[China Pharmaceutical Network Technology News] February 25th Science Online article reported two human monoclonal antibodies, mAb100 and mAb114 protect all Ebola virus symptoms, including viremia, from non-human primates effect. Researcher at the Tsinghua University School of Medicine and Nancy J. Sullivan of NIH are co-authors of the article.
Ebola virus can cause hemorrhagic fever, high mortality, and no proven treatment. The Ebola virus that broke out in West Africa in 2014-2015 caused 11,000 deaths. An article published online on February 25th reported two human-derived monoclonal antibodies, mAb100 and mAb114, which protect against all Ebola symptoms, including viremia, in non-human primates. In addition, intravenous treatment with mAb114 alone, even after 5 days of infection, can protect the macaque from infection and death. The control macaque showed the characteristics of Ebola virus and died nine days later. Researcher at the Tsinghua University School of Medicine and Nancy J. Sullivan of NIH are co-authors of the article.
Studies have shown that mAb 114 binds to the glycoprotein of the Ebola virus core and neutralizes the virus. The glycoprotein of the Ebola virus, known as the receptor binding domain, was previously thought to be unreachable for this region with antibodies. Because it is well protected by other parts of the virus, it is only exposed after the virus enters the interior of the cell. This is the first confirmed antibody to neutralize the virus by binding to the cellular receptors of the virus.
The glycoprotein of Ebola virus is a fusion protein of disulfide-bonded subunits GP1 and GP2, which form a wine-like trimer. The binding of GP1 to the viral receptor NPC1 allows for GP2-mediated fusion of the virus and host cell membranes. The GP1 subunit contains a core domain and a sugar cap structure that is highly glycosylated mucin-like domain (MLD). Using immunoprecipitation, it was found that mAb114 and mAb100 can recognize GP subunits without MLD.
To further identify the determinants of these antibodies, the crystal structures of the antibodies mAb 114 and mAb 100 were investigated. The results suggest that mAb100 recognizes the Ebola virus glycoprotein trimer, blocks the cycle of proteolytic cleavage, and prevents proteolytic cleavage of the virus into the desired glycoprotein. It has been found that the cap structure of mAb 114 and polysaccharide and the medial action of the neck of glycoprotein maintain the removal of the polysaccharide cap structure of the relevant protein and inhibit the binding of glycoprotein and its receptor.
The study suggests that mAb114 can be used as an effective therapy and deserves further exploration. These results represent the basis for the action of these two protective antibodies and may contribute to the development of treatments and vaccines.
Ebola virus can cause hemorrhagic fever, high mortality, and no proven treatment. The Ebola virus that broke out in West Africa in 2014-2015 caused 11,000 deaths. An article published online on February 25th reported two human-derived monoclonal antibodies, mAb100 and mAb114, which protect against all Ebola symptoms, including viremia, in non-human primates. In addition, intravenous treatment with mAb114 alone, even after 5 days of infection, can protect the macaque from infection and death. The control macaque showed the characteristics of Ebola virus and died nine days later. Researcher at the Tsinghua University School of Medicine and Nancy J. Sullivan of NIH are co-authors of the article.
Studies have shown that mAb 114 binds to the glycoprotein of the Ebola virus core and neutralizes the virus. The glycoprotein of the Ebola virus, known as the receptor binding domain, was previously thought to be unreachable for this region with antibodies. Because it is well protected by other parts of the virus, it is only exposed after the virus enters the interior of the cell. This is the first confirmed antibody to neutralize the virus by binding to the cellular receptors of the virus.
The glycoprotein of Ebola virus is a fusion protein of disulfide-bonded subunits GP1 and GP2, which form a wine-like trimer. The binding of GP1 to the viral receptor NPC1 allows for GP2-mediated fusion of the virus and host cell membranes. The GP1 subunit contains a core domain and a sugar cap structure that is highly glycosylated mucin-like domain (MLD). Using immunoprecipitation, it was found that mAb114 and mAb100 can recognize GP subunits without MLD.
Ebola virus surface glycoprotein (blue) combined with protective antibody mAb114 (red/white) and mAb100 (purple/white)
To further identify the determinants of these antibodies, the crystal structures of the antibodies mAb 114 and mAb 100 were investigated. The results suggest that mAb100 recognizes the Ebola virus glycoprotein trimer, blocks the cycle of proteolytic cleavage, and prevents proteolytic cleavage of the virus into the desired glycoprotein. It has been found that the cap structure of mAb 114 and polysaccharide and the medial action of the neck of glycoprotein maintain the removal of the polysaccharide cap structure of the relevant protein and inhibit the binding of glycoprotein and its receptor.
The study suggests that mAb114 can be used as an effective therapy and deserves further exploration. These results represent the basis for the action of these two protective antibodies and may contribute to the development of treatments and vaccines.
Organic cornstarch is the lightest and most versatile starch. It is made from organic corn through multiple processes. Corn starch contains linoleic acid and vitamin E, which can lower cholesterol levels in the body, thereby reducing the occurrence of arteriosclerosis. It contains more calcium and iron, which can prevent high blood pressure and coronary heart disease. It also contains trace element selenium, which can accelerate the decomposition of oxides in the body and inhibit malignant tumors.
Corn Starch,Organic Cornstarch,Organic Corn Starch,Organic Cornstarch Powder
Organicway (xi'an) Food Ingredients Inc. , https://www.organicwayince.com