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Protein A facilitates the adherence of S. aureus to human von Willebrand factor (vWF)-coated surfaces, thus increasing the bacteria's infectiousness at the site of skin penetration. Protein A can inflame lung tissue by binding to tumor necrosis factor 1 (TNFR-1) receptors. This interaction has been shown to play a key role in the pathogenesis ...
Many pathogenesis-related protein families also coincide with groups of human allergens, even though the allergy may have nothing to do with the defense function of the proteins. [5] Grouping these proteins by their sequence features allows for finding potential allergenic proteins from sequenced plant genomes, a field of study dubbed ...
Surfactant protein A (SP-A) is a protein of 248 amino acids usually found in large oligomeric structures. The mature SP-A1 monomer is a 35kDa protein that differs from SP-A2 in four amino acids at the coding region.
A new study, which appears in Nature Medicine, has identified a biomarker that may eventually allow doctors to spot the early signs of protein buildup before it causes significant damage.
Pathogenic strains often promote infections by producing virulence factors such as potent protein toxins, and the expression of a cell-surface protein that binds and inactivates antibodies. S. aureus is one of the leading pathogens for deaths associated with antimicrobial resistance and the emergence of antibiotic-resistant strains, such as ...
A potent three-protein virulence factor produced by Bacillus anthracis, called anthrax toxin, plays a key role in anthrax pathogenesis. Exotoxins are extremely immunogenic and trigger the humoral response (antibodies target the toxin). Exotoxins are also produced by some fungi as a competitive resource.
A pathogen may contain a protein that acts as a mitogen to encourage cell division, thus causing more B or T cell clones to be produced. Similarly, a pathogenic protein may act as a superantigen which causes rapid polyclonal activation of B or T cells.
Once a pathogen genome has been sequenced, effectors can be predicted based on protein sequence similarity, but such predictions are not always precise. More importantly, it is difficult to prove experimentally that a predicted effector is actually secreted into a host cell because the amount of each effector protein is tiny.