Cornell University researchers have discovered the 3-D crystal structure of a protein, human CD38, which may lead to important discoveries about how cells release calcium -- a mineral used in almost every cellular process. The findings also may offer insights into mechanisms involved in certain diseases, ranging from leukemia to diabetes and HIV-AIDS.
Qun Liu and Quan Hao. Copyright Elsevier Ltd.
This artistic rendering of the molecular structure of human CD38 appears on the cover of this months issue of the journal Structure. Copyright © Cornell University
Levels of the protein climb, for reasons unknown, when people fall ill, making human CD38 a marker for these diseases.
As one example, researchers have shown that CD38 interrupts an interaction between the AIDS virus and its point of entry into cells -- a protein receptor called CD4. By looking at CD38s 3-D structure, the Cornell researchers identified a peptide, an organic compound composed of amino acids, that they believe may play a role in interrupting the interface between CD4 and HIV-AIDS.
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Staphylococcus aureus is a feared pathogen (MRSA, multi-resistant S. aureus) due to frequent resistances against many antibiotics, especially in hospital infections. Researchers at the Paul-Ehrlich-Institut have identified immunological processes that prevent a successful immune response directed against the pathogenic agent. The delivery of bacterial proteins with RNA adjuvant or messenger RNA (mRNA) into immune cells allows the re-direction of the immune response towards an active defense against S. aureus. This could be of significant importance for the development of an effective vaccine. PLOS Pathogens has published these research results online on 25 May 2017.
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