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Bacterial Structure :: Cytoplasmic Structures :: Gram positive and Gram negative bacteria have similar internal, but very different external structures. The cytoplasm of the bacterial cell contains the DNA chromosome, the mRNA, ribosomes, proteins, and metabolites). Unlike eukaryotes, the bacterial chromosome is a single, double-stranded circle that is contained not in a nucleus but in a discrete area known as the nucleoid. Histones are not required to maintain the conformation of the DNA, and the DNA does not form nucleosomes. Plasmids, which are smaller, circular, extrachromosomal DNAs, may also be present. Plasmids are most commonly found in Gram negative bacteria, and although not usually essential for cellular survival, they often provide a selective advantage: many confer resistance to one or more antibiotics. Gram positive and Gram negative bacteria. A Gram positive bacterium has a thick layer of
peptidoglycan (left). A Gram negative bacterium has a thin peptidoglycan layer and an outer membrane (right). Structures in () are not found in all bacteria. The lack of a nuclear membrane simplifies the requirements and control mechanisms for the synthesis of proteins. Without a nuclear membrane, transcription and translation are coupled; in other words, ribosomes can bind to the mRNA, and protein can be made as the mRNA is being synthesized and still attached to the DNA. The bacterial ribosome consists of 30S + 50S subunits, forming a 70S ribosome. This is unlike the eukaryotic 80S (40S + 60S) ribosome. The proteins and RNA of the bacterial ribosome are significantly different from those of eukaryotic ribosomes and are major targets for antibacterial drugs. The cytoplasmic membrane has a lipid bilayer structure similar to the structure of the eukaryotic membranes, but it contains no steroids (e.g., cholesterol); mycoplasmas are the exception to this rule. The cytoplasmic membrane is responsible for many of the functions attributable to organelles in eukaryotes. These tasks include electron transport and energy production, which are normally achieved in the mitochondria. In addition, the membrane contains transport proteins that allow the uptake of metabolites and the release of other substances, ion pumps to maintain a membrane potential, and enzymes. A coiled cytoplasmic membrane, the mesosome, acts as an anchor to bind and pull apart daughter chromosomes during cell division. :: Cell Wall :: The structure, components, and functions of the cell wall distinguish Gram positive from Gram negative bacteria. The important differences in membrane characteristics are outlined in. The cytoplasmic membranes of most prokaryotes are surrounded by rigid peptidoglycan (murein) layers. The exceptions are Archaeobacteria organisms (which contain pseudoglycans or pseudomureins related to peptidoglycan) and mycoplasmas (which have no cell walls at all). Because the peptidoglycan provides rigidity, it also determines the shape of the particular bacterial cell. Gram negative bacteria are also surrounded by outer membranes. Bacterial Membrane Structures Structure Plasma Membrane Cell Wall Gram +ve Bacteria Peptidoglycan Teichoic Acid Chemical Constituents Phospholipids, proteins, enzymes for energy, membrane potential, transport. Glycan chains of GlcNAc and MurNAc cross linked by peptide bridge. Polyribitol phosphate or glycerol phosphate cross linked to peptidoglycan.
Lipoteichoic Acid Gram -ve Bacteria Peptidoglycan Periplasmic Space Outer Membrane Proteins LPS Other Structures Capsule Pili Flagellum Proteins
Lipid linked teichoic acid. Thinner version of that found in Gram positive bacteria. Enzymes involved in transport, degradation, and synthesis. Phospholipids with saturated fatty acids. Porins, lipoprotein, transport proteins. Lipid A, core polysaccharide, O antigen. Polysaccharides (disaccharides and trisaccharides) and polypeptides. Pilin, adhesins. Motor proteins, flagellin. M proteins of streptococci (for example).
GlcNac=N-Acetylglucosamine; MurNAc=N-acetylmuramic acid; LPS=lipopolysaccharide.
Functions Of The Bacterial Envelope Function Structural Rigidity Packaging Of Internal Contents Permeability Barrier Metabolic Uptake Energy Production Adhesion To Host Cells Immune Recognition By Host Escape From Host Recognition Antibiotic Sensitivity Antibiotic Resistance Motility Mating Adhesion :: Gram Positive Bacteria :: A Gram positive bacterium has a thick, multilayered cell wall consisting mainly of peptidoglycan (150 to 500 A) surrounding the cytoplasmic membrane. The peptidoglycan is a meshlike exoskeleton similar in function to the exoskeleton of an insect. Unlike the exoskeleton of the insect, however, the peptidoglycan of the cell is sufficiently porous to allow diffusion of metabolites to the plasma membrane. The peptidoglycan is essential for the structure, for replication, and for survival in the normally hostile conditions in which bacteria grow. During infection, the peptidoglycan can interfere with phagocytosis, is mitogenic (stimulates mitosis of lymphocytes), and has pyrogenic activity (induces fever). The peptidoglycan can be degraded by treatment with lysozyme. Lysozyme, an enzyme in human tears and mucus, is also produced by bacteria and other organisms. Lysozyme degrades the glycan backbone of the peptidoglycan. Without the peptidoglycan, the bacteria succumb to the large osmotic pressure differences across the cytoplasmic membrane and lyse. Removal of the cell wall produces a protoplast that lyses unless it is osmotically stabilized. The Gram positive cell wall may also include other components such as teichoic and lipoteichoic acids and complex polysaccharides (usually called C polysaccharides). Proteins such as the M protein of streptococci and R protein of staphylococci also associate with the peptidoglycan. Teichoic acids are watersoluble polymers of polyol phosphates, which are covalently linked to the peptidoglycan. Lipoteichoic acids have a fatty acid and are anchored in the cytoplasmic membrane. These molecules are common surface antigens that distinguish bacterial serotypes and promote attachment to other bacteria as well as to specific receptors on mammalian cell surfaces (adherence). Teichoic acids are important factors in virulence. Lipoteichoic acids are shed into the media and host and, although weaker, can initiate endotoxiclike activities. Component(s) All. All. Outer membrane or plasma membrane. Membranes and periplasmic transport proteins, porins, permeases. Plasma membrane. Pili, proteins, teichoic acid. All outer structures. Capsule, M protein. Peptidoglycan synthetic enzymes. Outer membrane. Flagella. Pili. Pili.
:: Gram Negative Bacteria :: Gram negative cell walls are more complex than Gram positive cell walls, both structurally and chemically. Structurally, a Gram negative cell wall contains two layers external to the cytoplasmic membrane. Immediately external to the cytoplasmic membrane is a thin peptidoglycan layer, which accounts for only 5% to 10% of the Gram negative cell wall by weight. There are no teichoic or lipoteichoic acids in the Gram negative cell wall. External to the peptidoglycan layer is the outer membrane, which is unique to Gram negative bacteria. The area between the external surface of the cytoplasmic membrane and the internal surface of the outer membrane is referred to as the periplasmic space. This space is actually a compartment containing a variety of hydrolytic enzymes, which are important to the cell for the breakdown of large macromolecules for metabolism. These enzymes typically include proteases, phosphatases, lipases, nucleases, and carbohydrate-degrading enzymes. In the case of pathogenic Gram negative species, many of the lytic virulence factors such as collagenases, hyaluronidases, proteases, and beta-lactamase are in the periplasmic space. This space also contains components of the sugar transport systems and other binding proteins to facilitate the uptake of different metabolites and other compounds. Some binding proteins can be components of a chemotaxis system, which senses the external environment of the cell. Comparison of the Gram positive and Gram negative bacterial cell walls. A, a Gram
positive bacterium has a thick peptidoglycan layer that contains teichoic and lipoteichoic acids. B, a Gram negative bacterium has a thin peptidoglycan layer and an outer membrane that contains lipopolysaccharide, phospholipids, and proteins. The periplasmic space between the cytoplasmic and outer membranes contains transport, degradative, and cell wasll synthetic proteins. The outer membrane is joined to the cytoplasmic membrane at adhesion points and is attached to the peptidoglycan by lipoprotein links. As mentioned previously, outer membranes are unique to Gram negative prokaryotes. The outer membrane is like a stiff canvas sack around the bacteria. The outer membrane maintains the bacterial structure and is a permeability barrier to large molecules (e.g., proteins such as Lysozyme) and hydrophobic molecules. It also provides protection from adverse environmental conditions such as the digestive system of the host (important for Enterobacteriaceae organisms). The outer membrane has an asymmetric bilayer structure that differs from any other biologic membrane in the structure of the outer leaflet of the membrane. The inner leaflet contains phospholipids normally found in bacterial membranes. However, the outer leaflet is composed primarily of an amphipathic molecule (meaning that it has both hydrophobic and hydrophilic ends) called lipopolysaecharide (LPS). Except for those LPS molecules in the process of synthesis, the outer leaflet of the outer membrane is the only location where LPS molecules are found. LPS is also called endotoxin, a powerful stimulator of immune responses. LPS activates B cells and induces macrophage and other cells to release interleukin-I and interleukin-6, tumor necrosis factor, and other factors. LPS causes fever and can cause shock. The Shwartzman reaction (disseminated intravascular coagulation) follows the release of large amounts of endotoxin into the blood stream. LPS is shed from the bacteria into the media and host. Neisseria meningitidis sheds large amounts of a related compound, lipooligosaccharide (LOS), resulting in fever and symptoms. The variety of proteins found in Gram negative outer membranes is limited, but several of the proteins are present in high concentration, resulting in a total protein content higher than that of the cytoplasmic membrane. Many of the proteins traverse the entire lipid bilayer and are thus transmembrane proteins. A group of these proteins is known as porins because they form pores that allow the diffusion of hydrophilic molecules less than 700 Da in mass through the membrane. The outer membrane and the porin channel allow passage of metabolites and small hydrophilic antibiotics, but the outer membrane is a barrier for large or hydrophobic antibiotics and proteins such as 1ysozyme. The outer membrane also contains structural proteins and receptor molecules for bacteriophages and other ligands. The outer membrane is connected to the cytoplasmic membrane at adhesion sites and is tied to the peptidoglycan by lipoprotein. The lipoprotein is covalently attached to the peptidoglycan and is anchored in the outer membrane. The adhesion sites provide a membranous route for the delivery of newly
synthesized outer membrane components to the outer membrane. The outer membrane is held together by divalent cation (Mg+2 and Ca+2) linkages between phosphates on LPS molecules and hydrophobic interactions betwecn the LPS and proteins. These interactions produce a stiff, strong membrane that can be disrupted by antibiotics (e.g., polymyxin) or by the removal of Mg and Ca ions (chelation with ethylenediaminetetraacetic acid [FDTA]). Disruption of the outer membrane weakens the bacteria and allows the permeability of large, hydrophobic molecules. The addition of lysozyme to cells treated in this manner produces spheroplasts, which, like protoplasts, are osmotically sensitive. :: External Structures :: Some bacteria (Gram positive or Gram negative) are closely surrounded by loose polysaccharide or protein layers called capsules. In cases in which it is loosely adherent and nonuniform in density or thickness, the material is referred to as a slime layer. The capsule and slime layers are also called the glycocalyx. Bacillus anthracis, the exception to this rule, produces a polypeptide capsule. The capsule is hard to see in a microscope but can be visualized by the exclusion of India ink particles. Transmission electrom micrographs of Porphyromonas (formerly Bacteroides)
gingivalis and Pseudomonas aeruginosa revealing the surface associated capsule. Both strains were isolated from human patients, P. gingivalis from an adult with peridontitis and P. aeruginosa from a patieng with cystic fibrosis. C = capsule; OM = outer membrane; PG = peptidoglycan; CM = cytoplasmic membrane; R = ribosome; PP = polyphosphate. Bar = 0.1 um. Capsules and slimes are unnecessary for the growth of bacteria but are very important for survival in the host. The capsule is poorly antigenic and antiphagocytic and is a major virulence factor (e.g., Streptococcus pneumoniae). The capsule can also act as a barrier to toxic hydrophobic molecules, such as detergents, and can promote adherence to other bacteria or to host tissue surfaces. For Streptococcus mutans, the dextran and levan capsules are the means by which the bacteria attach and stick to the tooth enamel. Synthesis of the capsule takes energy and will not be effected by the bacteria after continued growth under laboratory conditions away from the selective pressures of the host. Flagella are ropelike propellers composed of helically coiled protein subunits (flagellin) that are anchored in the bacterial membranes through hook and basal body structures and that are driven by membrane potential. Bacterial species may have one or several flagella on their surfaces, and they may be anchored at different parts of the cell. Flagella provide motility for bacteria, allowing the cell to swim (chemotaxis) toward food and away from poisons. Bacteria approach food by swimming straight and then tumbling in a new direction. The swimming period becomes longer as the concentration of chemoattractant increases. The direction of flagellar spinning determines whether the bacteria swim or tumble. Flagella also express antigenic and strain determinants. Fimbriae (pill) (Latin for "fringe") are hairlike structures on the outside of bacteria; they are composed of protein subunits (pilin). Fimbriae can be morphologically distinguished from flagella because they are smaller in diameter (3 to 8 nm versus 15 to 20 nm) and usually are not coiled in structure. Generally, several hundred fimbriae are arranged peritrichously (uniformly) over the entire surface of the bacterial cell. They may be as long as 15 to 20 nm, or many times the length of the cell. Fimbriae promote adherence to other bacteria or to the host (alternative names are adhesins, lectins, evasins, and aggressins). As an adherence factor (adhesin), fimbriae are an important virulence factor for E. coli colonization and infection of the urinary tract, for Neisseria gonorrhoeae and other bacteria. The tips of the fimbriae may contain proteins (lectins) that bind to specific sugars (e.g., mannose). F pili (sex pill) promote the transfer of large segments of bacterial chromosomes between bacteria. These pill are encoded by a plasmid (F). :: Bacterial Exceptions :: Mycobacteria have a peptidoglycan layer (slightly different structure), which is intertwined with and covalently attached to an arabinogalactan polymer and surrounded by a waxlike lipid coat of mycolic acid
(large alpha-branched beta-hydroxy fatty acids), cord factor (glycolipid of trehalose and two mycolic acids), waxD (glycolipid of 15 to 20 mycolic acids and sugar), and sulfolipids. These bacteria are described as acidfast staining. The coat is responsible for virulence and is anti phagocytic. Corynebacterium and Nocardia organisms also produce mycolic acid lipids. The mycoplasmas are also exceptions in that they have no peptidoglycan cell wall and they incorporate steroids from the host into their membranes.
Structure and Biosynthesis of the Cell Wall The cell wall components are large structures made up of polymers of subunits. This type of structure facilitates their synthesis. Like astronauts building a space station in space, bacteria face problems assembling their cell walls. Synthesis of the peptidoglycan, LPS, teichoic acid, and capsule occurs on the outside of the bacteria, away from the synthetic machinery and energy sources of the cytoplasm and in an inhospitable environment. For both the space station and the bacteria, prefabricated precursors and subunits of the final structure are assembled in a factory-like setting on the inside, attached to a conveyor belt-like structure, brought to the surface, and then attached to the preexisting structure. For bacteria, the molecular conveyor belt-like structure is a large hydrophobic phospholipid called bactoprenol (undecaprenol, C55 isoprenoid). The prefabricated precursors must also be activated with high energy bonds (e.g., phosphates) or other means to power the attachment reactions occurring outside the cell. For Gram negative bacteria, the outer membrane components are delivered through adhesion sites. :: Peptidoglycan (Mucopeptide, Murein) :: The peptidoglycan is a rigid mesh made up of ropelike linear polysaccharide chains cross-linked by peptides. The polysaccharide is made up of repeating disaccharides of N-acetylglucosamine (GlcNAc, NAG, G) and N-acetylmuramic acid (MurNAc, NAM, M). Precursor of peptidoglycan. The peptidoglycan is built from prefabricated units that
contain a pentapeptide attached to the MurNAc. The pentapeptide contains a terminal d-alanined-alanine unit. This dipeptide is required for cross linking the peptidoglycan and is the basis for the action of beta-lactam and vancomycin antibiotics. A tetrapeptide is attached to the MurNAc. The peptide is unusual because it contains both D and L amino acids (D amino acids are not normally used in nature) and the peptide is produced enzymatically. The first two amino acids attached to the MurNAc may vary for different organisms. The di-amino amino acids in the third position are essential for the cross-linking of the peptidoglycan chain. Examples of di-amino amino acids include lysine and diaminopimclic and di-aminobutyric acids. The peptide cross-link is formed between the free amine of the di-amino amino acid in the third position of the peptide and the n-alanine in the fourth position of another chain. S. aureus and other Gram positive bacteria use an amino acid bridge (e.g. a glycine, peptide) between these amino acids to lengthen the crosslink. The precursor form of the peptide has an extra D-alanine, which is released during the cross-linking step. The peptidoglycan in Gram positive bacteria forms multiple layers and is often cross-linked in three dimensions, providing a very strong, rigid cell wall. In contrast, the peptidoglycan in Gram negative cell walls is usually only one molecule (layer) thick. The rigidity of the peptidoglycan mesh is determined by the munber of cross-links and the length of the cross-link. :: Peptidoglycan Synthesis :: Peptidoglycan synthesis occurs in four steps. First, inside the cell, glucosamine is enzymatically converted into MurNAc and then energetically activated by a reaction with uridine triphosphate (UTP) to produce uridine diphosphate-N-acetylmuramic acid (UDPMurNAc). Next, the UDP-MurNAc-pentapeptide precursor is assembled in a series of enzymatic steps.
Peptidoglycan synthesis. A, peptidoglycan synthesis occurs in three phases. (1)
Peptidoglycan is synthesized from prefabricated units constructed and activated for assembly and transport inside the cell. (2) At the membrane, the units are assembled onto the undecaprenol phosphate conveyor belt, and assembly is completed. (3) The unit is translocated to the outside of the cell, where it is attached to the polysaccharide chain, and the peptide is cross linked to finish the construction. Such a construction can be compared with the assembly of a space station. B, the cross linking reaction is a transpeptide. One peptide bond (produced inside the cell) is traded for another (outside the cell) with the release of d-alanine. The enzymes that catalyze the reaction are called d-alanine, d-alanine transpeptidase-carboxypeptidases. These enzymes are the targets of beta-lactam antibiotics and are called penicillin binding proteins. Second, the UDP-MurNAc pentapeptide is attached to the bactoprenol "conveyor belt" in the cytoplasmic membrane through a pyrophosphate link with the release of uridine monophosphate (UMP). G1cNAc is added to snake the disaccharide building block of the peptidoglycan. Some bacteria (e.g., S. aureus) add a pentaglycine or another chain to the di-amino amino acid at the third position of the peptide chain to lengthen the cross-link. Third, the bactoprenol molecule translocates the disaccharide pentapeptide precursor to the outside of the cell. The G1cNAc-MurNAc disaccharide is then attached to a peptidoglycan chain using the pyrophosphate link between itself and the bactoprenol as energy to drive the reaction. The pyrophosphobactoprenol is converted back to a phosphobactoprenol and recycled. Fourth, outside the cell but near the membrane surface, peptide chains from adjacent glycan chains are cross-linked to each other by a peptide bond exchange (transpeptidation) between the free amine of the amino acid in the third position of the pentapeptide (e.g., lysine) or the N-terminus of the attached pentaglycine chain and the Dalanine at the fourth position of the other peptide chain, releasing the terminal D-alanine of the precursor. This step requires no additional energy because peptide bonds are "traded." The cross-linking reaction membrane-bound transpeptidases. Related enzymes, DD-carboxypeptidases, remove extra terminal D-alanines, which limit the extent of cross-linking. These enzymes are called penicillin-binding proteins (PBPs) because they are targets for penicillin and other beta-lactam antibiotics. Penicillin and related beta-lactain antibiotics resemble the "transition state" conformation of the DALA-DALA unit when bound to these enzymes. Different PBPs are used for extending the peptidoglycan, creating a septum for cell division, and curving the peptidoglycan mesh (cell shape). The peptidoglycan is constantly being synthesized and degraded. Autolysins such as lysozyme are important for determining bacterial shape. Inhibition of synthesis or the cross-linking of the peptidoglycan does not stop the autolysins, and their action weakens the mesh and the bacterial structure and leads to lysis and cell death. New peptidoglycan synthesis does not occur during starvation, which leads to a weakening of the peptidoglycan and a loss in the dependability of Gram stain. An understanding of the biosynthesis of peptidoglycan is essential in medicine because these reactions are unique to bacterial cells and hence can be inhibited with little or no adverse effect on host (human) cells. A number of antibiotics target one or more steps in this pathway. :: Teichoic Acid :: Teichoic and lipoteichoic acid are polymers of chemically modified ribose or glycerol connected by phosphates. Sugars, choline, or D-alanine may be attached to the hydroxyls of the ribose or glycerol, providing antigenic determinants. These can be distinguished by antibodies and inay determine the bacterial serotype. Lipoteichoic acid has a fatty acid and is anchored in the membrane. Teichoic acid is synthesized from building blocks in a manner similar to that of peptidoglycan. Teichoic acid and some surface proteins (e.g., protein A from S. aureus) are secreted from the cells and then enzymatically attached to the Nterminus of the peptide of peptidoglycan. Teichoic acid. Teichoic acid is a polymer of chemically modified ribitol (a) or glycerol
phosphate (b). The nature of the modification (eg. sugars, amino acids) can define the serotype of
the bacteria. Teichoic acid may be covalently attached to the peptidoglycan. Lipoteichoic acid is anchoted in the cytoplasm membrane by a covalently attached fatty acid. :: Lipopolysaccharide :: LPS (endotoxin) consists of three structural sections: Lipid A, core polysaccharide (rough core), and O antigen. Lipid A is a basic component of LPS and is essential for bacterial viability. Lipid A is responsible for the endotoxin activity of LPS. It has a phosphorylated glucosamine disaccharide backbone with fatty acids attached to anchor the structure in the outer membrane. The phosphates connect LPS units into aggregates. One carbohydrate chain is attached to the disaccharide backbone and extends away from the bacteria. The core polysaccharide is a branched polysaccharide of 9 to 12 sugars. Most of the core region is also essential for LPS structure and bacterial viability. The core region contains an unusual sugar, 2-keto-3deoxy-octanoate (KDO), and is phosphorylated. The 0 antigen is attached to the core and extends away from the bacteria. It is a long, linear polysaccharide consisting of 50 to 100 repeating saccharide units of 4 to 7 sugars per unit. The lipopolysaccharide of the Gram negative cell envelope. A, segment of the polymer
showing the arrangements of the major constituents. B, structre of lipid A of Salmonella typhimurim. C, polysaccharide core. D, typical repeat unit (S. typhimurium). LPS structure is used to classify bacteria. The basic structure of lipid A is identical for related bacteria and is similar for all Gram negative Enterobacteriaceae. The core region is the same for a species of bacteria. The 0 antigen distinguishes serotypes (strains) of a bacterial species. For example, the 0157:H7 serotype identifies the E. coli agent of hemolytic-uremic syndrome. The lipid A and core portions are enzymatically synthesized in a sequential manner on the inside surface of the cytoplasmic membrane. The repeat units of the O antigen are assembled on a bactoprenol molecule and then transferred to a growing O antigen chain. The finished O antigen chain is transferred to the core lipid A structure. The LPS molecule is translocated through adhesion sites to the outer surface of the outer membrane.
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Cell Division The replication of the bacterial chromosome also triggers the initiation of cell division. The production of two daughter bacteria requires the growth and extension of the cell wall components followed by the production of a septum (cross wall) to divide the daughter bacteria into two cells. The septum consists of two membranes separated by two layers of peptidoglycan. Septum formation is initiated at the cell membrane; the septum grows from opposite sides toward the center of the cell, causing cleavage of the daughter cells. This process requires special transpeptidases and other enzymes. New peptidoglycan is synthesized in a defined growth zone, usually in a ring on either side of the growing septum. For streptococci, the growth zone is at 180 degrees from each other, producing linear chains of bacteria. In contrast, the growth zone of staphylococci is at 90 degrees. Incomplete cleavage of the septum can cause the bacteria to remain linked, forming chains (e.g., streptococci) or clusters (e.g., staphylococci). Electrom photomicrographs of Gram positive cell division (Bacillus subtilis; left)
and Gram negative cell division (Escherichia coli; right). A to C represent a progression in cell division. CW = cell wall; CM = cytoplasmic membrane; S = septum; N = nucleoid; OM = outer membrane. Bar = 0.2 um. Spores Some Gram positive, but never Gram negative, bacteria such as members of the genera Bacillus and Clostridium (soil bacteria) are spore formers. Under harsh environmental conditions, such as the loss of a nutritional requirement, these bacteria can convert from a vegetative state to a dormant state, or spore. The location of the spore within a cell is a characteristic of the bacteria and can assist in identification of the bacterium. The spore is a dehydrated, multishelled structure that protects and allows the bacteria to exist in "suspended animation." It contains a complete copy of the chromosome, the bare minimum concentrations of essential proteins and ribosornes, and a high concentration of calcium bound to dipicolinic acid. The spore has an inner membrane, two peptidoglycan lavers, and an outer keratin-like protein coat. The spore looks refractile (bright) in the microscope. The structure of the spore protects the genoinic DNA from desiccation, intense heat, radiation, and attack by most enzymes and chemical agents. In fact, bacterial spores are so resistant to environmental factors that they can exist for centuries as viable spores. Spores are also difficult to decontaminate with standard disinfectants. Sporogenesis, the process of endospore formation.
Depletion of specific nutrients (e.g., alanine) from the growth medium triggers a cascade of genetic events (comparable to differentiation) leading to the production of a spore. Spore mRNA are transcribed and other mRNA are turned off. Dipicolinic acid is produced, and antibiotics and toxins are often excreted. After duplication of the chromosome, one copy of DNA and cytoplasmic contents (core) are surrounded by its cytoplastmic membrane, the peptidoglycan, and the membrane of the septum. This wraps the DNA in the two layers of membrane and peptidoglvcan that would normally divide the cell. This is surrounded by the cortex, which is made up of a thin inner layer of tightly crosslinked peptidoglycan surrounding a membrane (which used to be the cytoplasmic membrane) and a loose outer peptidoglycan layer. The cortex is surrounded by the tough, keratin-like protein coat which protects the spore. The process requires 6 to 8 hours for complection. The germination or transformation of spores into the vegetative state is stimulated by disruption of the outer coat by mechanical stress, pH, heat, or another stressor and requires water and a triggering nutrient (e.g., alanine). The process takes about 90 minutes. Once the germination process has begun, the spore will take up water, swell, shed its coats, and produce one new vegetative cell identical to the original vegetative
cell, thus completing the entire cycle. Once germination has begun and the spore coat has been compromised, the spore is weakened and can be inactivated like other bacteria.
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