Bacterial superbug protein structure solved

Feb 16, 2014
This is an overall ribbon diagram of FosB from Staphylococcus aureus. The unique "door" (highlighted in orange) is shown in the open position. Credit: M.Thompson/Vanderbilt

A research team from Vanderbilt University Medical Center in Nashville, Tenn., is the first to decipher the 3-D structure of a protein that confers antibiotic resistance from one of the most worrisome disease agents: a strain of bacteria called methicillin-resistant Staphylococcus aureus (MRSA), which can cause skin and other infections. The Vanderbilt team's findings may be an important step in combatting the MRSA public health threat over the next 5 to 10 years.

By deciphering the shape of a key S. aureus —an enzyme called FosB that inactivates an antibiotic called fosfomycin—the researchers have set the stage to devising a therapeutic method to inhibit FosB and hence improve the efficacy of the antibiotic. The team will present its work at the 58th Annual Meeting of the Biophysical Society, held Feb. 15-19, 2014, in San Francisco, Calif.

"Our hope is that now that we know the 3-D shape and overall function of the FosB protein, we will be able to design inhibitors of FosB that will enable fosfomycin to function appropriately as an antibiotic," said Matthew K. Thompson, a postdoctoral researcher on the team. "When we can successfully do that, we may very well be able to combat S. aureus infections with fosfomycin."

Identifying the FosB protein's three-dimensional structure helps scientists understand that protein's particular function. In particular, the new structural images of FosB, obtained by a technique called X-ray crystallography, provide insight into the functional role of a particular part of the protein's shape called a binding loop. It appears to function like a door that opens and closes to allow the antibiotic to enter the active site of FosB.

In addition to providing new insight on the function of this S. aureus protein, the research has also produced new evidence for the role zinc might play in inhibiting FosB. This could impact restoring the efficacy of fosfomycin, leading to treatment for a variety of multi-drug-resistant pathogens.

According to the U.S. Centers for Disease Control (CDC) and Prevention, MRSA poses a serious risk to public health. Studies show that about one in three people carry S. aureus in their nose, usually without any illness, and two in 100 people carry the methicillin-resistant version of the bacteria, though there is no data to show the total number of people who get MRSA skin infections.

Explore further: Oat breakfast cereals may contain a common mold-related toxin

More information: The presentation "Structure and Function of the Genomically-encoded Fosfomycin Resistance Enzyme, FOSB, from Staphylococcus aureus" by Matthew K. Thompson, Michael Goodman, Mary Keithly, Neal Hammer, Paul Cook, Kevin Jafessar, Joel Harp, Eric Skaar and Richard N. Armstrong will be at 1:45 p.m. on Sunday, February 16, 2014 in Hall D in San Francisco's Moscone Convention Center. Abstract: tinyurl.com/kxmcerd

add to favorites email to friend print save as pdf

Related Stories

Researchers uncover keys to antibiotic resistance in MRSA

Oct 04, 2013

(Phys.org) —University of Notre Dame researchers Shahriar Mobashery and Mayland Chang and their collaborators in Spain have published research results this week that show how methicillin-resistant Staphylococcus ...

MRSA strain gained dominance with help from skin bacteria

Dec 17, 2013

Scientists believe they have an explanation for how the most common strain of methicillin-resistant Staphylococcus aureus (MRSA) rapidly rose to prominence. Research published in mBio, the online open-access journal of th ...

Recommended for you

Researchers bring clean energy a step closer

Feb 27, 2015

For nearly half a century, scientists have been trying to replace precious metal catalysts in fuel cells. Now, for the first time, researchers at Case Western Reserve University have shown that an inexpensive metal-free catalyst ...

The construction of ordered nanostructures from benzene

Feb 27, 2015

A way to link benzene rings together in a highly ordered three-dimensional helical structure using a straightforward polymerization procedure has been discovered by researchers from RIKEN Center for Sustainable ...

Superatomic nickel core and unusual molecular reactivity

Feb 27, 2015

A superatom is a combination of two or more atoms that form a stable structural fragment and possess unique physical and chemical properties. Systems, that contain superatoms, open a number of amazing possibilities ...

Oat breakfast cereals may contain a common mold-related toxin

Feb 25, 2015

Oats are often touted for boosting heart health, but scientists warn that the grain and its products might need closer monitoring for potential mold contamination. They report in ACS' Journal of Agricultural and Food Chemistry that s ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.