Which Category of Antimicrobial Drug Essentially Acts to Stall a Ribosome as It Reads Mrna?

Inhibiting Cell Wall Synthesis

β-Lactam (beta-lactam) and glycopeptide antibiotics piece of work by inhibiting or interfering with cell wall synthesis of the target bacteria.

Learning Objectives

Describe the two types of antimicrobial drugs that inhibit cell wall synthesis: beta-lactam and glycopeptide antibiotics

Key Takeaways

Key Points

• The peptidoglycan layer is important for cell wall structural integrity, being the outermost and main component of the wall.
• β-Lactam antibiotics are a broad grade of antibiotics that includes penicillin derivatives (penams), cephalosporins (cephems), monobactams, and carbapenems.
• β-Lactam antibiotics are bacteriocidal and act by inhibiting the synthesis of the peptidoglycan layer of bacterial cell walls.
• Glycopeptide antibiotics include vancomycin, teicoplanin, telavancin, bleomycin, ramoplanin, and decaplanin.
• Glycopeptide antibiotics inhibit the synthesis of cell walls in susceptible microbes by inhibiting peptidoglycan synthesis.

Key Terms

• beta-lactam antibiotic: A wide class of antibiotics that inhibit cell wall synthesis, consisting of all antibiotic agents that contains a β-lactam nucleus in their molecular structures. This includes penicillin derivatives (penams), cephalosporins (cephems), monobactams, and carbapenems.
• Glycopeptide antibiotic: Glycopeptide antibiotics are composed of glycosylated cyclic or polycyclic nonribosomal peptides. Meaning glycopeptide antibiotics include vancomycin, teicoplanin, telavancin, bleomycin, ramoplanin, and decaplanin. This class of drugs inhibit the synthesis of prison cell walls in susceptible microbes by inhibiting peptidoglycan synthesis.
• peptidoglycan: A polymer of glycan and peptides found in bacterial prison cell walls.

Two types of antimicrobial drugs piece of work by inhibiting or interfering with cell wall synthesis of the target leaner. Antibiotics commonly target bacterial cell wall formation (of which peptidoglycan is an important component) because beast cells do not have cell walls. The peptidoglycan layer is important for cell wall structural integrity, existence the outermost and primary component of the wall.

The first form of antimicrobial drugs that interfere with cell wall synthesis are the β-Lactam antibiotics (beta-lactam antibiotics), consisting of all antibiotic agents that contains a β-lactam nucleus in their molecular structures. This includes penicillin derivatives (penams), cephalosporins (cephems), monobactams, and carbapenems. β-Lactam antibiotics are bacteriocidal and act by inhibiting the synthesis of the peptidoglycan layer of bacterial prison cell walls. The last step in the synthesis of the peptidoglycan is facilitated by penicillin-binding proteins (PBPs). PBPs vary in their affinity for binding penicillin or other β-lactam antibiotics.

Penicillin spheroplast generation: Diagram depicting the failure of bacterial jail cell division in the presence of a prison cell wall synthesis inhibitor (e.g. penicillin, vancomycin).one- Penicillin (or other jail cell wall synthesis inhibitor) is added to the growth medium with a dividing bacterium.two- The cell begins to abound, just is unable to synthesize new cell wall to accommodate the expanding cell.iii- As cellular growth continues, cytoplasm covered by plasma membrane begins to clasp out through the gap(south) in the cell wall.4- Jail cell wall integrity is further violated. The cell continues to increase in size, just is unable to "pinch off" the extra cytoplasmic material into two daughter cells because the formation of a division furrow depends on the power to synthesize new cell wall.v- The prison cell wall is shed entirely, forming a spheroplast, which is extremely vulnerable relative to the original cell. The loss of the jail cell wall besides causes the cell to lose command over its shape, so even if the original bacterium were rod-shaped, the sphereoplast is by and large spherical. Finally, the fact that the cell has now doubled much of its genetic and metabolic material further disrupts homeostasis, which usually leads to the cell's decease.

Leaner often develop resistance to β-lactam antibiotics by synthesizing a β-lactamase, an enzyme that attacks the β-lactam ring. To overcome this resistance, β-lactam antibiotics are often given with β-lactamase inhibitors such equally clavulanic acid.

The second course of antimicrobial drugs that interfere with cell wall synthesis are the glycopeptide antibiotics, which are composed of glycosylated cyclic or polycyclic nonribosomal peptides. Significant glycopeptide antibiotics include vancomycin, teicoplanin, telavancin, bleomycin, ramoplanin, and decaplanin. This class of drugs inhibit the synthesis of cell walls in susceptible microbes by inhibiting peptidoglycan synthesis. They bind to the amino acids within the cell wall preventing the improver of new units to the peptidoglycan.

Injuring the Plasma Membrane

Several types of antimicrobial drugs part past disrupting or injuring the plasma membrane.

Learning Objectives

Discuss the function of the plasma membrane and how antimicrobial drugs target it

Central Takeaways

Key Points

• The plasma membrane or cell membrane is a biological membrane that separates the interior of all cells from the outside surround.
• Plasma membranes are involved in a variety of cellular processes such as cell adhesion, ion conductivity, and cell signaling. They serve equally the attachment surface for several extracellular structures, including the jail cell wall, glycocalyx, and intracellular cytoskeleton.
• Disrupting the plasma membrane causes rapid depolarization, resulting in a loss of membrane potential leading to inhibition of protein, DNA and RNA synthesis, which results in bacterial prison cell death.

Key Terms

• plasma membrane: The semipermeable membrane that surrounds the cytoplasm of a cell.
• cell wall: A thick, fairly rigid layer formed around private cells of leaner, Archaea, fungi, plants, and algae, the cell wall is external to the jail cell membrane and helps the cell maintain its shape and avoid harm.
• plasma prison cell: a form of lymphocyte that produces antibodies when reacted with a specific antigen; a plasmacyte

Prokaryotic Cell: Diagram of a typical gram-negative bacterium, with the thin cell wall sandwiched between the red outer membrane and the sparse light-green plasma membrane.

The plasma membrane or jail cell membrane is a biological membrane that separates the interior of all cells from the outside environment. The plasma membrane is selectively permeable to ions and organic molecules. Information technology controls the movement of substances in and out of cells. The membrane basically protects the cell from exterior forces. It consists of the lipid bilayer with embedded proteins. Plasma membranes are involved in a diverseness of cellular processes such as jail cell adhesion, ion conductivity, and prison cell signaling. It serves as the attachment surface for several extracellular structures, including the cell wall, glycocalyx, and intracellular cytoskeleton. Fungi, bacteria, and plants also have the cell wall which provides a mechanical support for the cell and precludes the passage of larger molecules. The plasma membrane also plays a role in anchoring the cytoskeleton to provide shape to the prison cell and in attaching to the extracellular matrix and other cells to help group cells together to course tissues.

In that location are several types of antimicrobial drugs that role by disrupting or injuring the plasma membrane. One instance is daptomycin, a lipopeptide which has a singled-out mechanism of activity, disrupting multiple aspects of bacterial cell membrane part. It appears to bind to the membrane causes rapid depolarization, resulting in a loss of membrane potential leading to inhibition of protein, DNA and RNA synthesis, which results in bacterial cell death. Another example is polymyxins antibiotics which accept a full general construction consisting of a circadian peptide with a long hydrophobic tail. They disrupt the structure of the bacterial jail cell membrane by interacting with its phospholipids.

Inhibiting Nucleic Acid Synthesis

Antimicrobial drugs inhibit nucleic acrid synthesis through differences in prokaryotic and eukaryotic enzymes.

Learning Objectives

Country the steps where inhibitors of nucleic acrid synthesis can exert their role

Key Takeaways

Key Points

• Some antimicrobial drugs interfere with the initiation, elongation or termination of RNA transcription.
• Some antimicrobial drugs interfere with diverse aspects of Dna replication.
• The antimicrobial actions of these drugs are a result of differences in the prokaryotic and eukaryotic enzymes involved in nucleic acrid synthesis.

Cardinal Terms

• transcription: The synthesis of RNA under the management of Deoxyribonucleic acid.
• replication: Process by which an object, person, place or idea may exist copied mimicked or reproduced.

Diagram of Transcription: RNA Polymerase, an enzyme that produces RNA, from T. aquaticus pictured during elongation. Portions of the enzyme were made transparent so every bit to make the path of RNA and DNA more clear. The magnesium ion (yellow) is located at the enzyme active site.

Antimicrobial drugs can target nucleic acrid (either RNA or DNA) synthesis. The antimicrobial actions of these agents are a effect of differences in prokaryotic and eukaryotic enzymes involved in nucleic acid synthesis.

Prokaryotic transcription is the process in which messenger RNA transcripts of genetic material are produced for later translation into proteins. The transcription procedure includes the following steps: initiation, elongation and termination. Antimicrobial drugs have been developed to target each of these steps. For example, the antimicrobial rifampin binds to Dna-dependent RNA polymerase, thereby inhibiting the initiation of RNA transcription.

Other antimicrobial drugs interfere with DNA replication, the biological process that occurs in all living organisms and copies their DNA and is the footing for biological inheritance. The process starts when one double-stranded DNA molecule produces two identical copies of the molecule. In a cell, Deoxyribonucleic acid replication begins at specific locations in the genome, called "origins. " Uncoiling of DNA at the origin, and synthesis of new strands, forms a replication fork. In addition to DNA polymerase, the enzyme that synthesizes the new DNA by calculation nucleotides matched to the template strand, a number of other proteins are associated with the fork and assist in the initiation and continuation of Deoxyribonucleic acid synthesis. DNA replication, similar all biological polymerization processes, proceeds in iii enzymatically catalyzed and coordinated steps: initiation, elongation and termination. Whatsoever of the steps in the procedure of Dna replication can be targeted by antimicrobial drugs. For instance, quinolones inhibit Dna synthesis by interfering with the coiling of Dna strands.

Deoxyribonucleic acid Replication: The double helix is unwound and each strand acts equally a template for the next strand. Bases are matched to synthesize the new partner strands.

Inhibiting Protein Synthesis

Protein synthesis inhibitors are substances that disrupt the processes that atomic number 82 directly to the generation of new proteins in cells.

Learning Objectives

Paraphrase the general mechanism of activeness of protein synthesis inhibitors

Fundamental Takeaways

Key Points

• Poly peptide synthesis inhibitors commonly human action at the ribosome level, taking reward of the major differences between prokaryotic and eukaryotic ribosome structures.
• Protein synthesis inhibitors work at unlike stages of prokaryotic mRNA translation into proteins similar initiation, elongation (including aminoacyl tRNA entry, proofreading, peptidyl transfer, and ribosomal translocation), and termination.
• By targeting unlike stages of the mRNA translation, antimicrobial drugs can be changed if resistance develops.

Primal Terms

• translation: A process occurring in the ribosome, in which a strand of messenger RNA (mRNA) guides assembly of a sequence of amino acids to brand a protein.

A poly peptide synthesis inhibitor is a substance that stops or slows the growth or proliferation of cells by disrupting the processes that pb directly to the generation of new proteins. It unremarkably refers to substances, such as antimicrobial drugs, that act at the ribosome level. The substances take reward of the major differences between prokaryotic and eukaryotic ribosome structures which differ in their size, sequence, structure, and the ratio of protein to RNA. The differences in structure allow some antibiotics to kill leaner by inhibiting their ribosomes, while leaving human ribosomes unaffected.

Translation in prokaryotes involves the associates of the components of the translation system which are: the two ribosomal subunits (the big 50S & small-scale 30S subunits), the mRNA to exist translated, the outset aminoacyl tRNA, GTP (every bit a source of energy), and three initiation factors that help the assembly of the initiation circuitous. The ribosome has three sites: the A site, the P site, and the Due east site (not shown in ). The A site is the point of entry for the aminoacyl tRNA. The P site is where the peptidyl tRNA is formed in the ribosome. The E site which is the exit site of the now uncharged tRNA after it gives its amino acid to the growing peptide chain.

Simplified diagram of protein synthesis: Diagram showing how the translation of the mRNA and the synthesis of proteins is made past ribosomes.

In full general, protein synthesis inhibitors work at different stages of prokaryotic mRNA translation into proteins like initiation, elongation (including aminoacyl tRNA entry, proofreading, peptidyl transfer, and ribosomal translocation), and termination. The post-obit is a listing of common antibacterial drugs and the stages which they target.

• Linezolid acts at the initiation stage, probably by preventing the formation of the initiation circuitous, although the mechanism is non fully understood.
• Tetracyclines and Tigecycline (a glycylcycline related to tetracyclines) block the A site on the ribosome, preventing the binding of aminoacyl tRNAs.
• Aminoglycosides, among other potential mechanisms of action, interfere with the proofreading procedure, causing an increased rate of error in synthesis with premature termination.
• Chloramphenicol blocks the peptidyl transfer step of elongation on the 50S ribosomal subunit in both bacteria and mitochondria.
• Macrolides, clindamycin, and aminoglycosides accept evidence of inhibition of ribosomal translocation.
• Streptogramins also cause premature release of the peptide chain.

By targeting dissimilar stages of the mRNA translation, antimicrobial drugs can be changed if resistance develops to one or many of the drugs.

Inhibiting Essential Metabolite Synthesis

An antimetabolite is a chemic that inhibits the apply of a metabolite, a chemical that is role of normal metabolism.

Learning Objectives

Distinguish betwixt the three primary types of antimetabolite antibiotics (antifolates, pyrimidine and purine analogues)

Central Takeaways

Key Points

• The presence of antimetabolites tin have toxic effects on cells, such as halting cell growth or jail cell sectionalization.
• Antimetabolites are likewise used as antibiotics.
• The three primary types of antimetabolite antibiotics are antifolates, pyrimidine analogues and purine analogues.

Key Terms

• antimetabolite: Any substance that competes with or inhibits the normal metabolic procedure, often by acting as an analogue of an essential metabolite

An antimetabolite is a chemical that inhibits the use of a metabolite, a chemic that is part of normal metabolism. Such substances are often like in structure to the metabolite that they interfere with, such as antifolates that interfere with the utilize of folic acid. The presence of antimetabolites can have toxic effects on cells, such as halting cell growth or cell partitioning.

Antimetabolites are also used equally antibiotics. There are iii main types of antimetabolite antibiotics. The commencement, antifolates impair the function of folic acid leading to disruption in the product of Dna and RNA. For example, methotrexate is a folic acrid analogue, and owing to structural similarity with folic acrid, methotrexate binds and inhibits the enzyme dihydrofolate reductase, and thus prevents the formation of tetrahydrofolate. Because tetrahydrofolate is essential for purine and pyrimidine synthesis, its deficiency can atomic number 82 to inhibited production of DNA, RNA and proteins.

Folic Acrid Structure: This is the chemical structure of folic acid.

The second type of antimetabolite antibiotics consist of pyrimidine analogues which mimic the construction of metabolic pyrimidines. Three nucleobases found in nucleic acids, cytosine (C), thymine (T), and uracil (U), are pyrimidine derivatives and the pyrimidine analogues disrupt their germination and consequently disrupt DNA and RNA synthesis.

Pyrimidine Structure: This is the chemical structure of pyrimidine.

The purine analogues are the third type of antimetabolite antibiotics and they mimic the construction of metabolic purines. Ii of the four bases in nucleic acids, adenine and guanine, are purines. Purine analogues disrupt nucleic acrid production. For example, azathioprine is the main immunosuppressive cytotoxic substance that is widely used in transplants to control rejection reactions by inhibiting DNA synthesis in lymphocytes.

Purine Construction: This is the chemical structure of purine.

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Source: https://courses.lumenlearning.com/boundless-microbiology/chapter/functions-of-antimicrobial-drugs/

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