A3α l-Lys-l-Ser-Gly
  A11.l A3α l-Lys-l-Ala-Gly
  A11.51 A5α l-Lys-50-Lys-d-Glu
  A11.52 A5α l-Lys-l-Lys-d-Asp
  A11.53 A5α l-Lys-fifty-Ala-l-Lys-d-Glu
  A11.54 A4α l-Lys-l-Glu
  A11.55 A5α l-Lys(50-Orn)-l-Lys-d-Glu
  A11.56 A4α 50-Lys-Gly-l-Glu
  A11.57 A4α l-Lys-50-Thr-d-Glu
  A11.58 A4α fifty-Lys-l-Ser-l-Glu
  A11.59 A4α l-Lys-l-Ala-d-Glu
  A11.60 A4α l-Lys-d-Asp; α-carboxyl group of d-Glu substituted by Gly
  A11.61 A3α 50-Lys-l-Ala(l-Ser)
  A11.62 A3α l-Lys-fifty-Ala2-Glyii–3-l-Ala(Gly)
  A11.63 A3α l-Lys-50-Ala-Gly3, l-Ser0–i
  A12.i A3α΄ a 50-Lys-Gly
  A12.2 A4α΄ l-Lys-d-Glu
  A12.3 A4α΄ l-Lys-Gly-d-Asp
  A12.4 A3α΄ l-Lys-fifty-Ser
  A21.1 A3β l-Orn-Gly2–iii
  A21.ii A3β l-Orn(50-Lys)-l-Ala2–3
  A21.3 A3β l-Orn-l-Ser-l-Ala-l-Thr-l-Ala
  A21.four A4β l-Orn-d-Asp
  A21.5 A4β l-Orn-d-Glu
  A21.6 A4β l-Orn(50-Lys)-d-Glu
  A21.vii A4β l-Orn-d-Ser-d-Asp
  A21.viii A4β l-Orn(50-Lys)-d-Ser-d-Asp
  A21.ix A4β l-Orn-l-Ser-d-Glu
  A21.ten A3β l-Orn-β-Ala
  A21.xi A5β fifty-Orn-l-Lys-d-Glu
  A21.12 A4β l-Orn-d-Ser-d-Glu
  A21.13 A4β l-Orn-Gly2-d-Glu
  A21.14 A4β 50-Orn-l-Ala-Gly-d-Asp
  A22.i A4β΄ l-Orn-d-Asp
  A23.1 A4β l-Orn-l-Glu; position 1 of the peptid subunit is fifty-Ser
  A31 A1γ meso-Dpm-directly b
  A31.one A4γ meso-Dpm-d-Glutwo
  A31.2 A4γ meso-Dpm-d-Glutwo; α-carboxyl group of d-Glu substituted by Gly
  A31.three A4γ meso-Dpm-d-Asp-d-Glu; α-carboxyl group of d-Glu substituted by Gly
  A32.1 A1γ΄ meso-Dpm-direct
  A41.1 A3γ LL-Dpm-Gly
  A41.2 A3γ LL-Dpm-Gly3; α-carboxyl grouping of d-Glu substituted by Gly
  A42.ane A3γ΄ LL-Dpm-Gly
  A51 A1δ Lan-straight
Type B of cross-linkage
  B1 B1α {Gly} [l-Lys] d-Glu(Hyg)-Gly-l-Lys c
  B2 B1β {Gly} [l-Hse] d-Glu(Hyg)-Gly2-l-Lys
  B3 B1γ {Gly} [l-Glu] d-Glu(Hyg)-Gly2-l-Lys
  B4 B2α {l-Ser} [l-Orn] d-Glu-d-Lys(d-Orn)
  B5 B2β {Gly} [l-Hse] d-Glu-d-Orn
  B6 B2β {Gly} [l-Hse] d-Glu(Hyg)-Gly-d-Orn
  B7 B2γ {Gly} [fifty-Dab] d-Glu-d-Dab
  B8 B1β {Gly} [l-Hse] d-Glu-Gly-50-Dab
  B9 B2α {Gly} [l-Orn] d-Glu-d-Orn
  B10 B2β {Gly} [l-Hse] d-Glu-d-Dab
  B11 B2δ {Gly} [50-Ala] d-Glu-d-Dab-fifty-Thr
  B12 B2α {Gly} [50-Orn] d-Glu-Gly-d-Orn
  B13 B1δ {l-Ser} [l-Ala] d-Glu-l-Asp-l-Lys
  B14 B2β {Gly} [fifty-Hse] d-Glu-d-Lys
  B15 B1δ {50-Ser} [l-Ala] d-Glu-Gly-fifty-Lys-l-Lys
a
Extension by an apostrophe (due east.g. A3α΄) denotes that the l-Ala residuum found normally at position ane of the peptide subunit in type A is replaced by Gly.
b
Abbreviations: Dab, 2,4-diaminobutyric acid; Dpm, 2,6-diaminopimelic acid; Hse, homoserine; Hyg, threo-3-hydroxy-glutamic acid; Lan, lanthionine.
c
{   }, position 1; [   ], position 3.

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