The Coronavirus is covered in a sugary exterior which makes it hard for the body to fight against it. The sugar coat is known as the glycocalyx. The human body thinks it’s sort of similar to what should be in the body and then doesn’t attack it.
Keep reading below for possible solutions!
“It’s really those spike proteins that are really the main infection machinery of the virus," said UC San Diego computational chemist Rommie Amaro. "And these are the bits of the virus that get really heavily coated with this sugary coating so that our immune system can’t detect it in the body.”
Many cells in our body also have sugar coatings. Viruses like coronavirus have adapted to be covered in sugar to blend in, Amaro said. The body has a hard time detecting the virus, covered in this shield, so it can survive and be more infectious.
“The human body thinks it’s sort of similar to what should be in the body and then doesn’t attack it,” she said.
The existence of this coating on the coronavirus is well known in research, Amaro said. A May 2020 paper published in Science identified nearly two dozen sites where these sugars latch on to the infectious spikes on the virus.
The glycocalyx is a type of identifier that the body uses to distinguish between its own healthy cells (autoimmunity) and transplanted tissues, diseased cells, or invading organisms (viruses, bacteria, etc.).
Its protective functions are universal throughout the vascular system. In microvascular tissue, the glycocalyx serves as a vascular permeability barrier by inhibiting coagulation and leukocyte adhesion. Leukocytes must not stick to the vascular wall because they are important components of the immune system that must be able to travel to a specific region of the body when needed.
When leukocytes stick they increase inflammatory cytokines exponentially.
The shedding of the glycocalyx can be triggered by inflammatory stimuli, such as tumor necrosis factor-alpha.
Shedding of the glycocalyx leads to a drastic increase in vascular permeability. Vascular walls being permeable is disadvantageous, since that would enable passage of some macromolecules or other harmful antigens, which may trigger autoimmune and/or immunodeficiency.
The glycocalyx offers:
Protection: Cushions the plasma membrane and protects it from chemical injury
Immunity to infection: Enables the immune system to recognize and selectively attack foreign organisms.
Defense against cancer: Changes in the glycocalyx of cancerous cells enable the immune system to recognize and destroy them.
Transplant compatibility: Forms the basis for compatibility of blood transfusions, tissue grafts, and organ transplants.
Cell adhesion: Binds cells together so that tissues do not fall apart.
Inflammation regulation: Glycocalyx coating on endothelial walls in blood vessels prevents leukocytes from rolling/binding in healthy states.
Fertilization: Enables sperm to recognize and bind to eggs.
Embryonic development: Guides embryonic cells to their destinations in the body.
The endothelial and epithelial glycocalyx has emerged as an important participant in both inflammation and immunomodulation. Constituents of the glycocalyx have been used as biomarkers of injury severity and have the potential to be a target(s) for therapeutic interventions aimed at immune modulation.
Ignore at your own peril!
Glycoimmunology encompasses bonded sugar molecules known as monosaccharides, polysaccharides, or oligosaccharides etc., which are basically carbohydrate-based structures also known as Glycans, all of which are intimately involved in Glycoimmunology.
In fact, the loss of any component of these bonded sugar molecules can result in dire consequences and incompatibility with life itself. Changes in the patterns of glycans may lead to significant alterations in immune pathway signaling, as these glycans are important sugars that serve as the first contact point of cell-cell, but also host-pathogen interactions.
Glycans are essential biomolecules for energy storage, system regulatory purposes, and play an essential role in various immune and inflammatory diseases. Their diversity exceeds that even of DNA, with up to 25,000 genes, RNA, with approximately 360,000 mRNA, as every known cell is covered in glycans (sugars) which is as essential to life as a genome. Also, their structures exceed by orders of magnitude the number of the proteins encoded by our genome, which can be up to 400,000 proteins. This makes Glycoimmunlogy quintessentially supreme is all things health.
Interactions include the discrimination of self and non-self, antibody recognition, pathogen binding, modulation of immunity, infectious disease, inflammation, the binding of the hemagglutinin proteins, recognition of sialic acids, glycosaminoglycan synthesis, metastasis, cell adhesion, cell-cell signaling, intracellular transport, elimination of xenobiotics, sphingolipid metabolism, and more! Glycan patterns initiate immune reactions and virtually all cell surface receptors are glycoproteins. Glycan structures respond to environmental stimuli ranging from pH, ionic strength, hormonal stimulation, to inflammation, which aid in distinguishing health from disease, or self vs. non-self.
The "Manna", or Mannose and other sugar molecules regulate the Innate immune response to ANY and ALL viruses!
For example, A Unique new antiviral treatment made using sugar
Nearly all bacteria and viruses are coated with a thick glycocalyx (sugar coat).
Fact: both DNA and RNA are essentially polysaccharides; a carbohydrate (e.g. starch, cellulose, or glycogen) whose molecules consist of a number of sugar molecules bonded together.
This is the concept when speaking about Glycoimmunology.
When the "right" sugars, or polysaccharides, you ingest meet head-on with the glycocalyx (sugar coat) of the stealth pathogen what takes place?
The pathogens can no longer evade the immune system.
Again...the pathogens can no longer evade the immune system.
They get "tagged" and "bagged" for amelioration.
Your body, when given the "right" sugars, will flag foreign invaders all day long for destruction.
Then, your own adaptive immune response will finish the job, the way nature has intended. Cracking the "Sugar Code" through "Glycoimmunology"
A high-density coding system is essential to allow cells to communicate efficiently and swiftly through complex surface interactions.
The cell surface is the platform for the presentation of biochemical signals that are required for intercellular communication.
Sugar molecules surpass amino acids and nucleotides by far in information-storing capacity and serve as ligands in biorecognition processes for the transfer of information.
The ability of enzymes to generate an enormous diversity of biochemical signals is matched by receptor proteins (lectins), which are equally elaborate.
This is of medical importance in infection, tumor spread, or inflammation.
This implies a broad (patho)physiologic significance. By looking at the signals, at the writers, and the erasers of this information as well as its readers and ensuing consequences, we can rewrite the "sugar code" ensuring biorecognition processes for the transfer of information.
Sugar molecules play a vital role in both microbial and mammalian cells, where they are involved in cellular communication, govern microbial virulence, and modulate host immunity and inflammatory responses. The complement cascade, as part of a host’s innate immune system, is a potent weapon against invading bacteria but has to be tightly regulated to prevent inappropriate attack and damage to host tissues.
Monosaccharides, Polysaccharides, Oligosaccharides are basically sugar molecules bonded together and are carbohydrate-based structures also known as Glycans which are intimately involved in Glycoimmunology.
The loss of any component of these processes can result in dire consequences or incompatibility with life!
In Glycoimmunology Mannose, N-acetylglucosamine (GlcNAc/NAG), and Fucose (Bladderwrack) are at the core and the principal sugars found in human glycoproteins that impact our biology in a positive manner.
Sialic acid assists stealth pathogens evade the innate immune response of the host.
Sialic acid can "hide" mannose antigens on the surface of host cells or bacteria from mannose-binding lectin.
This prevents the activation of the complement system.
Many viruses can use host-sialylated structures for binding to their target host cell. Sialic acids provide a good target for these viruses since they are highly conserved and are abundant in large numbers in virtually all cells.
Sialic acid analogs (inhibitors) can interfere with the release of newly generated viruses from infected cells by inhibiting the viral enzyme neuraminidase.
This is what natural Neuraminidase inhibitors like Skullcap and Licorice, and other compounds accomplish.
They block neuraminidase and subsequently impact sialic acid glycans thus assisting in the blockage initial attachment, and the release of viral particles from the infected cell so as to stop viral replication.
Glycans serve as the first contact point of cell-cell but also cell-pathogen interactions.
Glycan (sugar) modifications play an essential role in various immune and inflammatory diseases. Glycans are also essential biomolecules for energy storage and system regulatory purposes.
Glycan diversity exceeds that even of DNA and RNA and every known cell is covered in glycans which are as essential to life as a genome.
Glycan structures exceed by orders of magnitude the number of the proteins encoded by our genome.
Glycans comprise the outer face of cells and interactions include the discrimination of self and non-self, antibody recognition, pathogen binding, modulation of immunity, infectious disease, inflammation, immunological response, the binding of the hemagglutinin proteins (viruses), recognition of sialic acids by Siglec (sialic acid-binding Ig-like lectin) receptors, glycosaminoglycan-mediated chemokine presentation, metastasis, cell adhesion, cell-cell interactions, signaling, intracellular transport, glucuronidation (xenobiotics), sphingolipid metabolism, and more!
Glycan patterns initiate immune reactions and virtually all cell surface receptors are glycoproteins.
Glycan structures respond to environmental stimuli ranging from pH, ionic strength, hormonal stimulation, to inflammation, which aid in distinguishing health from disease, or self vs. non-self.
The mannose receptor is a C-type lectin primarily present on the surface of macrophages, immature dendritic cells and liver sinusoidal endothelial cells, but is also expressed on the surface of skin cells such as human dermal fibroblasts and keratinocytes.
A C-type lectin (CLEC) is a type of carbohydrate-binding protein domain known as a lectin.
Proteins that contain C-type lectin domains have a diverse range of functions including cell-cell adhesion, immune response to pathogens, and apoptosis.
The mannose receptor recognizes terminal mannose, N-acetylglucosamine (NAG), and fucose (Bladderwrack) residues on glycans attached to proteins found on the surface of some microorganisms, playing a role in both the innate and adaptive immune systems.
Additional functions include clearance of glycoproteins from the circulation, including sulfated glycoprotein hormones and glycoproteins released in response to pathological events.
The mannose receptor recycles continuously between the plasma membrane and endosomal compartments in a clathrin-dependent manner.
The mannose receptor recognizes the patterns of carbohydrates that decorate the surfaces and cell walls of infectious agents, which appear to play a key role in host defense and provides a link between innate and adaptive immunity.
Mannose-binding lectin (MBL) is a serum protein of hepatic (liver) origin belonging to a family of Ca2+-dependent collagenous lectins, most of which are components of the innate immune system.
Mannose-binding lectin (MBL), also called mannan-binding lectin or mannan-binding protein (MBP), is a lectin that is instrumental in innate immunity as an opsonin and via the lectin pathway.
Mannose-binding lectin (MBL) is a key innate immunity pattern-recognition protein, activates the lectin complement pathway.
MBL has strong biologic plausibility as an innate immunity candidate protein that could protect against influenza-related sepsis with and without bacterial co-infection.
MBL binds to microbial surface glycosylation residues and targets influenza virus via direct neutralization, by recognition of influenza hemagglutinin surface proteins on infected cells, and can also ameliorate severity by defending against bacterial pathogens.
Additionally, the influenza virus uses a glycan-binding entry mechanism to invade host cells, and lectins such as MBL may interfere directly with the entry of the pathogen into the cell.
Another important function of MBL is that this molecule binds senescent and apoptotic cells and enhances engulfment of whole, intact apoptotic cells, as well as cell debris by phagocytes.
The complement system can be activated through three pathways: the classical pathway, the alternative pathway, and the lectin pathway. One way that the most-recently discovered lectin pathway is activated is through mannose-binding lectin protein.
MBL binds to carbohydrates (to be specific, D-mannose, and L-fucose residues) found on the surfaces of many pathogens. For example, MBL has been shown to bind to:
yeasts such as Candida albicans
viruses such as HIV and influenza A
many bacteria, including Salmonella and Streptococci
parasites like Leishmania
MBL deficiency is a risk factor for the development of infection.
Human cohort studies have described associations between MBL deficiency and susceptibility to meningococcal meningitis, human immunodeficiency virus (HIV) infection, hepatitis C virus (HCV) infection, and severe bacterial and fungal infections producing sepsis.
MBL deficiency has also been associated with increased frequencies of bacterial, viral, and fungal infections in both children and adults, particularly following bone marrow transplantation.
Studies of human immune cells suggest that MBL deficiency may influence proinflammatory cytokine production in monocytes, peripheral blood mononuclear cells, and neutrophils as well as neutrophil superoxide production.
Dendritic cells (DCs) are antigen-presenting cells that are central to the induction of antigen-specific immune responses.
To induce antigen-specific immune responses, DCs are required to recognize and process foreign material and present antigenic peptides, costimulatory molecules, and cytokines to cells of the adaptive immune system: namely to T and B lymphocytes.
Recognition of foreign antigens and subsequent delivery of costimulatory and cytokine signals are regulated by interactions between pathogen and pathogen recognition receptors (PRRs) which are expressed by DCs, or present as soluble plasma pattern recognition proteins, including MBL.
MBL-D individuals display unique functional characteristics, including higher production of proinflammatory cytokines interleukin (IL)-6 and tumor necrosis factor (TNF)-α.
As a pro-inflammatory cytokine, IL-6 plays an important role in the immune response. IL-6 regulates the expression of acute-phase response proteins, affects DC maturation and survival, and has been reported to play a role in T-cell differentiation. In the clinical setting, high IL-6 levels are associated with poor prognosis and poor outcome in sepsis and systemic inflammatory response syndrome.
Increased IL-6 produced by MDCs in MBL-D individuals may have important clinical implications and suggests a mechanism by which MBL-D individuals may suffer from a reduced ability to respond to the pathogen.
Mannose-binding lectin deficiency is a condition that affects the immune system. People with this condition have low levels (deficiency) of an immune system protein called mannose-binding lectin in their blood.
A lack of functional MBL to bind pathogens and activate the complement cascade may have important consequences for the health of an individual.
Indeed, MBL deficiency has been associated with a number of important infectious, inflammatory, and autoimmune disease states in humans.
People with mannose-binding lectin deficiency can develop infections of the upper respiratory tract and other body systems.
Individuals with this condition may also contract more serious infections such as pneumonia and meningitis. Depending on the type of infection, the symptoms caused by the infections vary in frequency and severity.
Infants and young children with mannose-binding lectin deficiency seem to be more susceptible to infections than affected adults, but adults can also develop recurrent infections. In addition, affected individuals undergoing chemotherapy or taking drugs that suppress the immune system are especially prone to infections.
Mannose-binding lectin plays an important role in the body's immune response by attaching to foreign invaders such as bacteria, viruses, or yeast and turning on (activating) the complement system.
The complement system is a group of immune system proteins that work together to destroy foreign invaders (pathogens), trigger inflammation, and remove debris from cells and tissues. Mannose-binding lectin can also stimulate special immune cells to engulf and break down the attached pathogen.
With decreased levels of mannose-binding lectin, the body does not recognize and fight foreign invaders efficiently. Consequently, infections can be more common in people with this condition.
Deficiencies have been associated with susceptibility to autoimmune and infectious diseases.
MBL facilitates phagocytosis of cellular debris and may, therefore, prevent autoimmunity.
Researchers believe that a number of factors, including other genetic and environmental factors, are involved in the development of mannose-binding lectin deficiency and susceptibility to infection.
MBL belongs to the class of collectins in the C-type lectin superfamily, whose function appears to be pattern recognition in the first line of defense in the pre-immune host. MBL recognizes carbohydrate patterns, found on the surface of a large number of pathogenic micro-organisms, including bacteria, viruses, protozoa, and fungi. Binding of MBL to a micro-organism results in the activation of the lectin pathway of the complement system.
MBL in the blood is complexed with (bound to) another protein, a serine protease called MASP (MBL-associated serine protease). In order to activate the complement system when MBL binds to its target (for example, mannose on the surface of a bacterium), the MASP protein functions to cleave the blood protein C4 into C4a and C4b. The C4b fragments can then bind to the surface of the bacterium, and initiate the formation of a C3-convertase.
The subsequent complement cascade catalyzed by C3-convertase results in creating a membrane attack complex, which causes lysis of the pathogen as well as altered-self in the context of apoptotic and necrotic cells.
The complement pathway plays an essential role in the innate and adaptive immune response. MASP proteins, through the function of MBL, are activated when it complexes with the pathogen recognition molecules of the lectin pathway, the mannose-binding lectin, and the ficolins (FCN2). MASP proteins are also involved with coagulation factors such as thrombin, fibrinogen, factor XIII, and thromboxane.
MASP proteins function in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them.
In order to activate the complement system when MBL binds to its target (for example, mannose on the surface of a bacterium), the MASP protein functions to cleave the blood protein C4 into C4a and C4b. The C4b fragments can then bind to the surface of the bacterium, and initiate the formation of a C3-convertase.
A mannose-binding lectin deficiency leads to a complement deficiency!
Complement deficiency is an immunodeficiency of absent or suboptimal functioning of one of the complement system proteins. Because there are redundancies in the immune system, many complement disorders are never diagnosed, some studies estimated that less than 10% are identified.
MBL has been reported as influencing Toll-like receptor 2 (TLR2) and TLR6 responses.
The mannose-binding lectin (MBL) pathway of the complement cascade has an essential role in the eradication of Borrelia burgdorferi (Lyme Disease). Deficiency in the MBL pathway of the complement cascade is a risk factor for developing disseminated Ab+ LB.
Malfunctions of MBL affects up to 50% of individuals in some populations.
More than two-thirds of patients with mycoplasma infections had genotypic MBL deficiency (compared with one-third in the general population).
In summary, up to 50% of individuals in some populations are affected by mannose-binding lectin deficiency. This leads to a complement deficiency to which only 10% are identified.
In other words, up to 90% of affected individuals have a propensity towards a malfunctioning immune system through MBL-D and complement deficiency!!!
Is it any wonder society is so plagued with infectious disease and malfunctioning immune systems? Glycosaminoglycans (GAGs)
GAG on this...BREAKING Research...
Glycosaminoglycans (GAGs) Such As Heparin Could Emerge As New Antivirals For...you guessed it, Coronavirus.
Glycosaminoglycans (GAGs) are complex linear polysaccharides (sugars molecules related to Glycoimmunology).
Subversion of Glycosaminoglycans (GAGs) is a pathogenic strategy shared by a wide variety of microbial pathogens, including viruses, bacteria, parasites, and fungi.
Pathogens use GAGs at virtually every major portals of entry to promote their attachment and invasion of host cells, movement from one cell to another, and to protect themselves from immune attack.
Pathogens co-opt fundamental activities of GAGs to accomplish these tasks.
The outcome of microbial infection is largely governed by the ability of pathogens to subvert host components and their activities.
Among the host components, glycosaminoglycans (GAGs) are prime targets of pathogens.
Heparin is a member of the glycosaminoglycan (GAG) family.
Nattokinase has heparin-binding properties and heparin plays important roles in almost all of nattokinase's potential therapeutically applications.
Chondroitin Sulfate also plays an important role in Glycosaminoglycans (GAGs).
Chondroitin Sulfate exhibited potent antiviral activity and substantially exceeded the antiviral potency of heparin, the known inhibitor of virus binding to cells.
Bench-to-bedside review: The role of glycosaminoglycans in respiratory disease
When we combine Mannose, Bladderwrack, NAG, Skullcap, Licorice, Nattokinase, and Chondroitin Sulfate together there is a synergy that takes place, unlike anything this world has ever seen!
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