A. Function of Peptidoglycan
Peptidoglycan prevents osmotic lysis (def). As seen earlier under the cytoplasmic membrane, bacteria concentrate dissolved nutrients (solute) through active transport. As a result, the bacterium's cytoplasm is usually hypertonic to its surrounding environment and the net flow of free water is into the bacterium. Without a strong cell wall, the bacterium would burst from the osmotic pressure of the water flowing into the cell.
B. Structure and Composition of Peptidoglycan
With the exceptions above, members of the domain Bacteria have a cell wall containing a semirigid, tight knit molecular complex called peptidoglycan (def).
Peptidoglycan, also called murein, is a vast polymer consisting of interlocking chains of identical peptidoglycan monomers (see Fig. 1A and Fig. 1B). A peptidoglycan monomer (def) consists of two joined amino sugars, N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM), with a pentapeptide (def) coming off of the NAM (see Fig. 2A and Fig. 2B). The types and the order of amino acids in the pentapeptide, while almost identical in gram-positive and gram-negative bacteria, show some slight variation among the domain Bacteria.
The peptidoglycan monomers (def) are synthesized in the cytosol of the bacterium where they attach to a membrane carrier molecule called bactoprenol. As discussed below, The bactoprenols transport the peptidoglycan monomers across the cytoplasmic membrane and work with the enzymes discussed below to insert the monomers into existing peptidoglycan enabling bacterial growth following binary fission.
Once the new peptidoglycan monomers are inserted, glycosidic bonds then link these monomers into the growing chains of peptidoglycan. These long sugar chains are then joined to one another by means of peptide cross-links between the peptides coming off of the NAMs. By linking the rows and layers of sugars together in this manner, the peptide cross-links provide tremendous strength to the cell wall, enabling it to function similar to a molecular chain link fence around the bacterium (see Fig. 1A and Fig. 1B).
C. Synthesis of Peptidoglycan
In order for bacteria to increase their size following binary fission, links in the peptidoglycan must be broken, new peptidoglycan monomers must be inserted, and the peptide cross links must be resealed.
The following sequence of events occur:
1. Bacterial enzymes called autolysins:
a) Break the glycosidic bonds between the peptidoglycan monomers at the point of growth along the existing peptidoglycan (see Fig. 3, steps 1-3); and
b) Break the peptide cross-bridges that link the rows of sugars together (see Fig. 3, steps 1-3).
by Gary E. Kaiser, Ph.D.
Professor of Microbiology, The Community College of Baltimore County, Catonsville Campus
This work is licensed under a Creative Commons Attribution 4.0 International License.
Based on a work The Grapes of Staph at https://cwoer.ccbcmd.edu/science/microbiology/index_gos.html.Last updated: August, 2019
Please send comments and inquiries to Dr. Gary Kaiser
2. The peptidoglycan monomers are synthesized in the cytosol (see Fig. 4, step-1 and Fig. 4, step-2) and bind to bactoprenol. The bactoprenols transport the peptidoglycan monomers across the cytoplasmic membrane and interacts with transglycosidases to insert the monomers into existing peptidoglycan (see Fig. 4, step-3, Fig. 4, step-4, Fig. 4, step-5, and Fig. 4, step-6)
by Gary E. Kaiser, Ph.D.
Professor of Microbiology, The Community College of Baltimore County, Catonsville Campus
This work is licensed under a Creative Commons Attribution 4.0 International License.
Based on a work The Grapes of Staph at https://cwoer.ccbcmd.edu/science/microbiology/index_gos.html.Last updated: August, 2019
Please send comments and inquiries to Dr. Gary Kaiser
3. Transglycosylase (transglycosidase) enzymes insert and link new peptidoglycan monomers into the breaks in the peptidoglycan (see Fig. 5, step 1 and Fig. 5, step 2).
by Gary E. Kaiser, Ph.D.
Professor of Microbiology, The Community College of Baltimore County, Catonsville Campus
This work is licensed under a Creative Commons Attribution 4.0 International License.
Based on a work The Grapes of Staph at https://cwoer.ccbcmd.edu/science/microbiology/index_gos.html.Last updated: August, 2019
Please send comments and inquiries to Dr. Gary Kaiser
4. Finally, transpeptidase enzymes reform the peptide cross-links between the rows and layers of peptidoglycan to make the wall strong (see Fig. 6, step 1 and see Fig. 6, step 2).
In Escherichia coli, the terminal D-alanine is cleaved from the pentapeptides to form a tetrapeptides. This provides the energy to bond the D-alanine of one tetrapeptide to the diaminopimelic acid of another tetrapeptide (see Fig. 1B). In the case of Staphylococcus aureus, the terminal D-alanine is cleaved from the pentapeptides to form a tetrapeptides. This provides the energy to bond a pentaglycine bridge (5 molecules of the amino acid glycine) from the D-alanine of one tetrapeptide to the L-lysine of another (see Fig. 1A).
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by Gary E. Kaiser, Ph.D. Last updated: August, 2019 |
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by Gary E. Kaiser, Ph.D. Last updated: August, 2019 |
In the center of the bacterium, a group of proteins called Fts (filamentous temperature sensitive) proteins interact to form a ring at the cell division plane. These proteins form the cell division apparatus known as the divisome and are directly involved in bacterial cell division by binary fission (see Fig. 1 and Fig. 2).
The divisome is responsible for directing the synthesis of new cytoplasmic membrane and new peptidoglycan to form the division septum.
D. Antimicrobial Agents that Inhibit Peptidoglycan Synthesis Causing Bacterial Lysis
Many antibiotics work by inhibiting normal synthesis of peptidoglycan in bacteria causing them to burst as a result of osmotic lysis (def).
As just mentioned, in order for bacteria to increase their size following binary fission, enzymes called autolysins break the peptide cross links in the peptidoglycan, transglycosylase enzymes then insert and link new peptidoglycan monomers into the breaks in the peptidoglycan, and transpeptidase enzymes reform the peptide cross-links between the rows and layers of peptidoglycan to make the wall strong.
Interference with this process results in a weak cell wall and lysis of the bacterium from osmotic pressure. Examples include the penicillins (penicillin G, methicillin, oxacillin, ampicillin, amoxicillin, ticarcillin, etc.), the cephalosporins (cephalothin, cefazolin, cefoxitin, cefotaxime, cefaclor, cefoperazone, cefixime, ceftriaxone, cefuroxime, etc.), the carbapenems (imipenem, metropenem), the monobactems (aztreonem), the carbacephems (loracarbef), and the glycopeptides (vancomycin, teichoplanin).
- For example, penicillins and cephalosporins bind to the transpeptidase enzymes (also called penicillin-binding proteins) responsible for resealing the cell wall as new peptidoglycan monomers are added during bacterial cell growth. This blocks the transpeptidase enzymes from cross-linking the sugar chains and results in a weak cell wall and subsequent osmotic lysis of the bacterium (see Fig. 8).
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by Gary E. Kaiser, Ph.D. Last updated: August, 2019 |
Antimicrobial chemotherapy will be discussed in greater detail later in Unit 2 under Control of Bacteria by Using Antibiotics and Disinfectants.
E. Gram-Positive, Gram-Negative, and Acid-Fast Bacteria
Most bacteria can be placed into one of three groups based on their color after specific staining procedures are performed: Gram-positive, Gram-negative, or acid-fast.
- Gram-positive: retain the initial dye crystal violet during the Gram stain procedure and appear purple when observed through the microscope. Common Gram-positive bacteria of medical importance include Streptococcus pyogenes, Streptococcus pneumoniae, Staphylococcus aureus, Enterococcus faecalis, and Clostridium species.
- Gram-negative: decolorize during the Gram stain procedure, pick up the counterstain safranin, and appear pink when observed through the microscope. Common Gram-negative bacteria of medical importance include Salmonella species, Shigella species, Neisseria gonorrhoeae, Neisseria meningitidis, Haemophilus influenzae, Escherichia coli, Klebsiella pneumoniae, Proteus species, and Pseudomonas aeruginosa. Also see Gram stain of a mixture of Gram-positive and Gram-negative bacteria.
- acid-fast: resist decolorization with an acid-alcohol mixture during the acid-fast stain procedure, retain the initial dye carbol fuchsin and appear red when observed through the microscope. Common acid-fast bacteria of medical importance include Mycobacterium tuberculosis, Mycobacterium leprae, and Mycobacterium avium-intracellulare complex.
We will now look at each of these three bacterial cell wall types in the following sections.
F. The S-layer
1. Structure and Composition
A common cell wall feature in species of Archaea is a paracrystalline surface layer (S-layer). It consists of a regularly structured layer composed of interlocking glycoprotein or protein molecules. In electron micrographs, has a pattern resembling floor tiles. Although they vary with the species, S-layers generally have a thickness between 5 and 25 nm and possess identical pores with 2-8 nm in diameter. Many Gram-positive and Gram-negative bacteria in the domain Bacteria have also been found to have S-layers.
To view electron micrographs of S-layers see the following:
- S-Layer Proteins, from Todar's Online Textbook of Bacteriology.
2. Functions and Significance to Bacteria Causing Infections
The S-layer has been associated with a number of possible functions. These include the following:
a. The S-layer may protect bacteria from harmful enzymes, from changes in pH, from the predatory bacterium Bdellovibrio, a parasitic bacterium that actually uses its motility to penetrate other bacteria and replicate within their cytoplasm, and from bacteriophages (def).
b. The S-layer can function as an adhesin, enabling the bacterium to adhere to host cells and environmental surfaces, colonize, and resist flushing.
c. The S-layer may contribute to virulence by protecting the bacterium against complement attack and phagocytosis.
d. The S-layer may act as a as a coarse molecular sieve.