June 16, 2011 Researchers report that a sugar-binding protein called galectin-9 traps PDI on T-cells' surface, making them more susceptible to HIV infection.
Specific types of "helper" T cells that are crucial to maintaining functioning immune systems contain an enzyme called PDI (protein disulfide isomerase). This enzyme affects how proteins fold into specific shapes, which in turn influences how the T cells behave. PDI also plays a role in HIV infection by helping to change the shape of the surface envelope protein of the virus, enabling the virus to interact optimally with receptors on the T cells, such as the CD4 molecule.
Though it is known that PDI inhibitors can prevent HIV infection, just how this happens has remained a mystery. And though it has been known that PDI, which normally lives inside the cell, can become entrapped on the cell's surface, it has not been understood how this happens.
Now, in a new study, UCLA researchers report that a sugar-binding protein called galectin-9 traps PDI on T-cells' surface, making them more susceptible to HIV infection.
IMPACT: The findings could lead researchers to a potential new target for anti-HIV therapeutics, such as therapies to inhibit PDI or galectin-9.
The National Institutes of Health supported the study.
Other social bookmarking and sharing tools:
The above story is reprinted from materials provided by University of California - Los Angeles Health Sciences, via EurekAlert!, a service of AAAS.
Note: Materials may be edited for content and length. For further information, please contact the source cited above.
- S. Bi, P. W. Hong, B. Lee, L. G. Baum. Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proceedings of the National Academy of Sciences, 2011; DOI: 10.1073/pnas.1017954108
Note: If no author is given, the source is cited instead.