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Heat shock proteins (HSP) are stable cellular stress proteins. Their amino-acid composition practically does not change throughout their development.
People and mice have HSP homology (similarity) is 99.9%, people and bacteria – 60%, people and chlamydia – 50%, between different types of chlamydia more then 95%.
All heat shock proteins are grouped into classes according to their molecular weight – HSP10, HSP25, HSP27, HSP60, HSP70, HSP90 and HSP110.
All heat shock proteins are divided into two main groups: constitutively expressed heat shock protein (HSC) and heat shock proteins of induced expression (HSP).
HSCs are produced daily, under certain physiologic conditions. Cell contains them molecularly. HSC are responsible for well-ordered anabolism, metabolism, and catabolism.
HSPs (stress proteins) are quickly synthesized by cells as a response to various physical, chemical and physiological impacts in order to increase cell’s defense functions.
In human immunogenetics, microbial HSP are dominant antigens. When infection develops, microorganisms significantly increase HSP synthesis to be able to protect themselves from foreign immunologic defense mechanisms. Thereupon, HSP60 becomes one of the most important bacterial proteins. Immune defense, effective in initial infection, has usually been limited by microbial-specific epitopes of HSP60.
Symptomless and indiagnosed chlamydial infection leads to permanent or intermittent controversy between human immune system and chlamydeous HSP60 (cHSP60).
At the Evromedika Medical Centre, IgG determines antibodies to HSP 60 – сhlamydia trachomatis – to diagnose oncoming chlamydial infection. Seeing as homology between species of сhlamydia is more then 95%, antibodies to HSP60 of other species of сhlamydia is detected.