Search for dissertations about: "Streptococcus pyogenes"
Showing result 11 - 15 of 94 swedish dissertations containing the words Streptococcus pyogenes.
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11. Interactions between Streptococcus pyogenes and the Human Immune System
Abstract : Streptococcus pyogenes is a common human pathogen causing mild infections such as tonsillitis and pharyngitis, but is also the cause of life-threatening conditions. To be able to infect the human host, S. pyogenes express different virulence factors. The surface-expressed M protein is a major virulence factor of S. READ MORE
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12. On the induction of inflammatory reactions by Streptococcus pyogenes
Abstract : Streptococcus pyogenes is an important human pathogen that causes significant morbidity and mortality worldwide. In order to successfully infect the human host, S. pyogenes is equipped with tools that modulate the human immune defence. READ MORE
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13. Streptococcus pyogenes secreted enzymes interacting with the human host
Abstract : Streptococcus pyogenes is one of the most common bacteria infecting humans. One of the factors contributing to the disease-causing properties is the secreted streptococcal cysteine proteinase, SpeB, which degrades several host proteins in connective tissue and circulation. READ MORE
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14. Interactions between Streptococcus pyogenes and the human immune defence
Abstract : Streptococcus pyogenes is an important human pathogen frequently colonizing the throat and skin of humans. To facilitate colonization and spread and to avoid the host immune defence, streptococci are endowed with a variety of virulence factors, two of which are investigated in this thesis namely streptolysin O (SLO) and M protein. READ MORE
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15. Streptococcus pyogenes and its interactions with the human host
Abstract : We have found that a set of group A streptococcal strains, primarily associated with skin infections, express surface-associated M proteins that bind plasminogen and plasmin with high affinity. The binding is mediated by a common 13 amino acid internal repeated sequence located in the NH2-terminal surface-exposed portion of these M proteins. READ MORE