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191 Cards in this Set

  • Front
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Nutrition
Process by which chemical substances (nutrients) are acquired from the environment and used in cellular activities.
Essential nutrients
Must be provided to an organism.
Essential nutrients:
Macronutrients
Required in large quantities; play principal roles in cell structure and metabolism.

Proteins, carbohydrates
Essential nutrients:
Micronutrients or trace elements
Required in small amounts; involved in enzyme function and maintenance of protein structure.

Manganese, zinc, nickel
Organic nutrients
Contain carbon and hydrogen atoms and are usually the products of living things.

Methane (CH4), carbohydrates, lipids, proteins, and nucleic acids
Inorganic nutrients
Atom or molecule that contains a combination of atoms other than carbon and hydrogen.

Metals and their salts (magnesium sulfate, ferric nitrate, sodium phosphate), gases (oxygen, carbon dioxide) and water
Microbial Cytoplasm
70% water

Proteins

96% of cell is composed of 6 elements:
Carbon
Hydrogen
Oxygen
Phosphorous
Sulfur
Nitrogen
Carbon Sources
Heterotroph: Must obtain carbon in an organic form made by other living organisms such as proteins, carbohydrates, lipids, and nucleic acids.

Autotroph: An organism that uses CO2, an inorganic gas as its carbon source.
Not nutritionally dependent on other living things.
Nitrogen Sources
Main reservoir is nitrogen gas (N2); 79% of earth’s atmosphere is N2.


Nitrogen is part of the structure of proteins, DNA, RNA and ATP – these are the primary source of N for heterotrophs i.e., they must consume those made by other organisms to use in their own DNA, RNA, ATP, etc…

Some bacteria and algae use inorganic N sources.

Some bacteria can fix N2.

Regardless of how N enters the cell, it must be converted to NH3, the only form that can be combined with carbon to synthesize amino acids, etc.
Oxygen Sources
Major component of carbohydrates, lipids, nucleic acids, and proteins.

Plays an important role in structural and enzymatic functions of cell.

Component of inorganic salts (sulfates, phosphates, nitrates) and water
O2 makes up 20% of atmosphere.

Essential to metabolism of many organisms.
Hydrogen Sources
Major element in all organic compounds and several inorganic ones (water, salts, and gases.)

Gases are produced and used by microbes.

Roles of hydrogen:
Maintaining pH
Acceptor of oxygen during cell respiration.
Gradient creation in cell respiration.
Phosphorous (Phosphate Sources)
Main inorganic source is phosphate (PO4-3) derived from phosphoric acid (H3PO4) found in rocks and oceanic mineral deposits.

Key component of nucleic acids, essential to genetics.

Serves in energy transfers (ATP)
Sulfur Sources
Widely distributed in environment, rocks; sediments contain sulfate, sulfides, hydrogen sulfide gas and sulfur.

Essential component of some vitamins and the amino acids: methionine and cysteine.

Contributes to stability of proteins by forming disulfide bonds.
Other Nutrients Important in Microbial Metabolism:
Potassium
Essential to protein synthesis and membrane function.
Other Nutrients Important in Microbial Metabolism:
Sodium
Important to some types of cell transport.
Other Nutrients Important in Microbial Metabolism:
Calcium
Cell wall and endospore stabilizer.
Other Nutrients Important in Microbial Metabolism:
Magnesium
Component of chlorophyll; membrane and ribosome stabilizer.
Other Nutrients Important in Microbial Metabolism:
Iron
Component of proteins of cell respiration.
Chemotroph
Gain energy from chemical compounds.
Phototrophs
Gain energy through photosynthesis.
Photoautotrophs
Photosynthesis
Oxygenic photosynthesis
Anoxygenic photosynthesis
Chemoautotrophs
Survive totally on inorganic substances.
Methanogens
A kind of chemoautotroph, produce methane gas under anaerobic conditions.
Heterotrophs and Their Energy Sources
Majority are chemoheterotrophs.
Aerobic respiration.

Two categories:
Saprobes: free-living microorganisms that feed on organic detritus from dead organisms.
Opportunistic pathogen.
Facultative parasite.

Parasites: derive nutrients from host.
Pathogens
Some are obligate parasites.
Passive transport
Does not require energy; substances exist in a gradient and move from areas of higher concentration toward areas of lower concentration.

Diffusion
Osmosis – diffusion of water.
Facilitated diffusion – requires a carrier.
Active transport
Requires energy and carrier proteins; gradient independent.

Active transport
Group translocation – transported molecule chemically altered
Bulk transport – endocytosis, exocytosis, pinocytosis.
Osmosis
The movement of water across a selectively permeable membrane.
Hypertonic solution
Concentration is greater than the concentration inside the cell.
Hypotonic solution
Concentration is less than the concentration inside the cell.
Isotonic solution
Concentration is equal with the concentration inside the cell.
Facilitated Diffusion
1. Does not use energy (passive).

2. Uses a protein channel.

3. Protein changes shape to allow molecule inside or outside of cell.

4. Relies on a concentration gradient.
Carrier mediated active transport
1. Requires energy (Active transport).

2. Runs independent of the concentration gradient.
Endocytosis
Requires energy (active transport). Object is engulfed by cell membrane to be carried into the cell in a vesicle.
Exocytosis
Requires energy (active transport). Object is expelled from the membrane.
Niche
Totality of adaptations organisms make to their habitat.
Environmental factors affect the function of metabolic enzymes:
Temperature
Oxygen requirements
pH
Osmotic pressure
Barometric pressure
Minimum temperature
Lowest temperature that permits a microbe’s growth and metabolism.
Maximum temperature
Highest temperature that permits a microbe’s growth and metabolism.
Optimum temperature
Promotes the fastest rate of growth and metabolism.
Psychrophiles
Optimum temperature below 15C
Capable of growth at 0C
Mesophiles
Optimum temperature 20-40C Most human pathogens
Thermophiles
Optimum temperature greater than 45C.
Toxic Products of Oxygen
1. Singlet oxygen (1O2)

2. Superoxide ion (O2-)

3. Peroxide (H2O2)

4. Hydroxyl radicals (OH-)
Enzymes that neutralize the toxic effects of oxygen:
1. Superoxide dismutase
2. Catalase
Aerobe
Utilizes oxygen and can detoxify it.
Obligate aerobe
Cannot grow without oxygen.
Facultative anaerobe
Utilizes oxygen but can also grow in its absence.
Microaerophilic
Requires only a small amount of oxygen.
Anaerobe
Does not utilize oxygen.
Obligate anaerobe
Lacks the enzymes to detoxify oxygen so cannot survive in an oxygen environment.
Aerotolerant anaerobes
Do not utilize oxygen but can survive and grow in its presence.
Capnophile
Grows best at higher CO2 tensions than normally present in the atmosphere.
Majority of microorganisms grow at a pH between:
6 and 8
Obligate acidophiles
Grow at extreme acid pH.
Alkalinophiles
Grow at extreme alkaline pH.
Halophiles
Require a high concentration of salt.
Osmotolerant
Do not require high concentration of solute but can tolerate it when it occurs.
Symbiotic:
Organisms live in close nutritional relationships; required by one or both members.

Mutualism
Commensalism
Parasitism
Non Symbiotic:
Organisms are free-living; relationships not required for survival.

Synergism
Antagonism
Mutualism
Obligatory, dependent; both members benefit.
Commensalism
The commensal benefits; other member not harmed.
Parasitism
Parasite is dependent and benefits; host is harmed.
Synergism
Members cooperate and share nutrients.
Antagonism
Some members are inhibited or destroyed by others.
Interrelationships Between Microbes and Humans
Human body is a rich habitat for symbiotic bacteria, fungi, and a few protozoa - normal microbial flora.

Commensal, parasitic, and synergistic relationships
Microbial Biofilms
1. Free swimming cells settle on a surface and remain there.

2. Cells synthesize a sticky matrix that holds them tightly to the substrate.

3. When biofilm grows to a certain density (quorum), the cells release inducer molecules that can coordinate a response.

4. Enlargement of one cell to show genetic induction. Inducer molecule stimulates expression of a particular gene and synthesis of a protein product, such as an enzyme.

5. Cells secrete their enzymes in unison to digest food particles.

6. Dominate the structure of most natural environments on earth.
Quorum Sensing
Communicate and cooperate in the formation and function of biofilms.
Binary Fission
Parent cell enlarges, duplicates its chromosome, and forms a central transverse septum dividing the cell into two daughter cells.
Generation, or Doubling Time
Time required for a complete fission cycle.

Generation times vary from minutes to days.
Exponential Growth
Each new fission cycle increases the population by a factor of 2.

Generation times vary from minutes to days.
Growth Curve
Populations typically display a predictable growth pattern over time.

1. Lag Phase
2. Exponential Growth Phase
3. Stationary Phase
4. Death Phase
Lag phase
“Flat” period of adjustment, enlargement; little growth.
Exponential growth phase
A period of maximum growth will continue as long as cells have adequate nutrients and a favorable environment.
Stationary phase
Rate of cell growth equals rate of cell death caused by depleted nutrients and O2, excretion of organic acids and pollutants.
Death phase
As limiting factors intensify, cells die exponentially.
Methods of Analyzing Population Growth
1. Turbidometry – most simple.
2. Degree of cloudiness, turbidity, reflects the relative population size.

3. Enumeration of bacteria:
Viable colony count (AKA Viable Plate Count)
Direct cell count – count all cells present; automated or manual.
Metabolism
All chemical and physical workings of a cell.
Catabolism
Degradative; breaks the bonds of larger molecules forming smaller molecules; releases energy.
Anabolism
Biosynthesis; process that forms larger macromolecules from smaller molecules; requires energy input.
Enzymes
1. Biological catalysts that increase the rate of a chemical reaction by lowering the energy of activation.

2. The energy of activation is the resistance to a reaction.

3. The enzyme is not permanently altered in the reaction.
4. Enzyme promotes a reaction by serving as a physical site for specific substrate molecules to position.

5. Most composed of protein.
Enzyme Structure
Simple enzymes – consist of protein alone.

Conjugated enzymes or holoenzymes – contain protein and nonprotein molecules.

Apoenzyme – protein portion.

Cofactors – nonprotein portion.
Metallic cofactors: iron, copper, magnesium
Coenzymes, organic molecules: vitamins.
Active Site, or Catalytic Site
Site for substrate binding in an enzymatic reaction.
Induced Fit
A temporary enzyme-substrate union occurs when substrate moves into active site.
Exoenzymes
Transported extracellularly, where they break down large food molecules or harmful chemicals.

Cellulase, amylase, penicillinase.
Endoenzymes
retained intracellularly and function there.

Most enzymes are endoenzymes.
Constitutive enzymes
Always present, always produced in equal amounts or at equal rates, regardless of amount of substrate.

Enzymes involved in glucose metabolism.
Regulated enzymes
Not constantly present. Production is turned on (induced) or turned off (repressed) in response to changes in concentration of the substrate.
Synthesis or Condensation Reactions
Anabolic reactions to form covalent bonds between smaller substrate molecules, require ATP, release one molecule of water for each bond formed (AKA dehydration).
Hydrolysis Reactions
Catabolic reactions that break down substrates into small molecules; requires the input of water to break bonds.
Sensitivity of Enzymes to Their Environment
Activity of an enzyme is influenced by cell’s environment.

Enzymes operate under temperature, pH, and osmotic pressure of organism’s habitat.

When enzymes are subjected to changes in organism’s habitat they become unstable.
Labile
Chemically unstable enzymes.
Denaturation
Weak bonds that maintain the shape of the apoenzyme are broken.
Competitive Inhibition
Substance that resembles normal substrate competes with substrate for active site.
Noncompetitive Inhibition
Enzymes are regulated by the binding of molecules other than the substrate on the active site.
Noncompetitive Inhibition: Enzyme Repression
Inhibits at the genetic level by controlling synthesis of key enzymes (Blocks synthesis).
Noncompetitive Inhibition:
Enzyme Induction
Enzymes are made only when suitable substrates are present.
Endergonic reactions
Consume energy.

Energy+A+B+Enzyme = C
Exergonic reactions
Release energy.

X+Y+Enzyme = Z+Energy
Cell Energetics
Energy present in chemical bonds of nutrients are trapped by specialized enzyme systems as the bonds of the nutrients are broke.

Energy released is temporarily stored in high energy phosphate molecules. The energy of these molecules is used in endergonic cell reactions.
Redox reactions
1. Always occur in pairs.

2. There is an electron donor and electron acceptor which constitute a redox pair.

3. Process salvages electrons and their energy.

4. Released energy can be captured to phosphorylate ADP or another compound.
Electron and Proton Carriers
Repeatedly accept and release electrons and hydrogen to facilitate the transfer of redox energy.

Most carriers are coenzymes:
1. NAD
2. FAD
3.NADP
4.Coenzyme A
5. Compounds of the respiratory chain.
Adenosine Triphosphate: ATP
1. Metabolic “currency”.

2. Three part molecule consisting of:
-Adenine – a nitrogenous base
-Ribose – a 5-carbon sugar
-3 phosphate groups.

3. ATP utilization and replenishment is a constant cycle in active cells.

4. Removal of the terminal phosphate releases energy.
Substrate-Level Phosphorylation
Transfer of phosphate group from a phosphorylated compound (substrate) directly to ADP to for ATP.
Oxidative Phosphorylation
Series of redox reactions occurring during respiratory pathway to for ATP.
Photophosphorylation
ATP is formed utilizing the energy of sunlight.
Bioenergetics
Study of the mechanisms of cellular energy release.

Includes catabolic and anabolic reactions.

Primary catabolism of fuels (glucose) proceeds through a series of three coupled pathways:
1. Glycolysis
2. Kreb’s cycle
3. Respiratory chain, electron transport.
Aerobic Respiration
Series or enzyme-catalyzed reactions in which electrons are transferred from fuel molecules (glucose) to oxygen as a final electron acceptor.

1. Glycolysis – glucose (6C) is oxidized and split into 2 molecules of pyruvic acid (3C), NADH is generated.

2. TCA – processes pyruvic acid and generates 3 CO2 molecules , NADH and FADH2 are generated.

3. Electron transport chain – accepts electrons from NADH and FADH; generates energy through sequential redox reactions called oxidative phosphorylation.
Anaerobic Respiration
Functions like aerobic respiration except it utilizes oxygen containing ions, rather than free oxygen, as the final electron acceptor.
-Nitrate (NO3-) and nitrite (NO2).

Most obligate anaerobes use the H+ generated during glycolysis and the Kreb’s cycle to reduce some compound other than O2.
Fermentation
Incomplete oxidation of glucose or other carbohydrates in the absence of oxygen.

Uses organic compounds as terminal electron acceptors.

Yields a small amount of ATP.

Production of ethyl alcohol by yeasts acting on glucose.

Formation of acid, gas, and other products by the action of various bacteria on pyruvic acid.

Pyruvic Acid is changed to lactic acid.
Electron Transport and Oxidative Phosphorylation
Final processing of electrons and hydrogen and the major generator of ATP.

Chain of redox carriers that receive electrons from reduced carriers (NADH and FADH2).

ETS shuttles electrons down the chain, energy is released and subsequently captured and used by ATP synthase complexes to produce ATP – Oxidative phosphorylation.
Chemiosmosis
The movement of ions across a selectively-permiable membrane, down their electrochemical gradient. More spacifically for the release of ATP.

As the electron transport carriers shuttle electrons, they actively pump hydrogen ions (protons) across the membrane setting up a gradient of hydrogen ions – proton motive force.

Hydrogen ions diffuse back through the ATP synthase complex causing it to rotate, causing a 3-dimensional change resulting in the production of ATP.
Terminal Step in Aerobic Respiration
Oxygen accepts 2 electrons from the ETS and then picks up 2 hydrogen ions from the solution to form a molecule of water. Oxygen is the final electron acceptor

2H+ + 2e- + ½O2 → H2O
Amphibolic
Many pathways of metabolism are bi-directional or amphibolic.

Catabolic pathways contain molecular intermediates (metabolites) that can be diverted into anabolic pathways.

Pyruvic acid can be converted into amino acids through amination.

Amino acids can be converted into energy sources through deamination.

Glyceraldehyde-3-phosphate can be converted into precursors for amino acids, carbohydrates, and fats.
Photosynthesis:
Light-Dependent
Photons are absorbed by chlorophyll, carotenoid, and phycobilin pigments.

Water split by photolysis, releasing O2 gas and provide electrons to drive photophosphorylation.

Released light energy used to synthesize ATP and NADPH.
Photosynthesis:
Light-Independent Reaction
Dark reactions.

Calvin cycle – uses ATP to fix CO2 to ribulose-1,5-bisphosphate and convert it to glucose.
Genetics
the study of heredity
Genome
sum total of genetic material of a cell (chromosomes + mitochondria/chloroplasts and/or plasmids)
Genome of cells – DNA
Genome of viruses – DNA or RNA
genes
Chromosome is subdivided into genes, the fundamental unit of heredity responsible for a given trait
genotype
All types of genes constitute the genetic makeup
phenotype
The expression of the genotype creates observable traits
DNA
Two strands twisted into a double helix
Basic unit of DNA structure is a nucleotide
Each nucleotide consists of 3 parts:
A 5 carbon sugar – deoxyribose
A phosphate group
A nitrogenous base – adenine, guanine, thymine, cytosine
Nucleotides covalently bond to form a sugar-phosphate linkage – the backbone
Each sugar attaches to two phosphates –
5′ carbon and 3′ carbon
DNA Replication
Making an exact duplicate of the DNA involves 30 different enzymes
Begins at an origin of replication
Helicase unwinds and unzips the DNA double helix
An RNA primer is synthesized at the origin of replication
DNA polymerase III adds nucleotides in a 5′ to 3′ direction
Leading strand – synthesized continuously in 5′ to 3′ direction
Lagging strand – synthesized 5′ to 3′ in short segments; overall direction is 3′ to 5
semiconservative
DNA replication is semiconservative because each chromosome ends up with one new strand of DNA and one old strand
transcription
Information stored on the DNA molecule is conveyed to RNA molecules through the process of transcription
translation
The information contained in the RNA molecule is then used to produce proteins in the process of translation
Gene-Protein Connection
Each triplet of nucleotides on the RNA specifies a particular amino acid
A protein’s primary structure determines its shape and function
Proteins determine phenotype. Living things are what their proteins make them.
DNA is mainly a blueprint that tells the cell which kinds of proteins to make and how to make them
RNAs
Single-stranded molecule made of nucleotides
5 carbon sugar is ribose
4 nitrogen bases – adenine, uracil, guanine, cytosine
Phosphate
Messenger RNA (mRNA
carries DNA message through complementary copy; message is in triplets called codons
Transfer RNA (tRNA)
made from DNA; secondary structure creates loops; bottom loop exposes a triplet of nucleotides called anticodon which designates specificity and complements mRNA; carries specific amino acids to ribosomes
Ribosomal RNA –(rRNA)
component of ribosomes where protein synthesis occurs
how many Termination codons
3
Polyribosomal complex
allows for the synthesis of many protein molecules simultaneously from the same mRNA molecule
start codon
AUG
AUG
formyl-methionine
operons
a set of genes, all of which are regulated as a single unit
types of operons
Inducible
operon is turned ON by substrate: catabolic operons - enzymes needed to metabolize a nutrient are produced when needed
types of operons
–Repressible
genes in a series are turned OFF by the product synthesized; anabolic operon –enzymes used to synthesize an amino acid stop being produced when they are not needed
Lactose Operon
Inducible Operon
Normally off
Lactose turns the operon on
Regulator
gene that codes for repressor
Arginine Operon
Repressible
Normally on and will be turned off when the product of the pathway is no longer required
When excess arginine is present, it binds to the repressor and changes it. Then the repressor binds to the operator and blocks arginine synthesis.
mutation
A change in phenotype due to a change in genotype
wild type (wild strain)
A natural, nonmutated characteristic
mutant strain
An organism that has a mutation
Spontaneous mutations
random change in the DNA due to errors in replication that occur without known cause
Induced mutations
result from exposure to known mutagens, physical (primarily radiation) or chemical agents that interact with DNA in a disruptive manner
Point mutation
addition, deletion, or substitution of a few bases
Missense mutation
causes change in a single amino acid
Nonsense mutation
changes a normal codon into a stop codon
Silent mutation
alters a base but does not change the amino acid
Back-mutation –
when a mutated gene reverses to its original base composition
Frameshift mutation
when the reading frame of the mRNA is altered
The Ames Test
Any chemical capable of mutating bacterial DNA can similarly mutate mammalian DNA
Agricultural, industrial, and medicinal compounds are screened using the Ames test
Genetic recombination
occurs when an organism acquires and expresses genes that originated in another organism
3 means for genetic recombination in bacteria:
Conjugation
Transformation
Transduction
Transformation
chromosome fragments from a lysed cell are accepted by a recipient cell; the genetic code of the DNA fragment is acquired by the recipient
Donor and recipient cells can be unrelated
Useful tool in recombinant DNA technology
Transduction
bacteriophage serves as a carrier of DNA from a donor cell to a recipient cell
Generalized transduction
random fragments of disintegrating host DNA are picked up by the phage during assembly; any gene can be transmitted this way
Specialized transduction
a highly specific part of the host genome is regularly incorporated into the virus
Transposons
Special DNA segments that have the capability of moving from one location in the genome to another – “jumping genes
Microbial Control methods:
Physical Agents
Heat (Dry & Moist)
Radiation
Microbial Control methods:
Chemical Agents
Gase
Liquids
Microbial Control methods:
Mechanical Removal Methods
Filtration (Air & Liquids)
Physical Agents
Sterilization:
Incineration
Dry Oven
Steam Under Pressure
Ionizing/X Ray, Cathode, Gamma

Disinfection:
Boiling/Hot Water/Pasteurization
Nonionizing/UV
Chemical Agents:
Sterilazition:
Gases
Liquids

Disinfection:
Gases
Liquids

Antisepsis:
Liquids
Mechanical Removal Methods
Sterilization:
Filtration/Liquids

Disinfection:
Filtration/ Air
Disinfection
The destruction or removal of vegatitive pathogens but not bacterial endospores. Usually used only on inanimate objects.
Sterilization
The complete removal or destruction of all viable microorganisims. Used on inanimate objects.
Antisepsis
Chemicals applied to body surfaces to destroy or inhibit vegetative pathogens.
Relative Resistance of Microbes
Highest resistance
Prions, bacterial endospores
Relative Resistance of Microbes
Moderate resistance
Pseudomonas sp.
Mycobacterium tuberculosis
Staphylococcus aureus
Protozoan cysts
Relative Resistance of Microbes
Least resistance
Most bacterial vegetative cells
Fungal spores and hyphae, yeast
Enveloped viruses
Protozoan trophozoites
Sanitization
any cleansing technique that mechanically removes microbes
Degermation
reduces the number of microbes through mechanical means
Antimicrobial Agents’ Modes of Action
Cellular targets of physical and chemical agents
The cell wall – cell wall becomes fragile and cell lyses; some antimicrobial drugs, detergents, and alcohol
The cell membrane – loses integrity; detergent surfactants
Protein and nucleic acid synthesis – prevention of replication, transcription, translation, peptide bond formation, protein synthesis; chloramphenicol, ultraviolet radiation, formaldehyde
Proteins – disrupt or denature proteins; alcohols, phenols, acids, heat
Thermal death time (TDT)
shortest length of time required to kill all test microbes at a specified temperature
Thermal death point (TDP)
lowest temperature required to kill all microbes in a sample in 10 minutes
Some desirable qualities of chemicals:
Rapid action in low concentration
Solubility in water or alcohol, stable
Broad spectrum, low toxicity
Penetrating
Noncorrosive and nonstaining
Affordable and readily available
Levels of Chemical Decontamination
High-level germicides
kill endospores; may be sterilants
Devices that are not heat sterilizable and intended to be used in sterile environments (body tissue)
Levels of Chemical Decontamination
Intermediate-level
kill fungal spores (not endospores), tubercle bacillus, and viruses
Used to disinfect devices that will come in contact with mucous membranes but are not invasive
Levels of Chemical Decontamination
Low-level
eliminate only vegetative bacteria, vegetative fungal cells, and some viruses
Clean surfaces that touch skin but not mucous membranes
selectively toxic
drugs should kill or inhibit microbial cells without simultaneously damaging host tissues
Mechanisms of Drug Action
Inhibition of cell wall synthesis
Breakdown of cell membrane structure or function
Inhibition of nucleic acid synthesis, structure or function
Inhibition of protein synthesis
Blocks on key metabolic pathways
Narrow-spectrum
effective on a small range of microbes
Target a specific cell component that is found only in certain microbes
Broad-spectrum
greatest range of activity
Target cell components common to most pathogens (ribosomes)
Competitive inhibition
drug competes with normal substrate for enzyme’s active site
Synergistic effect
the effects of a combination of antibiotics are greater than the sum of the effects of the individual antibiotics
Antibacterial Drugs that Act on the Cell Wall
Beta-lactam antimicrobials - all contain a highly reactive 3 carbon, 1 nitrogen ring
Primary mode of action is to interfere with cell wall synthesis
Greater than ½ of all antimicrobic drugs are beta-lactams
Penicillins and cephalosporins most prominent beta-lactams
The Acquisition of Drug Resistance
Adaptive response in which microorganisms begin to tolerate an amount of drug that would ordinarily be inhibitory; due to genetic versatility or variation; intrinsic and acquired
Acquired resistance:
Spontaneous mutations in critical chromosomal genes
Acquisition of new genes or sets of genes via transfer from another species
Originates from resistance factors (plasmids) encoded with drug resistance, transposons
Mechanisms of Drug Resistance
Drug inactivation by acquired enzymatic activity – penicillinases
Decreased permeability to drug or increased elimination of drug from cell – acquired or mutation
Change in drug receptors – mutation or acquisition
Change in metabolic patterns – mutation of original enzyme
Considerations in Selecting an Antimicrobial Drug
Identify the microorganism causing the infection
Test the microorganism’s susceptibility (sensitivity) to various drugs in vitro when indicated
The overall medical condition of the patient
Cephalosporins
Account for one-third of all antibiotics administered
Synthetically altered beta-lactam structure
Relatively broad-spectrum, resistant to most penicillinases, and cause fewer allergic reactions
Some are given orally; many must be administered parenterally
Generic names have root – cef, ceph, or kef
Cephalosporins
4 generations exist: each group more effective against gram-negatives than the one before with improved dosing schedule and fewer side effects
First generation
Second generation
Third generation
Fourth generation