Order Tubulavirales
Paul Pumpens, Peter Pushko, Philippe Le Mercier in Virus-Like Particles, 2022
After many important contributions to the classical molecular biology, the Inovirus members have won their remarkable place in history due to the phage display. This technique was elaborated by George P. Smith (1985) when he displayed a collection of peptides on live phage f1 libraries with following selection of one of them that was recognized by the specific antibody. The phage display was awarded with a half of the Nobel Prize in Chemistry 2018 jointly with George P. Smith and Gregory P. Winter “for the phage display of peptides and antibodies,” where the other half was awarded to Frances H. Arnold “for the directed evolution of enzymes.” As commented by the Nobel Committee, Gregory Winter used phage display for the directed evolution of antibodies, with the aim of producing new pharmaceuticals. The first one based on this method, adalimumab, was approved in 2002 and is used for rheumatoid arthritis, psoriasis and inflammatory bowel diseases. Since then, phage display has produced antibodies that can neutralize toxins, counteract autoimmune diseases and cure metastatic cancer.
The development of inovirus-associated vector vaccines using phage-display technologies
Published in Expert Review of Vaccines, 2019
Zachariah Stern, Dora C. Stylianou, Leondios G. Kostrikis
The life cycle of Ff filamentous viruses begins when an adsorption structure on the proximal end of the virus is adsorbed to the tip of the F+ specific pilus of E. coli. Following binding between the virus and the bacterial cell (for a recent review, see [10]), the major coat proteins of the virus become associated with the inner membrane of the cell [24–26]. The virion’s circular single-stranded DNA (cssDNA) is then ejected into the cytoplasm where it is converted to a parental double-stranded replicative form (RF). Using a rolling-circle mechanism, Ff inoviruses replicate their genome. The new virion is assembled through a complex set of interactions that binds the protein subunits to the ssDNA [15–17] and embeds newly synthesized coat proteins into the bacterial membrane [27–29]. ssDNA is passed through the mature coat protein, spanning the bacterial membrane, and additional coat proteins are added on the internal edge of the membrane. Additional proteins are used to package the inovirus and release it into the cell [23,30]. Inovirus assembly on the inner membrane of the bacteria is a harmonized sequential process with both viral-encoded and host proteins playing important roles. For more extensive reviews on inovirus life cycle and replication, see reviews [10,31]. Importantly, this process, which requires both virus and host to complete, does not kill the host, making inovirus replication a sustainable process.
Related Knowledge Centers
- Capsid
- Open Reading Frame
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- F-Plasmid
- Worm-Like Chain
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- Protein Data Bank