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A leukocidin is a type of cytotoxin created by some types of bacteria (Staphylococcus).It is a type of pore-forming toxin.The model for pore formation is step-wise. First, the cytotoxin's "S" subunit recognizes specific protein-containing receptors, or an integrin on the host cell's surface.
Pore-forming proteins (PFTs, also known as pore-forming toxins) are usually produced by bacteria, and include a number of protein exotoxins but may also be produced by other organisms such as apple snails that produce perivitellin-2 [1] [2] or earthworms, who produce lysenin.
In gram-positive bacteria, a protein or polysaccharide surface layer serves as the specific adhesin. To effectively achieve adherence to host surfaces, many bacteria produce multiple adherence factors called adhesins. Bacterial adhesins provide species and tissue tropism. Adhesins are expressed by both pathogenic bacteria and saprophytic bacteria.
Bacteria produce various adhesins including lipoteichoic acid, trimeric autotransporter adhesins and a wide variety of other surface proteins to attach to host tissue. Capsules, made of carbohydrate, form part of the outer structure of many bacterial cells including Neisseria meningitidis .
An S-layer (surface layer) is a cell surface protein layer found in many different bacteria and in some archaea, where it serves as the cell wall. All S-layers are made up of a two-dimensional array of proteins and have a crystalline appearance, the symmetry of which differs between species.
M protein is a virulence factor that can be produced by certain species of Streptococcus. [1] Viruses, parasites and bacteria are covered in protein and sugar molecules that help them gain entry into a host by counteracting the host's defenses. One such molecule is the M protein produced by certain streptococcal bacteria.
Protein A is a 42 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind immunoglobulins ...
This protein binds to integrins and facilitates uptake when attached to bacteria or beads. The shortest invasin fragment capable of integrin binding consists of the COOH-terminal 192 amino acids. Notably, this fragment lacks homology with the integrin-binding domains of fibronectin, specifically the fibronectin type III repeats 9 and 10 (Fn-III ...