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Receptor protein interacting with mycoplasma genitalium mgpa, isolation method and use thereof

A technology of mycoplasma genitalium and receptor protein, which is applied to the preparation method of peptides, peptide/protein components, biomaterial analysis, etc., and can solve problems such as invasion and adhesion

Active Publication Date: 2020-11-24
NANHUA UNIV
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  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

However, so far, there is no relevant report about the interaction between Mg and the receptor molecules on the host cell membrane through MgPa, which leads to its adhesion or invasion into the host epithelial cells

Method used

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  • Receptor protein interacting with mycoplasma genitalium mgpa, isolation method and use thereof
  • Receptor protein interacting with mycoplasma genitalium mgpa, isolation method and use thereof
  • Receptor protein interacting with mycoplasma genitalium mgpa, isolation method and use thereof

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Embodiment Construction

[0033] At present, mass spectrometry technology has played an important role in protein and proteomics research. It can separate different proteins by using the difference of the charge-to-mass ratio (M / Z) of protein molecules, so as to analyze and identify unknown proteins. The mass spectrometry analysis of about 14kDa protein in the patent of the present invention shows that the 14kDa receptor protein has a strong correlation with histone H2B.

[0034] Obtaining receptor protein and receptor protein antibody is helpful to study the characteristics and functions of receptor protein. In the present invention, H2B protein and H2B antibody are further used to study the interaction between rMgPa and receptor protein by ELISA and Far-western blotting methods. The results showed that rMgPa can interact with H2B and bind specifically; the specific protein in the target band of about 14kDa can also bind to rMgPa, indicating that the protein of about 14KDa contains histone H2B. The i...

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Abstract

The invention relates to a screened human urothelial cell membrane surface receptor protein of histone H2B. The histone H2B is separated from cell membrane protein of human urothelial cells, the nucleotide sequence of the histone H2B is shown as SEQ ID NO.1 and composed of 126 amino acids. An improved VOPBA (virus overlay protein blot assay) is implemented to screen out the receptor on the membrane of the human urothelial cells and accordingly provides a preliminary experiment basis for further illuminating possible adhesion and pathogenic mechanisms of Mg, further designing receptor-mimic molecules and antagonistic molecules to prevent Mg from adhering to or infecting host cells and preventing Mg infection. Therefore, the histone H2B can be applied to targeted drugs for treating or preventing mycoplasma genitalium infectious diseases.

Description

technical field [0001] The invention relates to a receptor protein interacting with mycoplasma genitalium MgPa—histone H2B (HistoneH2B), and also provides a separation method and application of the protein, belonging to the technical fields of bioengineering and disease diagnosis and prevention. Background technique [0002] Mycoplasma genitalium (Mg) is a genitourinary mycoplasma isolated from the urethral secretion of a patient with nongonococcal urethritis for the first time. Clinical studies have shown that Mg infection in women can cause cervicitis, pelvic inflammatory disease, and infertility; while infection in men can cause acute and chronic nongonococcal urethritis and infertility; in addition, Mg infection is also associated with human immunodeficiency virus (HIV) Opportunistic infections are closely related. [0003] The binding of pathogens to the corresponding receptors on the host cell membrane is the first step for pathogens to infect the host, and it is cruc...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C07K14/705C07K1/30C07K1/26G01N33/543A61K38/17A61P15/00A61P31/04
CPCA61K38/00C07K14/705G01N33/543G01N2333/705
Inventor 游晓星邓湘赢戴佩
Owner NANHUA UNIV
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