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Study identifies mechanism underlying multidrug resistance in fungi
Date:4/2/2008

patients with compromised immunity, says Nr, an assistant professor of Cell Biology at Harvard Medical School (HMS).

The researchers also found exactly how Pdr1p turns on the multidrug resistance program. After binding to drugs, the Pdr1p protein partners with another key mediator of genetic switches called Gal11p. In-depth molecular and structural studies in collaboration with the team of co-author Gerhard Wagner, PhD, Elkan Blout Professor of Biological Chemistry and Molecular Pharmacology at HMS identified the specific area of Gal11p that binds to Pdr1p to induce multidrug resistance.

This detailed understanding of the interaction between these proteins will allow screening for small-molecule inhibitors of protein binding. Such inhibitors may lead to novel co-therapeutics that will sensitize multidrug-resistant fungal infections to standard antifungal therapy, says Wagner.

To further investigate the relevance of their findings, the researchers used a C. elegans roundworm model system recently developed by co-author Eleftherios Mylonakis, MD, PhD, of MGH Infectious Disease to study fungal pathogens. They found that worms infected with Candida glabrata that lacked either the Pdr1p or Gal11p proteins could be successfully treated with typical antifungal medications, suggesting that targeting the gene switch controlled by those proteins interaction could restore the effectiveness of standard drugs.

Fungal infections have a serious impact on immunocompromised patients, and the development of resistance is particularly worrisome, since targets for antifungal drugs are limited, says Mylonakis, an assistant professor of Medicine at HMS. Given these concerns, having the opportunity to use our model system for the in vivo investigation of this resistance mechanism has been a particularly fulfilling endeavor.


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Contact: Sue McGreevey
smcgreevey@partners.org
617-724-2764
Massachusetts General Hospital
Source:Eurekalert

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