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Streptolysin
Streptolysins are two hemolytic exotoxins from ''Streptococcus''. Types include streptolysin O (SLO; ''slo''), which is oxygen-labile, and streptolysin S (SLS; ''sagA''), which is oxygen-stable. SLO is part of the thiol-activated cytolysin family. It is hemolytically active only in a reversibly reduced state. It is antigenic, so its antibody antistreptolysin O can be detected in an antistreptolysin O titre. SLS is stable in the presence of oxygen. It is not antigenic due to its small size. It is sometimes considered a bacteriocin due to similarities in the synthesis pathway. Streptolysin O Streptolysin O (SLO; ''slo),'' is a bacterial toxin that has four protein domains which is known to make the plasma membranes in animal cells permeable. It does this by creating pore complexes within the membrane by first binding a monomer to the cholesterol found in the target membrane and then forming an oligomeric transmembrane pore. This toxin excreted by a Gram-positive bacteria ''Str ...
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Streptococcal Proteins
''Streptococcus'' is a genus of gram-positive ' (plural ) or spherical bacteria that belongs to the family Streptococcaceae, within the order Lactobacillales (lactic acid bacteria), in the phylum Bacillota. Cell division in streptococci occurs along a single axis, so as they grow, they tend to form pairs or chains that may appear bent or twisted. This differs from staphylococci, which divide along multiple axes, thereby generating irregular, grape-like clusters of cells. Most streptococci are oxidase-negative and catalase-negative, and many are facultative anaerobes (capable of growth both aerobically and anaerobically). The term was coined in 1877 by Viennese surgeon Albert Theodor Billroth (1829–1894), by combining the prefix "strepto-" (from ), together with the suffix "-coccus" (from Modern , from .) In 1984, many bacteria formerly grouped in the genus ''Streptococcus'' were separated out into the genera '' Enterococcus'' and '' Lactococcus''. Currently, over 50 spe ...
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Streptococcus
''Streptococcus'' is a genus of gram-positive ' (plural ) or spherical bacteria that belongs to the family Streptococcaceae, within the order Lactobacillales (lactic acid bacteria), in the phylum Bacillota. Cell division in streptococci occurs along a single axis, so as they grow, they tend to form pairs or chains that may appear bent or twisted. This differs from staphylococci, which divide along multiple axes, thereby generating irregular, grape-like clusters of cells. Most streptococci are oxidase-negative and catalase-negative, and many are facultative anaerobes (capable of growth both aerobically and anaerobically). The term was coined in 1877 by Viennese surgeon Albert Theodor Billroth (1829–1894), by combining the prefix "strepto-" (from ), together with the suffix "-coccus" (from Modern , from .) In 1984, many bacteria formerly grouped in the genus ''Streptococcus'' were separated out into the genera ''Enterococcus'' and '' Lactococcus''. Currently, over 50 speci ...
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Streptococcus Pyogenes
''Streptococcus pyogenes'' is a species of Gram-positive, aerotolerant bacteria in the genus '' Streptococcus''. These bacteria are extracellular, and made up of non-motile and non-sporing cocci (round cells) that tend to link in chains. They are clinically important for humans, as they are an infrequent, but usually pathogenic, part of the skin microbiota that can cause Group A streptococcal infection. ''S. pyogenes'' is the predominant species harboring the Lancefield group A antigen, and is often called group A ''Streptococcus'' (GAS). However, both ''Streptococcus dysgalactiae'' and the ''Streptococcus anginosus'' group can possess group A antigen as well. Group A streptococci, when grown on blood agar, typically produce small (2–3 mm) zones of beta-hemolysis, a complete destruction of red blood cells. The name group A (beta-hemolytic) ''Streptococcus'' (GABHS) is thus also used. The species name is derived from Greek words meaning 'a chain' () of berries ( at ...
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Thiol-activated Cytolysin
The thiol-activated Cholesterol-dependent Cytolysin (CDC) familyTC# 1.C.12 is a member of the MACPF superfamily. Cholesterol dependent cytolysins are a family of β-barrel pore-forming exotoxins that are secreted by gram-positive bacteria. CDCs are secreted as water-soluble monomers of 50-70 kDa, that when bound to the target cell, form a circular homo-oligomeric complex containing as many as 40 (or more) monomers. Through multiple conformational changes, the β-barrel transmembrane structure (~250 Å in diameter depending on the toxin) is formed and inserted into the target cell membrane. The presence of cholesterol in the target membrane is required for pore formation, though the presence of cholesterol is not required by all CDCs for binding. For example, intermedilysin (ILYTC# 1.C.12.1.5 secreted by '' Streptococcus intermedius'' will bind only to target membranes containing a specific protein receptor, independent of the presence of cholesterol, but cholesterol is required b ...
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Cholesterol-dependent Cytolysin
The thiol-activated Cholesterol-dependent Cytolysin (CDC) familyTC# 1.C.12 is a member of the MACPF superfamily. Cholesterol dependent cytolysins are a family of β-barrel pore-forming exotoxins that are secreted by gram-positive bacteria. CDCs are secreted as water-soluble monomers of 50-70 kDa, that when bound to the target cell, form a circular homo-oligomeric complex containing as many as 40 (or more) monomers. Through multiple conformational changes, the β-barrel transmembrane structure (~250 Å in diameter depending on the toxin) is formed and inserted into the target cell membrane. The presence of cholesterol in the target membrane is required for pore formation, though the presence of cholesterol is not required by all CDCs for binding. For example, intermedilysin (ILYTC# 1.C.12.1.5 secreted by '' Streptococcus intermedius'' will bind only to target membranes containing a specific protein receptor, independent of the presence of cholesterol, but cholesterol is required b ...
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Thiol-activated Cytolysin
The thiol-activated Cholesterol-dependent Cytolysin (CDC) familyTC# 1.C.12 is a member of the MACPF superfamily. Cholesterol dependent cytolysins are a family of β-barrel pore-forming exotoxins that are secreted by gram-positive bacteria. CDCs are secreted as water-soluble monomers of 50-70 kDa, that when bound to the target cell, form a circular homo-oligomeric complex containing as many as 40 (or more) monomers. Through multiple conformational changes, the β-barrel transmembrane structure (~250 Å in diameter depending on the toxin) is formed and inserted into the target cell membrane. The presence of cholesterol in the target membrane is required for pore formation, though the presence of cholesterol is not required by all CDCs for binding. For example, intermedilysin (ILYTC# 1.C.12.1.5 secreted by '' Streptococcus intermedius'' will bind only to target membranes containing a specific protein receptor, independent of the presence of cholesterol, but cholesterol is required b ...
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Antistreptolysin O Titre
Anti-streptolysin O (ASO or ASLO) is the antibody made against streptolysin O, an immunogenic, oxygen-labile streptococcal hemolytic exotoxin produced by most strains of group A and many strains of groups C and G ''Streptococcus'' bacteria. The "O" in the name stands for ''oxygen-labile''; the other related toxin being oxygen-stable streptolysin-S. The main function of streptolysin O is to cause hemolysis (the breaking open of red blood cells)—in particular, beta-hemolysis. Increased levels of ASO titre in the blood could cause damage to the heart and joints. In most cases, penicillin is used to treat patients with increased levels of ASO titre. Clinical significance When the body is infected with streptococci, it produces antibodies against the various antigens that the streptococci produce. ASO is one such antibody. A raised or rising levels can indicate past or present infection. Historically it was one of the first bacterial markers used for diagnosis and follow up of rh ...
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Anti-streptolysin O
Anti-streptolysin O (ASO or ASLO) is the antibody made against streptolysin O, an immunogenic, oxygen-labile streptococcal hemolytic exotoxin produced by most strains of group A and many strains of groups C and G ''Streptococcus'' bacteria. The "O" in the name stands for ''oxygen-labile''; the other related toxin being oxygen-stable streptolysin-S. The main function of streptolysin O is to cause hemolysis (the breaking open of red blood cells)—in particular, beta-hemolysis. Increased levels of ASO titre in the blood could cause damage to the heart and joints. In most cases, penicillin is used to treat patients with increased levels of ASO titre. Clinical significance When the body is infected with streptococci, it produces antibodies against the various antigens that the streptococci produce. ASO is one such antibody. A raised or rising levels can indicate past or present infection. Historically it was one of the first bacterial markers used for diagnosis and follow up of ...
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Hematology
Hematology ( always spelled haematology in British English) is the branch of medicine concerned with the study of the cause, prognosis, treatment, and prevention of diseases related to blood. It involves treating diseases that affect the production of blood and its components, such as blood cells, hemoglobin, blood proteins, bone marrow, platelets, blood vessels, spleen, and the mechanism of coagulation. Such diseases might include hemophilia, blood clots ( thrombus), other bleeding disorders, and blood cancers such as leukemia, multiple myeloma, and lymphoma. The laboratory analysis of blood is frequently performed by a medical technologist or medical laboratory scientist. Specialization Physicians specialized in hematology are known as hematologists or haematologists. Their routine work mainly includes the care and treatment of patients with hematological diseases, although some may also work at the hematology laboratory viewing blood films and bone marrow slides unde ...
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Bacterial Toxins
Microbial toxins are toxins produced by micro-organisms, including bacteria, fungi, protozoa, dinoflagellates, and viruses. Many microbial toxins promote infection and disease by directly damaging host tissues and by disabling the immune system. Endotoxins most commonly refer to the lipopolysaccharide (LPS) or lipooligosaccharide (LOS) that are in the outer plasma membrane of Gram-negative bacteria. The botulinum toxin, which is primarily produced by ''Clostridium botulinum'' and less frequently by other ''Clostridium'' species, is the most toxic substance known in the world. However, microbial toxins also have important uses in medical science and research. Currently, new methods of detecting bacterial toxins are being developed to better isolate and understand these toxin. Potential applications of toxin research include combating microbial virulence, the development of novel anticancer drugs and other medicines, and the use of toxins as tools in neurobiology and cellular biology ...
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Post-translational Modification
Post-translational modification (PTM) is the covalent and generally enzymatic modification of proteins following protein biosynthesis. This process occurs in the endoplasmic reticulum and the golgi apparatus. Proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo PTM to form the mature protein product. PTMs are important components in cell signaling, as for example when prohormones are converted to hormones. Post-translational modifications can occur on the amino acid side chains or at the protein's C- or N- termini. They can extend the chemical repertoire of the 20 standard amino acids by modifying an existing functional group or introducing a new one such as phosphate. Phosphorylation is a highly effective mechanism for regulating the activity of enzymes and is the most common post-translational modification. Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called gly ...
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Virulence
Virulence is a pathogen's or microorganism's ability to cause damage to a host. In most, especially in animal systems, virulence refers to the degree of damage caused by a microbe to its host. The pathogenicity of an organism—its ability to cause disease—is determined by its virulence factors. In the specific context of gene for gene systems, often in plants, virulence refers to a pathogen's ability to infect a resistant host. The noun ''virulence'' derives from the adjective ''virulent'', meaning disease severity. The word ''virulent'' derives from the Latin word ''virulentus'', meaning "a poisoned wound" or "full of poison." From an ecological standpoint, virulence is the loss of fitness induced by a parasite upon its host. Virulence can be understood in terms of proximate causes—those specific traits of the pathogen that help make the host ill—and ultimate causes—the evolutionary pressures that lead to virulent traits occurring in a pathogen strain. Virulen ...
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