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The study, titled “Predicting HIV-1 transmission and antibody neutralization efficacy in vivo from stoichiometric parameters,” is published online May 4, 2017 in the journal PLoS Pathogens. Study authors include Oliver Brandenberg at California Institute of Technology, Carsten Magnus and Roland Regoes at ETH Zurich, and Peter Rusert, Huldrych Günthard, and Alexandra Trkola at the University of Zürich.
Broadly neutralizing antibodies (bNAbs) are neutralizing antibodies which neutralize multiple HIV-1 viral strains. The potent effect of bNAbs that target the HIV-1 envelope glycoprotein trimer (Env) has opened a new avenue for therapies and vaccines. Unfortunately, the implementation of these antibodies is impeded by multiple questions. If we can better understand HIV-antibody interactions and the mucosal transmission process, it may accelerate the development of HIV management strategies.
The researchers started by studying how many neutralizing antibodies (nAbs) are required to neutralize each HIV-1 envolop HIV-1 Env trimer. Next, they looked into the mechanism of mucosal HIV-1 transmission. Finally, they used all previously determined parameters to model human HIV-1 sexual transmission.
The researchers noted that their study represents a useful tool to enhance our knowledge of virus-antibody interactions and viral mucosal transmission and may lay the foundation for future development of HIV-antibody-based therapies and vaccines. (Cusabio offers various antibodies.
Researchers have resolved the three-dimensional structure of the cystic fibrosis transmembrane conductance regulator (CFTR), according to a paper appearing in the journal Cell.
The CFTR protein, which is encoded by the CFTR gene, functions as a channel across the membrane of cells that produce mucus, sweat, saliva, tears, and digestive enzymes. It transports chloride ions into and out of cells. CFTR has been implicated in several human diseases, including cystic fibrosis. Cystic fibrosis is caused by the presence of mutations in both copies of CFTR gene. The mutated CFTR causes the body to produce abnormally thick and sticky mucus. This kind of mucus accumulates in various organs, mostly the lungs, causing tissue damage. Over time, cystic fibrosis can lead to difficulty breathing and frequent lung infections.
Cystic fibrosis has no cure. The primary goals of current treatment are to control lung infection and manage complications. To develop more specific treatments for the disease, a better understanding of CFTR s function is necessary. However, the human CFTR protein is unable to work well in the lab.
Given that a number of animals also have the protein, the researchers chose to study the zebrafish version of CFTR. They used zebrafish CFTR to map the location of disease-causing mutations. Using an imaging technique called cryo-electron microscopy, they revealed the detailed structure of both human and zebrafish CFTR, and found that under identical conditions human CFTR structure is very similar to zebrafish CFTR structure.
The structural data presented in the study would help understand CFTR function and how mutations in it can trigger cystic fibrosis. Although cystic fibrosis is a rare disease, affecting 70,000 people worldwide, it can seriously affect quality of life. Patients require long-term treatment, frequent hospitalization, and even lung transplant.
The study is carried out by Fangyu Liu, Zhe Zhang, David Gadsby, and Jue Chen from The Rockefeller University in collaboration with László Csanády from Semmelweis University. Besides, CFTR and other proteins and antibodies can be offered by CusAb. http://www.cusabio.com/