Nature Finds a Way: Antibiotic Resistance in Streptococcus Pneumoniae Introduction There is an estimate of 1 million children age five and under dying to Streptococcus pneumoniae (S. pneumoniae) each year (Schrag S, Beall B, and Dowell S 2001). This is due to the growing threat of bacteria becoming resistant to more and more antibiotics. The first case of S. pneumoniae becoming resistant to an antibiotic was in 1965, to penicillin, just twenty-two years after the drug was first created. This is cause for concern because should bacteria become resistant to antibiotics, we will have no way to treat bacteria-born disease. Fowler et al. have attempted to warn the world about the “antibiotic apocalypse” we have entered by continual use of …show more content…
Penicillin is crystalline in structure and can be dissolved in water; its structural formula can be seen in Figure 1. β-Lactam What is β-lactam? β-Lactam (beta-lactam) is a type of broad spectrum antibiotic classified by having a beta-lactam ring in the pharmaceutical drug’s chemical structure; penicillin has this ring present as seen in Figure 1. Kong, Schneper, and Mathee (2010) discuss that “beta-lactam antibiotics have been seen to have four independent effects on bacteria: (1) growth, viability, shape division, and integrity of bacterial cells; (2) a bacterium’s cell wall and enzymes associated with its biosynthesis; (3) cellular components that tightly bind penicillin and attempts to correlate binding with its physiological effects; (4) mutants with altered response to the β-lactam antibiotics. These ultimately became coherent.” How do β-lactam antibiotics work to fight against gram-positive bacteria? Transpeptidases are known for being sensitive to penicillin because their activity is inhibited by beta-lactam antibiotics. Transpeptidase is an enzyme that catalyzes the transpeptidation reaction (“Transpeptidase”). Transpeptidation, the chemical reaction conversion amino acid residue or a peptide residue is transferred from one amino compound to another (“Transpeptidation”). Once penicillin binds the PBP it is resilient to many forms of detachment, but can be removed by destroying the PBP through high
Throughout my life, adults have insisted the use of antibiotics to fight against the most inconsequential illnesses, whether it’s the cold or the flu. However, neither illness is due to invasion of bacteria. This misuse can lead to antibiotic resistance, also known as antimicrobial resistance(AMR), currently one of the central issues facing the public health system. While the process for antibiotic resistance occurs naturally through the process of adaptation, the mismanagement of antibiotic resources has accelerated the rate at which the bacteria adapt. The occurrence of this misinformation isn’t limited to a few adults: even some of my peers suggest taking antibiotics when faced with the flu. This leads to asking whether AMR is truly a problem and are present regulations enough to combat the issue.
Antibiotics are inarguably one of the greatest advances in medical science of the past century. Although the first natural antibiotic Penicillin was not discovered until 1928 by Scottish biologist Alexander Flemming, evidence exists that certain plant and mold growths were used to treat infections in ancient Egypt, ancient India, and classical Greece (Forrest, 1982). In our modern world with the advent of synthetic chemistry synthetic antibiotics like Erithromycin and its derivative Azithromycin have been developed. Antibiotics have many uses including the treatment of bacterial and protozoan infection, in surgical operations and prophylactically to prevent the development of an infection. Through these applications, antibiotics have saved countless lives across the world and radically altered the field of medicine. Though a wonderful and potentially lifesaving tool, antibiotic use is not without its disadvantages. Mankind has perhaps been too lax in regulation and too liberal in application of antibiotics and growing antibiotic resistance is the price we must now pay. A recent study showed that perhaps 70% of bacterial infections acquired during hospital visits in the United States are resistant to at least one class of antibiotic (Leeb, 2004). Bacteria are not helpless and their genetic capabilities have allowed them to take advantage of society’s overuse of antibiotics, allowing them to develop
Cephalexin, is a beta-lactam antibiotic. The antibiotic binds to specific penicillin-binding proteins positioned inside the bacterial cell wall, this inhibits the third and last stage of bacterial cell wall synthesis. The consequences are fatal to the susceptible bacteria but comparatively harmless for the human cells because the latter does not possess such a structure. Cell
They mimicked the cross-links, peptide bonds, that were used in Gram positive bacterium for the cell walls. As the cell wall of the bacterium attempted to use the penicillin-binding proteins as peptide bonds, no bonds would form and this destroyed or lysed the cell wall. Even more interesting is the way in which these bacterium became resistant. The bacterium began to mutate and started producing enzymes that destroy the penicillin structure. Which in turn would stop the penicillin from lysing the cell walls. In a short amount of time the Gram positive bacteria, such as Staphylococcus aureus, are able to have genetic mutations that allow the species to
The TEM-1 type of Beta-lactamase is the most common -lactamase enzyme found in E. coli. More importantly, this enzyme is highly interactive with antibiotics by inhibiting antibiotics from accomplishing their purpose of: halting the synthesis of bacteria cell walls to cease the spread and existence of the bacteria. This makes TEM type
Gram-Negative infections are a major cause of mortality in the hospital, intensive care unit and healthcare system. For years the Carbapenems have been a major last line player in eliminating infections. Carbapenem resistance is now increasing. Two drugs Avycaz and Zerbaxa are available to fight against those microbes with Carbapenem resistance. The newly approved combination drug Avycaz is composed of Ceftazidime and Avibactam. Ceftazidime is a 3rd generation cephalosporin. It inhibits bacterial cell wall synthesis by binding to the penicillin binding protein. Avibactam is a non- Beta lactam Beta Lactamase Inhibitor. It is essential in increasing the
β-lactam antibiotics (beta-lactam antibiotics) are a class of broad-spectrum antibiotics, consisting of all antibiotic agents that contain a beta-lactam ring in their molecular structures. They kill bacteria by generally inhibiting their cell wall synthesis. They are mainly active against gram positive bacterias but many gram negative bacteria are also susceptible to amoxicillin. Staphylococcus aureus being a gram positive bacteria are highly susceptible to amoxillin.
Penicillin (P-10) was measured at 0mm in diameters. There was no susceptibility. Therefore, with the zone size as 0, Escherichia coli was resistant to penicillin.
Antibiotics have played an essential role in the fight against diseases and infections since the 1940’s. Antibiotics are a leading cause for the rise of global average life expectancy in the 20th and 21st century. They have greatly reduced illnesses and deaths due to diseases. With the introductions of antibiotics in the 1940’s, like penicillin into clinical practice, formally deadly illnesses became immediately curable and saved thousands of lives (Yim 2006). Antibiotic use has been beneficial and when prescribed and taken correctly their effects on patients are exceedingly valuable. However, because these drugs have been used so widely and for such a long period of time the bacteria that the antibiotics are designed to kill have adapted,
When antibiotic is used most of the bacteria die but a few bacteria with antibiotic resistance gene survive and reproduce and pass this advantage to their offsprings. This selective pressure exists naturally, however antibiotic misuse can be accused for fastening the spread of the antibiotic resistance gene [Refer to figure 2] (Learn Genetics 2015). Consequently, inappropriate antibiotic intake will lead to a greater chance of superbugs being developed. Antibiotic resistance can be defined as a new ability which a bacterium has developed to stay unattached in the presence of an antibiotic that was previously effective to destroy the bacterium (ABC science 2015). Four key mechanisms that has been identified for bacterial antibiotic resistance can be listed as: producing enzymes that inhibit the functionality of the drug, reducing the effectiveness of the drug by producing targets against which the antibiotic, reducing the permeability of the drug into the bacterium and active export of antibiotics using various pumps (Pogson 2012). All these mechanisms can be developed by any of the bacteria when the corresponding mutated gene of antibacterial resistance is received. The genes code for specific proteins, and variation in the gene leads to alteration of the shape of proteins. This leads to changing the functionality
Generally, it is used to treat bacterial infections such as pneumonia, bronchitis, and ear, lung, skin, and urinary tract infections. Ampicillin comes in three forms: capsule, liquid, and pediatric drops. Capsules should be kept at room temperature and not stored in bathrooms to avoid excessive heat and moisture. Ampicillin and penicillin are both beta-lactamase agents. This means they affect the formation of the bacterial cell wall, specifically the final step: binary fission. Ampicillin is different from penicillin because of an amino group. This amino group allows ampicillin to also be effective on gram-negative cell
Antibiotics are amongst the most important medical discoveries and their introduction represents a remarkable success story (Hedin, 2011). The term antibiotics literally means against life (Walsh, 2000). Thus antibiotics can be used against any microbe such as bacteria, viruses, fungi, and protozoa. However, some people use the term to only apply to bacteria, but in this paper, the more appropriate term will be used.
In the past tense 60 years, antibiotic drugs have been critical to the fight against infectious disease caused by bacteria and other microbe. Antimicrobial chemotherapy has been a lead cause for the dramatic rise of norm life expectancy in the Twentieth Century. 1 However, disease-causing bug that have become resistant to antibiotic drug therapy are an increasing public health trouble. “Wound contagion, tuberculosis, pneumonia, gonorrhea, childhood ear infections, and septicemia are just a few of the diseases that have become hard to treat with antibiotics.” 2 One part of the job is that bacteria and other germ that cause infections are remarkably resilient and have developed several ways to resist antibiotics and other antimicrobial drug. 3 Another part of the problem is due to increasing use, and abuse, of existing
Penicillin, as well as other β- lactams, inhibits the enzyme that places essential cross-links between the individual polymer strings of the cell wall. It does this specifically by using the β-lactam ring to irreversibly block the active site of the enzyme, which catalyzes the reaction, transpeptidase. This inhibition allows the bacteria to newly synthesize a cell wall and to elongate, but not divide. This is due to the lack of cross-linking. The result is disruption of cell wall integrity, making the cell osmotically unstable and susceptible to lysis (Walsh, 2003). Penicillin reacts with the transpeptidase to form a stable acyl intermediate. The β-lactam ring acylates the hydroxyl group of one specific serine residue in the transpeptidase, producing an inactive penicilloyl-enzyme complex (Williams et al.,
Choice “A” is not the best answer. β-lactamase is anThe enzyme β-lactamase that hydrolyzes the β-lactam ring of penicillin, hence conferring antibiotic resistance to bacteria that secrete it. Clavulanic acid is an antibiotic that inactivates β-lactamase hence overcoming antibiotic resistance. It is given along with amoxicillin, not alone.