Science

Monomeric CH3: A Small, Stable Antibody Domain with Therapeutic Promise

Two men talking by the computer

Tianlei Ying, Ph.D. (facing camera), postdoctoral fellow, and Dimiter Dimitrov, Ph.D., head, Protein Interactions Group, Cancer and Inflammation Program, Center for Cancer Research.

By Ashley DeVine, Staff WriterPlatinum Highlight Icon

Antibody domains are emerging as promising biopharmaceuticals because of their relatively small size compared to full-sized antibodies, which are too large to effectively penetrate tumors and bind to sterically restricted therapeutic targets.

In an article published in The Journal of Biological Chemistry, Tianlei Ying, Ph.D., Dimiter Dimitrov, Ph.D., and their colleagues in the Protein Interactions Group, Cancer and Inflammation Program, Center for Cancer Research, reported their design of a novel antibody domain, monomeric CH3 (mCH3).

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New Animal Model Could Boost Research on AIDS Drugs and Vaccines

Monkeys with cells illustration

The figure shows the serial passage of minimally changed HIV into a series of pigtail macaques to adapt the virus, which became capable of causing AIDS in the monkeys, beginning after the third animal-to-animal passage (“P4” in the figure). Inverted monkey icons indicate animals that succumbed to AIDS-defining conditions. The background demonstrates depletion of CD4+ T cells from gut-associated lymphoid tissues, a hallmark of AIDS virus pathogenesis.

By Frank Blanchard, Staff Writer, and Jeff Lifson, Guest Writer

In a research milestone reported in the June 20 issue of the journal Science, scientists have developed a minimally modified version of HIV-1, the virus that causes AIDS in infected humans, that is capable of causing progressive infection and AIDS in monkeys. The advance should help create more authentic animal models of the disease and provide a potentially invaluable approach for faster and better preclinical evaluation of new drugs and vaccines.

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NCI Researchers Discover Exceptionally Potent Antibodies with Potential for Prophylaxis and Therapy of MERS-Coronavirus Infections

Crystal structures.

Docked complexes of MERS-CoV RBD with mAbs (A) m336, (B) m337, and (C) m338. (D) Superposition of the docked complexes of RBD-m336,7,8 and the crystal structure of the RBD-DPP4 complex.

By Andrea Frydl, Contributing Writer

In a recent article published in the Journal of Virology, Tianlei Ying, Ph.D., Dimiter Dimitrov, Ph.D., and their colleagues in the Laboratory of Experimental Immunology (LEI), Cancer and Inflammation Program, NCI Center for Cancer Research, reported the identification of three human monoclonal antibodies (m336, m337, and m338) that target the part of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) that is responsible for binding to its receptor. These antibodies are exceptionally potent inhibitors of MERS-CoV infection and also provide a basis for creating a future MERS-CoV vaccine.

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Second Annual David Derse Memorial Lecture and Award

Three people with an award.

Second Annual David Derse Memorial Lecture and Award. From left: Hye Kyung Chung-Derse, Ph.D.; Chou-Zen Giam, Ph.D.; and Stephen Hughes, Ph.D., director, HIV Drug Resistance Program. 

By Anne Arthur, Guest Writer

The Second Annual David Derse Memorial Lecture and Award presentation was held on November 12, 2013, at the NCI at Frederick Conference Center to honor David Derse’s outstanding research accomplishments and to stimulate the exchange of innovative ideas that Derse was well known for promoting throughout his scientific career.

The Annual David Derse Memorial Lecture and Award is sponsored by the HIV Drug Resistance Program, with support from Hye Kyung Chung-Derse, Ph.D., the National Cancer Institute (NCI), the Foundation for the National Institutes of Health (NIH), and colleagues and friends of Derse who contributed to the memorial fund in his honor.

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