Anaplastic large cell lymphoma, a form of non-Hodgkin lymphoma, is the most common aggressive lymphoma in children. Chemotherapy and radiation fail to cure about 30% of cases. When tumors are driven by the oncogene ALK—which is the case for the majority of children—kinase inhibitor drugs like crizotinib are very effective in blocking tumor growth. They also lack the serious side effects of chemotherapy.

However, ALK inhibitors also very expensive—about $80,000 a year—and must be taken for a lifetime. As soon as they’re stopped, the lymphoma comes back. Roberto Chiarle, MD, a hematopathologist and researcher at Boston Children’s Hospital, wanted to know why.

“ALK inhibitors can control the lymphoma, but you cannot reach a cure,” he says. “Why do lymphoma cells persist for so long?”

Scientists have shown that a protein called NLRP11 has an essential role in the immune system; it alerts the body that a bacterial infection is occurring, triggering an immune response that battles the bacterial invader. NLRP11 appears to identify bacteria that are taken up by immune cells called macrophages, by recognizing a part of the bacterial coat. These findings have provided new insights into our understanding of the immune response to bacterial infection, and have been reported in Science Immunology.

The NLRP11 protein is expressed by humans, but not mice, which are a common animal model for infection. In this study, the researchers overcame that gap by using a mouse model that expressed a so-called humanized immune system. Humanized mice have been grafted with human cells and tissues so they replicate human biological functions more accurately.

At Prenuvo, we provide whole body, radiation-free MRI scans in order for our patients to focus on early detection of over 500 cancers and diseases.

Antiviral therapies are notoriously difficult to develop, as viruses can quickly mutate to become resistant to drugs, or hide within cells. Researchers at NYU have now developed a new approach to antiviral treatment that ignores the fast-mutating proteins on the surface of viruses and instead targets lipids in the membranes of enveloped viruses, which disrupts their protective layers. In a newly published study the researchers showed how these novel peptoid molecules, inspired by the immune system, could inactivate several viruses, including Zika and chikungunya. The team suggests their approach may not only lead to drugs that can be used against many viruses, but could also help overcome antiviral resistance.

“We found an Achilles heel of many viruses: their bubble-like membranes,” said Kent Kirshenbaum, PhD, professor of chemistry at NYU. “Exploiting this vulnerability and disrupting the membrane is a promising mechanism of action for developing new antivirals.” Kirshenbaum is senior author of the team’s published paper in ACS Infectious Diseases, which is titled “Peptidomimetic Oligomers Targeting Membrane Phosphatidylserine Exhibit Broad Antiviral Activity.”

In their paper the authors concluded, “We provide the first evidence for the engagement of distinct viral envelope lipid constituents, establishing an avenue for specificity that may enable the development of a new family of therapeutics capable of averting the rapid development of resistance.”