Archive of Medical Research

Viral vectors for production of recombinant proteins in plants.

Global demand for recombinant proteins has steadily accelerated for the last 20 years. These recombinant proteins have a wide range of important applications, including vaccines and therapeutics for human and animal health, industrial enzymes, new materials and components of novel nano-particles for various applications. The majority of recombinant proteins are produced by traditional biological \”factories,\” that is, predominantly mammalian and microbial cell cultures along with yeast and insect cells. However, these traditional technologies cannot satisfy the increasing market demand due to prohibitive capital investment requirements. During the last two decades, plants have been under intensive investigation to provide an alternative system for cost-effective, highly scalable, and safe production of recombinant proteins. Although the genetic engineering of plant viral vectors for heterologous gene expression can be dated back to the early 1980s, recent understanding of plant virology and technical progress in molecular biology have allowed for significant improvements and fine tuning of these vectors. These breakthroughs enable the flourishing of a variety of new viral-based expression systems and their wide application by academic and industry groups. In this review, we describe the principal plant viral-based production strategies and the latest plant viral expression systems, with a particular focus on the variety of proteins produced and their applications. We will summarize the recent progress in the downstream processing of plant materials for efficient extraction and purification of recombinant proteins. J. Cell. Physiol. (c) 2008 Wiley-Liss, Inc.

Lico C, Chen Q, Santi L.

UTS BIOTEC, Section of Genetics and Plant Genomics, ENEA CR Casaccia, Rome, Italy.

Pyrin, product of the MEFV locus, interacts with the proapoptotic protein, Siva.

Mutations in pyrin cause the autoinflammatory disorder familial Mediterranean fever (FMF), a syndrome characterized by sporadic and unpredictable attacks of fever and localized severe pain. Currently, it is not clear how attacks are triggered, nor why they spontaneously resolve after 2 or 3 days. In fact, the cellular function of the pyrin protein and the molecular underpinnings of its malfunction in FMF have so far eluded clear definition. The identification of pyrin-interacting proteins has the potential to increase our understanding of the cellular networks in which pyrin functions. Previous reports have established that pyrin interacts with the apoptotic protein ASC, the cytoskeletal adaptor protein PSTPIP1, the inflammatory caspase, Caspase-1 and certain forms of the cytosolic anchoring protein 14-3-3. Here, we report that pyrin also interacts with Siva, a pro-apoptotic protein first identified for its interaction with the cytosolic tail of CD27, a TNF family receptor. The interaction between pyrin and Siva involves the C-terminal B30.2/rfp/SRPY domain of pyrin and exon 1 of Siva. We show that Siva and pyrin are indeed co-expressed in human neutrophils, monocytes, and synovial cells. Furthermore, using a novel protein/protein interaction assay, we demonstrate that pyrin can recruit Siva to ASC specks, establishing a potential platform for intersection of ASC and Siva function. Finally, we show that pyrin modulates the apoptotic response to oxidative stress mediated by Siva. Thus, the Siva-pyrin interaction may be a potential target for future therapeutic strategies. J. Cell. Physiol. (c) 2008 Wiley-Liss, Inc.

Balci-Peynircioglu B, Waite AL, Hu C, Richards N, Staubach-Grosse A, Yilmaz E, Gumucio DL.

Department of Medical Biology, Faculty of Medicine, Hacettepe University, Ankara, Turkey.

Transparent Carbon Films as Electrodes in Organic Solar Cells.

Wang X, Zhi L, Tsao N, Tomović Z, Li J, Müllen K.

Max-Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany, Fax: (+49) 6131-379-350.

Expanding the Synthetic Potential of Asymmetric Deprotonation: Arylation of Carbanions.

O\’Brien P, Bilke JL.

Department of Chemistry, University of York, Heslington, York YO10 5DD, UK, Fax: (+44) 1904-432-535.

Helical (5Z, 11E)-Dibenzo[a,e]cyclooctatetrene: A Spring-Loaded Monomer.

Carnes M, Buccella D, Decatur J, Steigerwald ML, Nuckolls C.

Department of Chemistry and, The Center for Electron Transport in Molecular Nanostructures, Columbia University, New York, NY 10027, USA, Fax: (+1) 212-932-1289 http://nuckolls.chem.columbia.edu.

Distannylations and Silastannylations of In Situ Generated Allenes.

Wesquet AO, Kazmaier U.

Institut für Organische Chemie, Universität des Saarlandes, Im Stadtwald, Geb. C4.2, 66123 Saarbrücken, Germany, Fax: (+49) 681–302–2409 http://www.uni-saarland.de/fak8/kazmaier/

The Groves-Spiro Dioxomanganese(V) Story.

Gross Z.

Schulich Faculty of Chemistry, Technion—Israel Institute of Technology, Haifa 32,000, Israel, Fax: (+972) 4829-5703.

A Nitrido-Centered Uranium Azido Cluster Obtained from a Uranium Azide.

Nocton G, Pécaut J, Mazzanti M.

Laboratoire de Reconnaissance Ionique et Chimie de Coordination, Laboratoire de Chimie Inorganique et Biologique, (UMR-E 3 CEA-UJF), INAC, CEA-Grenoble, 17 rue des Martyrs, 38054 Grenoble, Cedex 09, France, Fax: (+33) 4-3878-5090.

Porous, Covalent Triazine-Based Frameworks Prepared by Ionothermal Synthesis.

Kuhn P, Antonietti M, Thomas A.

Max Planck Institute of Colloids and Interfaces, Research Campus Golm, 14424 Potsdam, Germany, Fax: (+49) 331-567-9502.

Evolution of Chemical Bonding during HCNright arrow over left arrowHNC Isomerization as Revealed through Nuclear Quadrupole Hyperfine Structure.

Bechtel HA, Steeves AH, Wong BM, Field RW.

Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Fax: (+1) 617-253-7030 rwf.mit.edu.