Microbiology Terms Starting With R
Microbiology Glossary: R
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Rabies
/ RAY-beez / · Latin rabere (to rave)
Rabies is a fatal viral encephalitis caused by rabies lyssavirus, transmitted primarily through the saliva of infected mammals and characterized by progressive neurological deterioration that is almost universally lethal once clinical symptoms appear.
Rabies lyssavirus belongs to the family Rhabdoviridae and carries a negative-sense, single-stranded RNA genome. After entering a bite wound, the virus binds to nicotinic acetylcholine receptors at the neuromuscular junction and travels by retrograde axonal transport toward the central nervous system at a rate of roughly 50 to 100 millimeters per day, which explains why bites closer to the head carry shorter incubation periods. Once the virus reaches the brain, it causes acute encephalitis marked by agitation, hydrophobia, and autonomic instability.
Post-exposure prophylaxis, a series of vaccine doses combined with rabies immunoglobulin administered promptly after a high-risk exposure, is nearly 100 percent effective at preventing disease if started before symptoms develop.
The Milwaukee Protocol, an experimental treatment attempted in 2004 on teenager Jeanna Giese, induced a medically supervised coma to protect the brain while the immune system cleared the virus; Giese survived, becoming one of fewer than 20 people ever documented to recover from symptomatic rabies without prior vaccination.
Rabies spreads only through dog bites. Bats, raccoons, skunks, and foxes are all significant wildlife reservoirs in North America, and bat bites, which can leave marks too small to notice, account for the majority of human rabies cases in the United States.
The little brown bat (Myotis lucifugus) is among the most common wildlife sources of human rabies exposure in North America. Rabies lyssavirus can incubate in bats for weeks to months before neurological signs appear, during which time an infected bat may still fly and bite, making surveillance of bat populations a priority for public health agencies.
Fun Facts About the Nervous System →Reservoir Host
/ REZ-er-vwar HOHST / · Old French reservoir; Latin hospes, host
Reservoir Host is an animal or environmental source that maintains a pathogen through long-term infection without developing serious disease, providing a persistent source from which the pathogen can spread to other species.
Reservoir hosts typically share a long evolutionary history with their pathogens, and this coevolution has produced immunological adaptations that limit disease. Bats, for example, tolerate a remarkable diversity of RNA viruses, including the ancestors of SARS-CoV-2, Ebola virus, and Marburg virus, partly because their constitutively active interferon signaling suppresses viral replication without triggering the damaging inflammatory responses seen in naive hosts. Rodents maintain Yersinia pestis, the plague bacterium, in flea-mediated transmission cycles across grassland ecosystems on multiple continents, sustaining the pathogen between human outbreaks.
When a pathogen spills over into a host species that lacks coevolved tolerance, such as humans encountering a bat coronavirus for the first time, the mismatch between viral replication rate and host immune response can produce severe or fatal disease.
White-footed mice (Peromyscus leucopus) are the primary reservoir for Borrelia burgdorferi, the bacterium that causes Lyme disease in the northeastern United States. Studies have shown that a single mouse can infect up to 95 percent of the larval ticks that feed on it, making this one rodent species the principal amplifier of Lyme disease risk across entire woodland ecosystems.
A reservoir host must show obvious signs of illness. Reservoir hosts often carry pathogens at high titers with minimal or no clinical signs, precisely because natural selection favors host survival and continued pathogen transmission over acute disease.
Fruit bats of the genus Pteropus are reservoir hosts for Nipah virus across South and Southeast Asia, shedding the virus in urine, saliva, and partially eaten fruit without developing illness. Spillover events to pigs or humans have recorded case fatality rates between 40 and 75 percent, illustrating the stark difference in outcome between a coevolved reservoir and a naive incidental host.
Resistance Gene
/ reh-ZIS-tuns JEEN / · Latin resistere (to oppose) + Greek genesis (origin)
Resistance Gene is a gene encoding a product that confers on the host bacterium the ability to survive antibiotic concentrations that would otherwise inhibit or kill susceptible strains.
Resistance genes encode diverse mechanisms, including enzymes that destroy antibiotics, proteins that pump drugs out of the cell, and altered targets that drugs no longer bind effectively. Beta-lactamases, for example, hydrolyze the beta-lactam ring of penicillins and cephalosporins, rendering these drugs inactive before they can inhibit cell wall synthesis. Many of these genes sit on mobile genetic elements such as plasmids, transposons, and integrons, which transfer between bacterial cells through conjugation, transformation, or transduction.
A single plasmid can carry multiple resistance genes simultaneously, allowing one horizontal transfer event to confer resistance to several unrelated drug classes at once.
The New Delhi metallo-beta-lactamase gene (blaNDM-1), first identified in a Swedish patient treated in India in 2008, encodes an enzyme that destroys nearly all beta-lactam antibiotics, including carbapenems that are typically reserved as last-resort treatments.
Are Enzymes Proteins? →One resistance gene protects against every antibiotic. Resistance genes are specific: a gene encoding a beta-lactamase destroys penicillins but offers no protection against fluoroquinolones or aminoglycosides.
The blaTEM gene encodes a beta-lactamase enzyme carried on plasmids by many Gram-negative bacteria, including Escherichia coli. More than 200 blaTEM variants have been described, and related enzymes hydrolyze the beta-lactam ring of ampicillin and other drugs in clinical isolates worldwide.
Reverse Transcriptase
/ reh-VERS tran-SKRIP-taze / · Latin reversus (turned back) + transcribere (to copy) + -ase
Reverse Transcriptase is an enzyme encoded by retroviruses and some other mobile genetic elements that synthesizes a DNA strand using an RNA molecule as its template.
Reverse transcriptase in HIV (human immunodeficiency virus) copies the viral RNA genome into DNA at a rate of roughly 100 nucleotides per second, far slower than most cellular DNA polymerases. Critically, the enzyme lacks a proofreading domain, introducing approximately one error per 10,000 nucleotides copied; across a genome of about 9,700 nucleotides, nearly every new viral copy carries at least one mutation. This high error rate generates enormous genetic diversity within a single infected patient, accelerating the emergence of drug-resistant variants.
After synthesizing a complementary DNA strand to form an RNA-DNA hybrid, the enzyme’s built-in RNase H activity degrades the original RNA template, and reverse transcriptase then synthesizes the second DNA strand to complete a double-stranded DNA copy ready for integration into the host chromosome.
Researchers harnessed reverse transcriptase as a laboratory tool in the early 1970s, when David Baltimore and Howard Temin independently discovered the enzyme in 1970, work that earned them the Nobel Prize in Physiology or Medicine in 1975. Scientists now use purified reverse transcriptase routinely to convert messenger RNA into complementary DNA (cDNA) for gene expression studies and RNA sequencing.
Building Blocks of Nucleic Acids →DNA is always copied only from DNA. Reverse transcriptase copies RNA into DNA, a direction of information flow that retroviruses depend on to establish permanent infection.
HIV uses reverse transcriptase within hours of entering a CD4-positive T cell to convert its RNA genome into double-stranded DNA. The resulting DNA copy is about 9,700 nucleotides long and can integrate into the host chromosome, where it may persist silently for decades.
Rhizobium
/ ry-ZOH-bee-um / · Greek rhiza, root; bios, life
Rhizobium is a genus of soil bacteria that fixes atmospheric nitrogen inside root nodules formed through a symbiotic relationship with leguminous plants, converting nitrogen gas into ammonia that the host plant can absorb as a nutrient.
Atmospheric nitrogen gas makes up about 78% of air, yet plants cannot absorb it directly because the triple bond holding the two nitrogen atoms together requires more energy to break than most organisms can supply. Rhizobium bacteria produce nitrogenase, an enzyme complex that cleaves this bond and combines nitrogen with hydrogen to yield ammonia, a form plants readily take up. The plant supplies the bacteria with photosynthetically derived sugars in return, and the root nodule maintains very low oxygen concentrations using a protein called leghemoglobin, which protects the oxygen-sensitive nitrogenase from inactivation.
A single soybean (Glycine max) plant can host nodules fixing more than 100 kilograms of nitrogen per hectare per growing season when conditions are optimal, reducing the need for synthetic nitrogen fertilizer.
Leghemoglobin, the oxygen-buffering protein inside legume root nodules, is closely related to animal hemoglobin and gives active nodules a distinctive pink or red color. Its presence in a nodule is a reliable field indicator that nitrogen fixation is occurring.
Are Enzymes Proteins? →Rhizobium is a fertilizer chemical added to soil. Rhizobium is a living bacterium that must colonize legume roots and form nodules before any nitrogen fixation occurs; simply adding the cells to bulk soil without a compatible host plant produces no fixed nitrogen.
Rhizobium leguminosarum forms nodules on the roots of peas (Pisum sativum) and clovers (Trifolium spp.). Each nodule can contain several hundred million bacterial cells, and a well-nodulated pea crop can fix between 50 and 200 kilograms of nitrogen per hectare over a single growing season.
Rickettsia
/ rih-KET-see-ah / · Howard Taylor Ricketts (1871-1910), who discovered it
Rickettsia are obligate intracellular bacteria transmitted to humans primarily through the bites of infected arthropods such as ticks, fleas, and lice, and they cause diseases including Rocky Mountain spotted fever and epidemic typhus.
Unlike most bacteria that grow freely in nutrient broths, Rickettsia cannot replicate outside a living eukaryotic cell because they lack the metabolic machinery to produce their own ATP independently. After an infected tick or louse deposits the bacteria during feeding, Rickettsia enter host endothelial cells lining blood vessels, escape the phagosome before it fuses with a lysosome, and replicate directly in the cytoplasm. Rickettsia prowazekii, the agent of epidemic typhus, spreads between cells by hijacking the host cell’s actin polymerization machinery, propelling itself through the cytoplasm and into adjacent cells.
Rocky Mountain spotted fever, caused by Rickettsia rickettsii, kills roughly 20% of untreated patients, making early antibiotic treatment with doxycycline critical to survival.
During World War I, epidemic typhus caused by Rickettsia prowazekii killed an estimated 3 million people in Eastern Europe between 1918 and 1922, more deaths than many individual battles of the war. The disease spread explosively in crowded, louse-infested conditions.
Rickettsia are viruses because they live inside cells. Rickettsia are bacteria with a cell wall, ribosomes, and their own DNA; they evolved an obligate intracellular lifestyle but retain all the structural features that define bacteria.
Rickettsia rickettsii causes Rocky Mountain spotted fever after transmission by the American dog tick (Dermacentor variabilis) or the Rocky Mountain wood tick (Dermacentor andersoni). A tick typically must remain attached for at least 6 to 10 hours before transmitting enough bacteria to establish infection.
RNA Virus
/ ar-en-ay VY-rus / · Ribonucleic Acid; Latin virus, poison
RNA Virus is a virus that carries its genetic information as ribonucleic acid rather than DNA and replicates using RNA-dependent polymerases or reverse transcriptase.
Because RNA-dependent RNA polymerases introduce errors at roughly one mutation per genome per replication cycle, RNA virus populations exist as swarms of closely related but genetically distinct variants called quasispecies, which accelerates adaptation to new hosts and antiviral drugs. RNA viruses are classified by genome polarity: positive-sense genomes can be translated directly by host ribosomes, negative-sense genomes must first be copied into a complementary strand, and double-stranded RNA genomes are found in viruses such as rotaviruses. Retroviruses such as HIV carry a reverse transcriptase enzyme that converts their RNA genome into DNA, which then integrates into the host chromosome as a provirus.
Among the most consequential human pathogens are RNA viruses: influenza viruses, SARS-CoV-2, measles virus, poliovirus, and rabies lyssavirus all belong to this category.
The hepatitis C virus, an RNA virus discovered by Michael Houghton and colleagues in 1989, mutates so rapidly that a single infected patient can harbor millions of distinct viral variants simultaneously, which long frustrated vaccine development and allowed the virus to evade immune responses for decades.
Are Enzymes Proteins? →All viruses store their genetic information as DNA. A large proportion of medically important viruses, including influenza, HIV, and coronaviruses, use RNA genomes and replicate without any DNA intermediate in their life cycle.
Building Blocks of Nucleic Acids →Influenza A virus carries its RNA genome as eight separate segments, each encoding one or two proteins. When two different influenza A strains infect the same cell simultaneously, their segments can reassort into new combinations, a process that generated the pandemic H1N1 strain responsible for the 2009 influenza pandemic.
