Streptolysin S
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Streptolysin S
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 ''S ...
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Hemolytic
Hemolysis or haemolysis (), also known by several other names, is the rupturing (lysis) of red blood cells (erythrocytes) and the release of their contents (cytoplasm) into surrounding fluid (e.g. blood plasma). Hemolysis may occur in vivo or in vitro. One cause of hemolysis is the action of hemolysins, toxins that are produced by certain pathogenic bacteria or fungi. Another cause is intense physical exercise. Hemolysins damage the red blood cell's cytoplasmic membrane, causing lysis and eventually cell death. Etymology From hemo- + -lysis, from , "blood") + , "loosening"). Inside the body Hemolysis inside the body can be caused by a large number of medical conditions, including some parasites (''e.g.'', ''Plasmodium''), some autoimmune disorders (''e.g.'', autoimmune haemolytic anaemia, drug-induced hemolytic anemia, atypical hemolytic uremic syndrome (aHUS)), some genetic disorders (''e.g.'', Sickle-cell disease or G6PD deficiency), or blood with too low a solute conce ...
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Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling l ...
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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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NAD+ Glycohydrolase
In enzymology, a NAD+ glycohydrolase () is an enzyme that catalyzes the chemical reaction :NAD+ + H2O \rightleftharpoons ADP-ribose + nicotinamide Thus, the two substrates of this enzyme are NAD+ and H2O, whereas its two products are ADP-ribose and nicotinamide. Unlike ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6), which catalyzes the same reaction, this reaction does not proceed through a cyclic ADP-ribose. This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is NAD+ glycohydrolase. Other names in common use include NAD+ nucleosidase, NADase, DPNase, DPN hydrolase, NAD hydrolase, diphosphopyridine nucleosidase, nicotinamide adenine dinucleotide nucleosidase, NAD glycohydrolase, NAD nucleosidase, and nicotinamide adenine dinucleotide glycohydrolase. This enzyme participates in nicotinate and nicotinamide metabolism and calcium signaling pathway Ca ...
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Keratinocyte
Keratinocytes are the primary type of cell found in the epidermis, the outermost layer of the skin. In humans, they constitute 90% of epidermal skin cells. Basal cells in the basal layer (''stratum basale'') of the skin are sometimes referred to as basal keratinocytes. Keratinocytes form a barrier against environmental damage by heat, UV radiation, water loss, pathogenic bacteria, fungi, parasites, and viruses. A number of structural proteins, enzymes, lipids, and antimicrobial peptides contribute to maintain the important barrier function of the skin. Keratinocytes differentiate from epidermal stem cells in the lower part of the epidermis and migrate towards the surface, finally becoming corneocytes and eventually be shed off, which happens every 40 to 56 days in humans. Function The primary function of keratinocytes is the formation of a barrier against environmental damage by heat, UV radiation, water loss, pathogenic bacteria, fungi, parasites, and viruses. Pathogens ...
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Group A Streptococcal Infection
Group A streptococcal infections are a number of infections with ''Streptococcus pyogenes'' a group A streptococcus (GAS). ''S. pyogenes'' is a species of beta-hemolytic gram-positive bacteria that is responsible for a wide range of infections that are mostly common and fairly mild. If the bacteria enter the bloodstream an infection can become severe and life-threatening, and is called an invasive GAS (iGAS). Infection of GAS may spread through direct contact with mucus or sores on the skin. GAS infections can cause over 500,000 deaths per year. Despite the emergence of antibiotics as a treatment for group A streptococcus, cases of iGAS are an increasing problem, particularly on the continent of Africa. There are many other species of ''Streptococcus'', including Group B streptococcus ''Streptococcus agalactiae'', and ''Streptococcus pneumoniae'', which cause other types of infections. Several virulence factors contribute to the pathogenesis of GAS, such as M protein, hemol ...
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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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Clostridioides Difficile (bacteria)
''Clostridioides difficile'' (synonym (taxonomy), syn. ''Clostridium difficile'') is a bacterium that is well known for causing serious diarrheal infections, and may also cause colon cancer. Also known as ''C. difficile'', or ''C. diff'' (), is Gram-positive species of Bacterial spore, spore-forming bacteria. ''Clostridioides'' spp. are Anaerobic organism, anaerobic, Motility, motile bacteria, ubiquitous in nature and especially prevalent in soil. Its vegetative cells are rod-shaped, Pleomorphism (microbiology), pleomorphic, and occur in pairs or short chains. Under the microscope, they appear as long, irregular (often drumstick- or spindle-shaped) cells with a bulge at their terminal ends (forms subterminal spores). Under Gram staining, ''C. difficile'' cells are Gram-positive and show optimum growth on blood agar at human body temperatures in the absence of oxygen. ''C. difficile'' is catalase- and superoxide dismutase-negative, and produces up to three types of toxins: Clostr ...
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Human Serum Albumin
Human serum albumin is the serum albumin found in human blood. It is the most abundant protein in human blood plasma; it constitutes about half of serum protein. It is produced in the liver. It is soluble in water, and it is monomeric. Albumin transports hormones, fatty acids, and other compounds, buffers pH, and maintains oncotic pressure, among other functions. Albumin is synthesized in the liver as preproalbumin, which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi apparatus to produce the secreted albumin. The reference range for albumin concentrations in serum is approximately 35–50 g/L (3.5–5.0 g/dL). It has a serum half-life of approximately 21 days. It has a molecular mass of 66.5 kDa. The gene for albumin is located on chromosome 4 in locus 4q13.3 and mutations in this gene can result in anomalous proteins. The human alb ...
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