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Rockville, MD, United States

Emergent BioSolutions is a multinational specialty biopharmaceutical company headquartered in Rockville, Maryland. It develops vaccines and antibody therapeutics for infectious diseases, oncology and autoimmune disorders.The company has two divisions: a Biodefense division for medical countermeasures and a Biosciences division to treat infectious disease, autoimmune diseases, and cancer.Fuad El-Hibri, the founder of the company and former CEO, led the company since its founding as BioPort Inc. until his retirement on April 1, 2012. He continues to serve as the executive chairman of Emergent BioSolutions’ board of directors. The current CEO is Daniel Abdun-Nabi. Wikipedia.

McAtee C.P.,SACHEM Inc | Hornbuckle J.,Emergent BioSolutions
Current Protocols in Protein Science | Year: 2012

This unit discusses the important parameters in designing and optimizing a separation of monoclonal antibody (mAb) charge variants from process streams by ion-exchange displacement chromatography, including sample preparation and selection of matrix, column, and appropriate buffer. A protocol is provided for determination of optimal column binding and displacement conditions, including cleaning and regeneration of the displacement columns. © 2012 by John Wiley & Sons, Inc.

Park J.,University of Michigan | Chen Y.,University of Chicago | Tishkoff D.X.,University of Michigan | Tishkoff D.X.,Emergent BioSolutions | And 11 more authors.
Molecular Cell | Year: 2013

Protein function is regulated by diverse posttranslational modifications. The mitochondrial sirtuin SIRT5 removes malonyl and succinyl moieties from target lysines. The spectrum of protein substrates subject to these modifications is unknown. We report systematic profiling of the mammalian succinylome, identifying 2,565 succinylation sites on 779 proteins. Most of these do not overlap with acetylation sites, suggesting differential regulation of succinylation and acetylation. Our analysis reveals potential impacts of lysine succinylation on enzymes involved in mitochondrial metabolism; e.g., amino acid degradation, the tricarboxylic acid cycle (TCA) cycle, and fatty acid metabolism. Lysine succinylation is also present on cytosolic and nuclear proteins; indeed, we show that a substantial fraction of SIRT5 is extramitochondrial. SIRT5 represses biochemical activity of, and cellular respiration through, two protein complexes identified in our analysis, pyruvate dehydrogenase complex and succinate dehydrogenase. Our data reveal widespread roles for lysine succinylation in regulating metabolism and potentially other cellular functions. © 2013 Elsevier Inc.

Tian J.-H.,Intercell | Tian J.-H.,Novavax | Fuhrmann S.R.,Intercell | Fuhrmann S.R.,Intrexon Corporation | And 6 more authors.
Vaccine | Year: 2012

Antibodies targeting the Clostridium difficile toxin A and toxin B confer protective immunity to C. difficile associated disease in animal models and provided protection against recurrent C. difficile disease in human subjects. These antibodies are directed against the receptor binding domains (RBD) located in the carboxy-terminal portion of both toxins and inhibit binding of the toxins to their receptors. We have constructed a recombinant fusion protein containing portions of the RBD from both toxin A and toxin B and expressed it in Escherichia coli. The fusion protein induced high levels of serum antibodies to both toxins A and B capable of neutralizing toxin activity both in vitro and in vivo. In a hamster C. difficile infection model, immunization with the fusion protein reduced disease severity and conferred significant protection against a lethal dose of C. difficile spores. Our studies demonstrate the potential of the fusion protein as a vaccine that could provide protection from C. difficile disease in humans. © 2012 Elsevier Ltd.

Phillips A.H.,Genentech | Phillips A.H.,St Jude Childrens Research Hospital | Schoeffler A.J.,Genentech | Matsui T.,SLAC | And 7 more authors.
Nature Structural and Molecular Biology | Year: 2014

Cellular inhibitor of apoptosis 1 (cIAP1) is a ubiquitin ligase with critical roles in the control of programmed cell death and NF-ΰ B signaling. Under normal conditions, the protein exists as an autoinhibited monomer, but proapoptotic signals lead to its dimerization, activation and proteasomal degradation. This view of cIAP1 as a binary switch has been informed by static structural studies that cannot access the protein's dynamics. Here, we use NMR spectroscopy to study micro-and millisecond motions of specific domain interfaces in human cIAP1 and use time-resolved small-angle X-ray scattering to observe the global conformational changes necessary for activation. Although motions within each interface of the 'closed' monomer are insufficient to activate cIAP1, they enable associations with catalytic partners and activation factors. We propose that these internal motions facilitate rapid peptide-induced opening and dimerization of cIAP1, which undergoes a dramatic spring-loaded structural transition. © 2014 Nature America, Inc. All rights reserved.

Emergent BioSolutions | Date: 2015-01-07

Disclosed herein are compounds of Formula I wherein R1, R2, X, and Y are defined herein. These compounds are type II topoisomerase inhibitors and can be used in methods for treating infections caused by gram-positive pathogens, gram-negative pathogens, and drug-resistant strains thereof.

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