Non-transmissibility of Pepper whitefly borne vein yellows virus (PeWBVYV) by the Mediterranean species of Bemisia tabaci and identification of a candidate insect receptor protein for poleroviruses

Recent reports of transmission of poleroviruses by whiteflies is indicative of evolution of new virus-vector relationships. Pepper whitefly-borne vein yellows virus (PeWBVYV), was the first report of a polerovirus infecting pepper in Israel which was transmitted by whiteflies (MEAM1) and not aphids. This study reports the inability of the Mediterranean species (MED, Q biotype) of B. tabaci to transmit PeWBVYV. However we show that non-transmission of PeWBVYV by MED is not due to the lack of interaction with the GroEL protein of the Hamiltonella symbiont. Although not transmitted by MED, PeWBVYV was detected in its hemolymph, indicating its translocation across the MED midgut barrier. The aphid transmitted Pepper vein yellows virus 2 (PeVYV-2) was also detected in the hemolymph of MEAM1 whiteflies but PeWBVYV could not be detected in the aphid hemolymph. Interestingly, relative amounts of PeWBVYV in the hemolymph of the, MED was much lower than in hemolymph of MEAM1 whiteflies. We also identified a candidate receptor protein, complement component 1Q sub-complement binding protein (C1QBP) which interacts with the capsid proteins of PeWBVYV and PeVYV-2 but not with the whitefly transmitted Tomato yellow leaf curl virus by a yeast two-hybrid approach using the minor capsid protein (RTD) as bait to screen for interacting proteins against the whitefly cDNA library. C1QBP, is a known receptor of bacterial and viral pathogens but this is the first report of its interaction with a plant virus.

Implantomics: A Paradigm Shift in Implantology

Implantomics is the science of the implantome. The implantome is a blend of the two terms implant and proteome. The proteome is defined as the protein complement of the genome. The term proteome also implies the mass screening of proteins for the determination of all proteins - and indirectly of all genes - involved in a certain tissue or organ response. In this sense the term proteome is employed here in a new way to specify the totality of proteins associated with a foreign body inserted into the human body. It will be addressed, why the determination of the implanttome is important and which role the implantome may play in the bone-implant interface.

A Glycal-Based Photoaffinity Probe That Enriches Sialic Acid Binding Proteins

<p>To identify sialic acid binding proteins from complex proteomes, three photocrosslinking affinity-based probes were constructed using Neu5Ac (<b>5 </b>and <b>6</b>) and Neu5Ac2en (<b>7</b>) scaffolds. Kinetic inhibition assays and Western blotting revealed the Neu5Ac2en-based <b>7 </b>to be an effective probe for the labeling of a purified gut microbial sialidase (BDI_2946) and a purified human sialic acid binding protein (hCD33). Additionally, LC-MS/MS affinity-based protein profiling verified the ability of <b>7</b>to enrich a low-abundance sialic acid binding protein (complement factor H) from human serum thus validating the utility of this probe in a complex context.</p>

A Glycal-Based Photoaffinity Probe That Enriches Sialic Acid Binding Proteins

<p>To identify sialic acid binding proteins from complex proteomes, three photocrosslinking affinity-based probes were constructed using Neu5Ac (<b>5 </b>and <b>6</b>) and Neu5Ac2en (<b>7</b>) scaffolds. Kinetic inhibition assays and Western blotting revealed the Neu5Ac2en-based <b>7 </b>to be an effective probe for the labeling of a purified gut microbial sialidase (BDI_2946) and a purified human sialic acid binding protein (hCD33). Additionally, LC-MS/MS affinity-based protein profiling verified the ability of <b>7</b>to enrich a low-abundance sialic acid binding protein (complement factor H) from human serum thus validating the utility of this probe in a complex context.</p>

On the move: Redox –dependent protein relocation

ABSTRACTCompartmentation of proteins and processes is a defining feature of eukaryotic cells. The growth and development of organisms is critically dependent on the accurate sorting of proteins within cells. The mechanisms by which cytosol-synthesized proteins are delivered to the membranes and membrane compartments have been extensively characterised. However, the protein complement of any given compartment is not precisely fixed and some proteins can move between compartments in response to metabolic or environmental triggers. The mechanisms and processes that mediate such relocation events are largely uncharacterized. Many proteins can in addition perform multiple functions, catalyzing alternative reactions or performing structural, non-enzymatic functions. These alternative functions can be equally important functions in each cellular compartment. Such proteins are generally not dual targeted proteins in the classic sense of having targeting sequences that directde novosynthesised proteins to specific cellular locations. Accumulating evidence suggests that redox post-translational modifications (PTMs) can control the compartmentation of many such proteins, including antioxidant and/or redox associated enzymes.