Features | Partner Sites | Information | LinkXpress
Sign In
GLOBETECH PUBLISHING LLC
GLOBETECH PUBLISHING LLC
PZ HTL SA

A Unique Mycoplasma Protein Generically Binds All Types of Antibodies and Blocks Antigen Binding

By BiotechDaily International staff writers
Posted on 20 Feb 2014
Image: Protein M, an unusual bacterial protein, attaches to virtually any antibody, possibly helping bacteria establish long-term infections. Compared to thousands of known structures, this protein appears to be unique (Photo courtesy of the Scripps Research Institute).
Image: Protein M, an unusual bacterial protein, attaches to virtually any antibody, possibly helping bacteria establish long-term infections. Compared to thousands of known structures, this protein appears to be unique (Photo courtesy of the Scripps Research Institute).
A team of molecular biologists has isolated a bacterial protein that binds to all types of antibodies and prevents them attaching to their specific antigens.

The novel protein—Protein M—may join the ranks of other nonspecific antibody binding proteins such as Protein A and Protein G as a tool for researchers seeking to purify antibodies from mixtures of other biological molecules.

Investigators at The Scripps Research Institute (La Jolla, CA, USA) discovered Protein M, which was being produced by the primitive bacterium Mycoplasma genitalium, during a study on the relationship between chronic bacterial infection and myeloma.

After isolating the protein, the investigators used X-ray crystallography and other techniques, including electron microscopy, to determine Protein M's three-dimensional atomic structure while the protein was bound to various human antibodies. They reported in the February 7, 2014, issue of the journal Science that the crystal structure of the external domain of transmembrane Protein M differed from other known protein structures, as did its mechanism of antibody binding. Protein M bound with high affinity to all types of human and nonhuman immunoglobulin G, predominantly through attachment to the conserved portions of the variable region of the kappa and gamma light chains. Furthermore, Protein M blocked antibody-antigen binding, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens.

The investigators suggested that the most immediate use for Protein M will likely be as a tool for immobilizing antibodies in mixtures and cell cultures as a preparatory step in the generation of highly purified antibodies for research and drug manufacturing. “It may be the most useful antibody purification device ever found,” said senior author Dr. Richard A. Lerner, professor of immunochemistry at The Scripps Research Institute.

Related Links:

The Scripps Research Institute



comments powered by Disqus

Channels

Drug Discovery

view channel
Image: Disruption and removal of malaria parasites by the experimental drug (+)-SJ733 (Photo courtesy of the University of California, San Francisco).

Experimental Antimalaria Drug Induces the Immune System to Destroy Infected Red Blood Cells

An experimental drug for the treatment of malaria was found to induce morphological changes in infected erythrocytes that enabled the immune system to recognize and eliminate them. Investigators at... Read more

Biochemistry

view channel

Blocking Enzyme Switch Turns Off Tumor Growth in T-Cell Acute Lymphoblastic Leukemia

Researchers recently reported that blocking the action of an enzyme “switch” needed to activate tumor growth is emerging as a practical strategy for treating T-cell acute lymphoblastic leukemia. An estimated 25% of the 500 US adolescents and young adults diagnosed yearly with this aggressive disease fail to respond to... Read more

Business

view channel

R&D Partnership Initiated to Reduce Development Time for New Drugs

nanoPET Pharma, GmbH (Berlin, Germany) signed an open-ended framework contract with the international pharmaceutical company Boehringer Ingelheim (Ridgefield, CT, USA). By developing customized contrast agents for research in both basic and preclinical studies, nanoPET Pharma will contribute to the enhancement of Boehringer... Read more
 
Copyright © 2000-2014 Globetech Media. All rights reserved.