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1. Binding to viral nucleic acids with specific RNA 5' caps or 5' end structure. This is based on 5′-triphosphorylated RNA and Cap-0 RNA binding. Cap-0 is a messenger RNA cap that has N7-methyl guanosine but lacks the 2' O-methylation found in Cap-1, which is important in evading the innate immune response as detection as non-self RNA.
Antigen and antibody interact through a high affinity binding much like lock and key. [10] A dynamic equilibrium exists for the binding. For example, the reaction is a reversible one, and can be expressed as: [11] [] + [] []
Scheme of the complement system. The complement system, also known as complement cascade, is a part of the humoral, innate immune system and enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism, promote inflammation, and attack the pathogen's cell membrane. [1]
C5a is a protein fragment released from cleavage of complement component C5 by protease C5-convertase into C5a and C5b fragments. C5b is important in late events of the complement cascade, an orderly series of reactions which coordinates several basic defense mechanisms, including formation of the membrane attack complex (MAC), one of the most basic weapons of the innate immune system, formed ...
Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD (TANK-binding kinase 1-binding protein 1) can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD .
Lambda phage is a non-contractile tailed phage, meaning during an infection event it cannot 'force' its DNA through a bacterial cell membrane. It must instead use an existing pathway to invade the host cell, having evolved the tip of its tail to interact with a specific pore to allow entry of its DNA to the hosts.
In molecular biology, the guanylate-binding proteins family is a family of GTPases that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma ( Interferon-inducible GTPase ) are key to the protective immunity against microbial and viral pathogens .
In the α4 subunit, Tyr187 was identified as a critical amino acid in integrin α4β7-mediated cell adhesion. Its mutation affects interactions between integrin α4β7 and its ligands. The binding site on the α4 subunit is located on the upper surface of a N-terminal β-propeller structure where this α4 Tyr187 residue is situated. [3]