Historically, the study of plant viruses has contributed greatly to the elucidation of eukaryotic biology. Recently, concurrent with the development of viruses into expression vectors, the biotechnology industry has developed an increasing number of disease therapies utilizing recombinant proteins. Plant virus vectors are viewed as a viable option for recombinant protein production. Employing pathogens in the process of creating added value to agriculture is, in effect, making an ally from an enemy. This review discusses the development and use of viruses as expression vectors, with special emphasis on (+) strand RNA virus systems. Further, the use of virus expression vectors in large-scale agricultural settings to produce recombinant proteins is described, and the technical challenges that need to be addressed by agriculturists and molecular virologists to fully realize the potential of this latest evolution of plant science are outlined.

Nitrogen fixation activity in the photosynthetic bacterium Rhodospirillum rubrum is controlled by the reversible ADP-ribosylation of the dinitrogenase reductase component of the nitrogenase enzyme complex. This report describes the cloning and characterization of the genes encoding the ADP-ribosyltransferase (draT) and the ADP-ribosylglycohydrolase (draG) involved in this regulation. These genes are shown to be contiguous on the R. rubrum chromosome and highly linked to the nifHDK genes. Sequence analysis revealed the use of TTG as the initiation codon of the draT gene as well as a potential open reading frame immediately downstream of draG. The mono-ADP-ribosylation system in R. rubrum is the first in which both the target protein and modifying enzymes as well as their structural genes have been isolated, making it the model system of choice for analysis of this post-translational regulatory mechanism.

The complete nucleotide sequence of the temperate phage HP1 of Haemophilus influenzae was determined. The phage contains a linear, double-stranded genome of 32 355 nt with cohesive termini. Statistical methods were used to identify 41 probable protein coding segments organized into five plausible transcriptional units. Regions encoding proteins involved in recombination, replication, transcriptional control, host cell lysis and phage production were identified. The sizes of proteins in the mature HP1 particle were determined to assist in identifying genes for structural proteins. Similarities between HP1 coding sequences and those in databases, as well as similar gene organizations and control mechanisms, suggest that HP1 is a member of the P2-like phage family, with strong similarities to coliphages P2 and 186 and some similarity to the retronphage Ec67.

The mechanism for "NH4+ switch-off/on" of nitrogenase activity in Azospirillum brasilense and A. lipoferum was investigated. A [39]) has been well studied in the purple nonsulfur photosynthetic bacterium Rhodospirillum rubrum. In R. rubrum, the loss of cellular nitrogenase activity during switch-off by NH4Cl is correlated with the covalent modification and resulting inactivation of dinitrogenase reductase (13). The covalent modification consists of the ADP-ribosylation of dinitrogenase reductase at . This reaction is catalyzed by dinitrogenase reductase ADP-ribosyltransferase (DRAT) (18,19). Dinitrogenase reductase is composed of two identical subunits, and the ADP-ribosylated subunit migrates more slowly than the unmodified subunit during sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Dinitrogenase reductase-activating glycohydrolase (DRAG) catalyzes the removal of the ADP-ribose group from the inactive dinitrogenase reductase, thereby reactivating the dinitrogenase reductase (20,31,32

In this review, we focus on the potential that tobacco mosaic virus (TMV) has as a carrier for immunogenic epitopes, and the factors that must be considered in order to bring products based on this platform to the market. Large Scale Biology Corporation developed facile and scaleable methods for manufacture of candidate peptide display vaccines based on TMV. We describe how rational design of peptide vaccines can improve the manufacturability of particular TMV products. We also discuss downstream processing and purification of the vaccine products, with particular attention to the metrics that a product must attain in order to meet criteria for regulatory approval as injectable biologics.