Infectious diseases – viral systemic diseases
Oncovirus
DNA virus HBV Hepatocellular carcinomaHPV Cervical cancerAnal cancerPenile cancerVulvar cancerVaginal cancerOropharyngeal cancerKSHV Kaposi's sarcomaEBV Nasopharyngeal carcinomaBurkitt's lymphomaHodgkin lymphomaFollicular dendritic cell sarcomaExtranodal NK/T-cell lymphoma, nasal typeMCPyV Merkel-cell carcinoma
RNA virus HCV Hepatocellular carcinomaSplenic marginal zone lymphomaHTLV-I Adult T-cell leukemia/lymphoma
Immune disorders
HIV AIDS
Central
nervous system
Encephalitis/
meningitis
DNA virus Human polyomavirus 2 Progressive multifocal leukoencephalopathy
RNA virus MeV Subacute sclerosing panencephalitisLCV Lymphocytic choriomeningitisArbovirus encephalitisOrthomyxoviridae (probable) Encephalitis lethargicaRV RabiesChandipura vesiculovirusHerpesviral meningitisRamsay Hunt syndrome type 2
Myelitis
Poliovirus PoliomyelitisPost-polio syndromeHTLV-I Tropical spastic paraparesis
Eye
Cytomegalovirus Cytomegalovirus retinitisHSV Herpes of the eye
Cardiovascular
CBV PericarditisMyocarditis
Respiratory system/
acute viral
nasopharyngitis/
viral pneumonia
DNA virus
Epstein–Barr virus EBV infection/Infectious mononucleosisCytomegalovirus
RNA virus
IV: Human coronavirus 229E/NL63/HKU1/OC43 Common coldMERS coronavirus Middle East respiratory syndromeSARS coronavirus Severe acute respiratory syndromeSARS coronavirus 2 COVID-19
V, Orthomyxoviridae: Influenza virus A/B/C/D Influenza/Avian influenza
V, Paramyxoviridae: Human parainfluenza viruses ParainfluenzaHuman orthopneumovirushMPV
Human
digestive system
Pharynx/Esophagus
MuV MumpsCytomegalovirus Cytomegalovirus esophagitis
Gastroenteritis/
diarrhea
DNA virus Adenovirus Adenovirus infection
RNA virus RotavirusNorovirusAstrovirusCoronavirus
Hepatitis
DNA virus HBV (B)
RNA virus CBVHAV (A)HCV (C)HDV (D)HEV (E)HGV (G)
Pancreatitis
CBV
Urogenital
BK virusMuV Mumps
Categories: EnterovirusesPolioInfraspecific virus taxa
https://en.wikipedia.org/wiki/Poliovirus
In chemistry, pyrophosphates are phosphorus oxyanions that contain two phosphorus atoms in a P-O-P linkage. A number of pyrophosphate salts exist, such as disodium pyrophosphate (Na2H2P2O7) and tetrasodium pyrophosphate (Na4P2O7), among others. Often pyrophosphates are called diphosphates. The parent pyrophosphates are derived from partial or complete neutralization of pyrophosphoric acid. The pyrophosphate bond is also sometimes referred to as a phosphoanhydride bond, a naming convention which emphasizes the loss of water that occurs when two phosphates form a new P-O-P bond, and which mirrors the nomenclature for anhydrides of carboxylic acids. Pyrophosphates are found in ATP and other nucleotide triphosphates, which are very important in biochemistry.
Pyrophosphates are prepared by heating phosphates, hence the name pyro-phosphate (from the Ancient Greek: πῦρ, πυρός, romanized: pyr, pyros, lit. 'fire'[1]). More precisely, they are generated by heating phosphoric acids to the extent that a condensation reaction occurs.
Pyrophosphates are generally white or colorless. The alkali metal salts are water-soluble.[2] They are good complexing agents for metal ions (such as calcium and many transition metals) and have many uses in industrial chemistry. Pyrophosphate is the first member of an entire series of polyphosphates.[3]
The term pyrophosphate is also the name of esters formed by the condensation of a phosphorylated biological compound with inorganic phosphate, as for dimethylallyl pyrophosphate. This bond is also referred to as a high-energy phosphate bond.
https://en.wikipedia.org/wiki/Pyrophosphate
Sulfate-reducing microorganisms can be traced back to 3.5 billion years ago and are considered to be among the oldest forms of microbes, having contributed to the sulfur cycle soon after life emerged on Earth.[3]
Many organisms reduce small amounts of sulfates in order to synthesize sulfur-containing cell components; this is known as assimilatory sulfate reduction. By contrast, the sulfate-reducing microorganisms considered here reduce sulfate in large amounts to obtain energy and expel the resulting sulfide as waste; this is known as dissimilatory sulfate reduction.[4] They use sulfate as the terminal electron acceptor of their electron transport chain.[5] Most of them are anaerobes; however, there are examples of sulfate-reducing microorganisms that are tolerant of oxygen, and some of them can even perform aerobic respiration.[6] No growth is observed when oxygen is used as the electron acceptor.[7] In addition, there are sulfate-reducing microorganisms that can also reduce other electron acceptors, such as fumarate, nitrate (NO3−), nitrite (NO2−), ferric iron [Fe(III)], and dimethyl sulfoxide (DMSO).[1][8]
In terms of electron donor, this group contains both organotrophs and lithotrophs. The organotrophs oxidize organic compounds, such as carbohydrates, organic acids (e.g., formate, lactate, acetate, propionate, and butyrate), alcohols (methanol and ethanol), aliphatic hydrocarbons (including methane), and aromatic hydrocarbons (benzene, toluene, ethylbenzene, and xylene).[9] The lithotrophs oxidize molecular hydrogen (H2), for which they compete with methanogens and acetogens in anaerobic conditions.[9] Some sulfate-reducing microorganisms can directly utilize metallic iron [Fe(0)] (zerovalent iron, or ZVI) as electron donor, oxidizing it to ferrous iron [Fe(II)].[10]
https://en.wikipedia.org/wiki/Sulfate-reducing_microorganism
Cydia pomonella granulovirus (CpGV) is a granulovirus belonging to the family Baculoviridae.[1] It has a double-stranded DNA genome that is 123,500 base pairs in length with 143 ORFs.[2] The virus forms small bodies called granules containing a single virion. CpGV is a virus of invertebrates – specifically Cydia pomonella, commonly known as the Codling moth.[3] CpGV is highly pathogenic, it is known as a fast GV – that is, one that will kill its host in the same instar as infection; thus, it is frequently used as a biological pesticide.
https://en.wikipedia.org/wiki/Cydia_pomonella_granulovirus
https://nikiyaantonbettey.blogspot.com/2021/08/08-23-2021-0842-cydia-pomonella.html
Monday, August 23, 2021
08-23-2021-1144 - heparan sulfate proteoglycan glycan glycoprotein peptidoglycan g-protein protein wnt respiratory syncytial virus (method of entry presentation, virus like particle, prions, defective interfering particle, etc.) SARS CoV 2 SARS-CoV-2 ACE2 (developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB (Granzyme B),[6] and tumour metastasis.)
Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues.[1] It occurs as a proteoglycan (HSPG, i.e. Heparan Sulfate ProteoGlycan) in which two or three HS chains are attached in close proximity to cell surface or extracellular matrix proteins.[2][3] It is in this form that HS binds to a variety of protein ligands, including Wnt,[4][5] and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB (Granzyme B),[6] and tumour metastasis. HS has also been shown to serve as cellular receptor for a number of viruses, including the respiratory syncytial virus.[7] One study suggests that cellular heparan sulfate has a role in SARS-CoV-2 Infection, particularly when the virus attaches with ACE2.[8]
The major cell membrane HSPGs are the transmembrane syndecans and the glycosylphosphatidylinositol (GPI) anchored glypicans.[9][10] Other minor forms of membrane HSPG include betaglycan[11] and the V-3 isoform of CD44 present on keratinocytes and activated monocytes.[12]
In the extracellular matrix, especially basement membranes, the multi-domain perlecan, agrin and collagen XVIII core proteins are the main HS-bearing species.
Heparan sulfate is a member of the glycosaminoglycan family of carbohydrates and is very closely related in structure to heparin. Heparin, commonly known as an anticoagulant, is a highly sulfated form of HS which, in contrast to HS, is mainly found in mast cell secretory granules.[13] Both consist of a variably sulfated repeating disaccharide unit. The main disaccharide units that occur in heparan sulfate and heparin are shown below.
The most common disaccharide unit within heparan sulfate is composed of a glucuronic acid (GlcA) linked to N-acetylglucosamine (GlcNAc), typically making up around 50% of the total disaccharide units. Compare this to heparin, where IdoA(2S)-GlcNS(6S) makes up 85% of heparins from beef lung and about 75% of those from porcine intestinal mucosa. Problems arise when defining hybrid GAGs that contain both 'heparin-like' and 'HS-like' structures. It has been suggested that a GAG should qualify as heparin only if its content of N-sulfate groups largely exceeds that of N-acetyl groups and the concentration of O-sulfate groups exceeds those of N-sulfate.[14]
Not shown below are the rare disaccharides containing a 3-O-sulfated glucosamine (GlcNS(3S,6S) or a free amine group (GlcNH3+). Under physiological conditions the ester and amide sulfate groups are deprotonated and attract positively charged counterions to form a salt. It is in this form that HS is thought to exist at the cell surface.
Abbreviations[edit]
- GlcA = β-D-glucuronic acid
- IdoA = α-L-iduronic acid
- IdoA(2S) = 2-O-sulfo-α-L-iduronic acid
- GlcNAc = 2-deoxy-2-acetamido-α-D-glucopyranosyl
- GlcNS = 2-deoxy-2-sulfamido-α-D-glucopyranosyl
- GlcNS(6S) = 2-deoxy-2-sulfamido-α-D-glucopyranosyl-6-O-sulfate
The cell surface receptor binding region of Interferon-γ overlaps with the HS binding region, near the protein's C-terminal. Binding of HS blocks the receptor binding site and as a result, protein-HS complexes are inactive.[41]
WNTGlypican-3 (GPC3) interacts with both Wnt and Frizzled to form a complex and triggers downstream signaling.[4][10] It has been experimentally established that Wnt recognizes a heparan sulfate modif on GPC3, which contains IdoA2S and GlcNS6S, and that the 3-O-sulfation in GlcNS6S3S enhances the binding of Wnt to the glypican.[5]
The HS-binding properties of a number of other proteins are also being studied:
Heparan sulfate analogues are thought to display identical properties as heparan sulfate with exception of being stable in a proteolytic environment like a wound.[42][43] Because heparan sulfate is broken down in chronic wounds by heparanase, the analogues only bind sites where natural heparan sulfate is absent and cannot be broken down by any known heparanases and glycanases.[citation needed] Also the function of the heparan sulfate analogues is the same as heparan sulfate, protecting a variety of protein ligands such as growth factors and cytokines. By holding them in place, the tissue can then use the different protein ligands for proliferation.
https://en.wikipedia.org/wiki/Heparan_sulfate
| Unsulfated, extracellular | |
|---|---|
| Sulfated, extracellular | |
| Sulfated, intracellular | |
| Synthetic | |
respiratory syncytial virus.[7]
Heparan sulfate proteoglycans (HSPGs) are glycoproteins, with the common characteristic of containing one or more covalently attached heparan sulfate (HS) chains, a type of glycosaminoglycan (GAG) (Esko et al. 2009). Cells elaborate a relatively small set of HSPGs (∼17) that fall into three groups according to their location: membrane HSPGs, such as syndecans and glycosylphosphatidylinositol-anchored proteoglycans (glypicans), the secreted extracellular matrix HSPGs (agrin, perlecan, type XVIII collagen), and the secretory vesicle proteoglycan, serglycin (Table 1). Much of the early work in the field concentrated on composition (size, chain number, and structure of the HS chains), biosynthesis, and binding properties of the chains. In 1985, the first somatic cell mutants altered in HSPG expression were identified (Esko et al. 1985), which allowed functional studies in the context of a cell culture model (Zhang et al. 2006). A decade later, the first HSPG mutants in a model organism (Drosophila melanogaster) were identified (Rogalski et al. 1993; Nakato et al. 1995; Häcker et al. 1997; Bellaiche et al. 1998; Lin et al. 1999), which was followed by identification of mutants in nematodes, tree frogs, zebrafish, and mice (Tables 2 and and3).3). HS is evolutionarily ancient and its composition has remained relatively constant from Hydra to humans (Yamada et al. 2007; Lawrence et al. 2008).
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