Volume 92 Issue 6 | p. 27 | Concentrates
Issue Date: February 10, 2014

Antibody-Loving Protein Binds Around

Newly discovered bacterial protein binds a cornucopia of antibodies, a property that could be leveraged to help purify the antibodies
Department: Science & Technology | Collection: Life Sciences
News Channels: Biological SCENE, Environmental SCENE
Keywords: antibody, pathogen, immune system
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Protein M (blue and red) appears to bind all antibodies it encounters, including this human antibody (green and yellow).
Credit: Christina Corbaci & Rajesh K. Grover
This blue antibody that can bind any other antibody, including the yellow and green one shown here.
 
Protein M (blue and red) appears to bind all antibodies it encounters, including this human antibody (green and yellow).
Credit: Christina Corbaci & Rajesh K. Grover

A wildly promiscuous protein produced by pathogenic Mycoplasma, such as those that cause genital and respiratory tract infections, appears to have the ability to bind any antibody it encounters—including those from humans, mice, rabbits, pigs, and goats. In doing so, the protein covers up the variable section of the antibodies, preventing them from hooking up with their intended targets (Science 2014, DOI: 10.1126/science.1246135). Researchers led by Richard A. Lerner of Scripps Research Institute California have named the antibody-interfering molecule Protein M. They believe it is unique because its crystal structure does not appear in the Protein Data Bank, the international online structure repository. Protein M is not the only pathogenic protein known to bind a variety of antibodies, but it is the largest discovered to date. Lerner’s team proposes that the protein could find good use in industry as a tool to purify antibodies. Still to be learned is exactly how the bacteria employ the protein for their own gain, although the pathogens presumably produce the protein to interfere with host immune responses and thus allow chronic infection.

 
Chemical & Engineering News
ISSN 0009-2347
Copyright © American Chemical Society

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