Antibiotic compound Sulfamethoxazole can reduce adverse events in HIV infected patients

In a new study, researchers from Britain, Japan and Zimbabwe found that a common antibiotic called compound sulfamethoxazole reduced adverse health events in children infected with HIV. The study describes the effectiveness of the antibiotic in young HIV patients and what they found.
In the past few decades, scientists have made so much progress in treating HIV infection that it is no longer considered fatal, at least among people living in developed countries. But in many parts of Africa, the situation is grim, with many infected people unable to afford the drugs needed to treat the infection. There is also the problem of high transmission rates. In response, medical workers in Africa have been looking for other ways to help people living with HIV, especially children. One way to do this is to use the cheap compound sulfamethoxazole, which is preventative. It is speculated that the antibiotic may also reduce adverse health events associated with HIV infection, such as pneumonia. In the new study, the researchers tried to determine whether the antibiotic actually helped people with HIV.
The researchers gave compound sulfamethoxazole to 300 Hiv-infected children living in Zimbabwe for 100 weeks. They then collected plasma samples from all children infected with HIV and stopped giving the antibiotic to half of them. They recollected plasma samples from all the children after 36 weeks and compared their findings.
The researchers reported lower levels of systemic inflammation in children who continued to receive compound sulfamethoxazole than in those who stopped taking it. They also found a decrease in streptococci levels and activity in the intestines. More specifically, they found that children who stopped taking the antibiotic were 28 percent more likely to have an adverse health event than those who continued using the drug.
Further studying the effects of the antibiotic on the body, the researchers found that in 20 adults infected with HIV, ......

BRISC-SHMT2 protein complex regulates immune signalling

Researchers from the University of Leeds and the University of Pennsylvania have discovered a new internal regulator that helps control the body's response to infection. This finding may open up new avenues for the development of drugs for the treatment of autoimmune diseases (type 1 diabetes, rheumatoid arthritis, lupus and scleroderma).
The researchers observed the detailed structure of the regulator through a powerful cryo-electron microscope at the Astbury Center at the University of Leeds. It consists of two proteins, called BRISC and SHMT2. The SHMT2 protein is a small molecule, but there are many evidences show it is involved in cellular metabolism and immune responses. By establishing a precise 3D model, they found that the BRISC-SHMT2 complex played a completely unexpected role in regulating immune responses.
The role of protein complexes is to increase the cellular immune response, which occurs when they detect invading pathogens. The structure of the protein complex is resolved, it is possible to design a genetically engineered version of the protein and map the function of the complex in the cell.
The scientists also found that the BRISC-SHMT2 protein complex can be regulated by the active form of vitamin B6.
Although experiments have shown that vitamin B6 is proven to be important for the function of this regulator, they warned that further research is needed to fully understand its role.
This research uses cutting-edge techniques to reveal the basic biological functions of two proteins and how they interact to control the body's immune response to infection. Destroying these proteins may be a new way to address autoimmune diseases. The study may help scientists find a new drug for this regulator that suppresses the immune system and prevents the body from destroying its cells without infection.
"We have a long way to go to find a new way to treat autoimmune diseases, but we are excited because this discovery may open th......

Study on the expression level of prostate acid phosphatase in ovarian cancer

Ovarian cancer is a common tumor in women, because the ovary is in the depths of the pelvic cavity, so early ovarian cancer often does not have obvious symptoms, generally diagnosed when it has been late, the mortality rate is higher. It is important to search for better early diagnostic indicators and new therapeutic targets.
The expression of prostate-associated antigen, or prostate acid phosphatase (PAP), has been found in many other epithelial tumors, including gastric cancer, colon cancer, and breast cancer. PAP is an enzyme synthesized by prostate epithelial cells, which is the main source of male serum acid phosphatase (APC) and an isoenzyme produced by lysosomes of prostate epithelial cells in APC. The prostate gland is the main source of this enzyme. PAP is a glycoprotein composed of 2 subunits, mainly distributed in urine and low in serum. Increased serum PAP is often used as the diagnostic criteria for prostate cancer. PAP has always been considered as a specific tumor marker of prostate cancer. According to the latest research, PAP also exists in the prostate and other tissues besides prostate cancer, so PAP is not an absolute tissue specific marker. In addition, the researchers confirmed the presence of prostate-associated antigen, or prostate acid phosphatase (PAP), in epithelial tissues of patients with a variety of cancers, but there has been no systematic study of PAP expression in ovarian cancer. Therefore, the researchers can use this as a starting point to test the expression level of PAP in the cancer cells and tumor tissues of ovarian cancer patients, and explore the possibility of PAP as the target for diagnosis and treatment of ovarian cancer, so as to provide further research basis for the diagnosis and treatment of ovarian cancer.
E0168r is a microwave band ELISA kit for the analysis of lysins and metalloproteinases 30(prostate acid phosphatase) in biological samples. The concentration gradient of the standard or positive contr......

New therapeutic target BPTF to c-MYC related cancers

c-MYC is one of the major proteins that regulate gene expression in cells. c-MYC regulates 2000-3000 genes and accounts for 15% of the entire genome. Therefore, c-MYC is involved in many cellular functions: cell growth, proliferation, differentiation, and apoptosis.
When c-MYC regulation occurs abnormally, it promotes a variety of cancers, such as pancreatic cancer, colon cancer, ovarian cancer, and lymphoma. The c-MYC gene has changed in more than half of human cancers and is often associated with very aggressive tumors.
Researchers at the Spanish National Cancer Research Center (CNIO) have successfully identified a protein that is critical for MYC carcinogenesis in a mouse model. The study used genome-wide data analysis to investigate the behavior of c-MYC in a network of hundreds of genes.
They found c-MYC interacts with BPTF, it is a core subunit of the NURF chromatin-remodelling complex. BPTF is required for the activation of the full c-MYC transcriptional programme in fibroblasts. When BPTF is knockdown, c-MYC recruitment to DNA is decreased and chromatin accessibility changes. In Bptf-null MEFs, BPTF is necessary for c-MYC-driven proliferation, G1–S progression and replication stress, but not for c-MYC-driven apoptosis. It is also found that BPTF levels correlate positively with c-MYC-driven transcriptional signatures. In vivo, Bptf inactivation in pre-neoplastic pancreatic acinar cells significantly delays tumour development and extends survival.
This study confirms that blocking BPTF, tumor cells fail to proliferate or their proliferation is inhibited; therefore, the researchers believe that this gene may be a new target for the treatment of many cancer types.
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To reveal the mechanism of HIV escape human defense system

A joint team of researchers at the University of California, San Francisco, and others have discovered the molecular mechanism by which HIV, the human immunodeficiency virus that causes AIDS, escapes from the defenses of host cells.
After the initial HIV invasion into the human body, immune cells are gradually destroyed, making the body vulnerable to pathogen infection and causing various diseases. The medical community has shown that there is no treatment to completely eliminate HIV from the body, infected people need to continue to take antiviral drugs for treatment. As virus genes mutate, resistant viruses emerge that cannot be treated with drugs. So while HIV vaccines are being developed, new drugs for resistant viruses need to be developed.
Human cells have corresponding defenses against various viruses. For example, SAMHD1 is an enzyme produced by human cells that strongly blocks HIV-infected macrophages and T cells. On the other hand, the particles of hiv-2, which many infected people carry, contain a protein called VPX that breaks down SAMHD1 in the cells, causing hiv-2 to infect bone marrow cells.
Most viral proteins work with the help of "virus regulators" in human cells. They searched for VPX interacting proteins from more than 300 host proteins involved in phosphorylation and found that PIM kinase host proteins bind to VPX effectively and are specifically phosphorylated. Mass spectrometer analysis showed that serine, the 12th amino acid of VPX, was phosphorylated by PIM kinase. If the serine is replaced, the phosphorylation of VPX will not occur and the virus's replication ability will be reduced.
The results show that host PIM kinase is the factor that VPX ACTS on SAMHD1, and can effectively block the replication of hiv-2 by blocking PIM kinase.