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Vectored vaccines
Published in Amine Kamen, Laura Cervera, Bioprocessing of Viral Vaccines, 2023
Zeyu Yang, Kumar Subramaniam, Amine Kamen
The standard VSV particle is a bullet-shaped, single-strand, negative-sense RNA virus with 65 × 180 nm. The viral genome is about 11 kilobases, which encodes five major viral proteins including nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and the viral polymerase (L) [65]. The N protein associates to form viral nucleocapsid for genomic RNA, which serves as functional template for viral replication and transcription. This protein is also the most abundant protein expressed in infected cells. The M protein is the main protein in the VSV particle. The M protein has various functions in infected cells. This protein can regulate the viral transcription, inhibit the gene expression of host cells, and contribute to virus budding. The P and L genomic motifs associate to express the viral RNA polymerase with the functions of transcriptase and replicase. The G protein is a transmembrane glycoprotein on the virus surface with a trimeric spike-like structure. The G protein is responsible for virus attachment to the receptors of host cells.
Virus-Based Nanobiotechnology
Published in Yubing Xie, The Nanobiotechnology Handbook, 2012
Magnus Bergkvist, Brian A. Cohen
It is common to refer to the highly symmetric virus structure as a nucleocapsid, that is, a protein-coated nucleic acid. A fully assembled virus is called a virion, and is composed of nucleic acid, the protein coat in the form of a capsid, which may or may not incorporate other nonstructural proteins and/or a lipid envelope. The nucleic acid contained within the virus can be in the form of single- or double-stranded DNA, or RNA (ssDNA, dsDNA, ssRNA, dsRNA). In the case of ssRNA viruses, the RNA can be positive-sense (+), or negative-sense (−). Positive-sense RNA may be directly translated into protein, whereas negative-sense RNA must first be transcribed into the positive-sense by an RNA polymerase before the translation into protein can occur (Knipe et al. 2007).
Biology of Coronaviruses with Special Reference to SARS-CoV-2
Published in Joystu Dutta, Srijan Goswami, Abhijit Mitra, COVID-19 and Emerging Environmental Trends, 2020
Joystu Dutta, Srijan Goswami, Abhijit Mitra
The protein encoded by nucleocapsid protein gene plays a fundamental role in packaging the positive-strand viral RNA into a structure called helical ribonucleocapsid proteins. It also plays a critical role during virion assembly through its interactions with the viral genome and membrane protein M (Chan et al., 2020). Moreover, the nucleocapsid protein enhances the efficiency of subgenomic viral RNA transcription and viral replication (UniProtKB-59595, 2020).
Critical Review and Research Needs of Ozone Applications Related to Virus Inactivation: Potential Implications for SARS-CoV-2
Published in Ozone: Science & Engineering, 2021
Christina Morrison, Ariel Atkinson, Arash Zamyadi, Faith Kibuye, Michael McKie, Samantha Hogard, Phil Mollica, Saad Jasim, Eric C. Wert
Ozone has received increased attention for use against viruses due to its strong disinfection abilities. In general, viruses consist of a nucleic acid genome (DNA or RNA) coated by a protein comprised nucleocapsid. Some viruses, such as SARS-CoV-2, additionally maintain a viral envelope comprised lipids and proteins from its host cell membrane as its outermost layer. Enveloped viruses have long been assumed to exhibit decreased environmental persistence when compared to non-enveloped viruses, which has resulted in their omission in many environmental-related disinfection studies (Wigginton, Ye, and Ellenberg 2015).
On the Action of Ozone on Phospholipids, a Model Compound of the External Envelope of Pericapsidic Viruses like Coronavirus. Part 1
Published in Ozone: Science & Engineering, 2020
In most viruses, the genetic material (either RNA or DNA) is enclosed inside a proteic coat called capsid. In its turn, the capsid is further enclosed inside a phospholipidic double layer called pericapsid (Backer 2010; Dulbecco and Ginsberg 1990). The gap between capsid and pericapsid is filled by virus-specific proteins and enzymes which play a key role in virus replication. In the coronavirus, the generic material is constituted by a positive-sense-single strand of RNA macromolecule composed by 30 kbases and with a molecular weight of the order of 5.5 × 106 Da, with an infecting cap and polyadenilated tail (Backer 2010; Dulbecco and Ginsberg 1990). The RNA macromolecule is enclosed into the nucleocapsid having helical symmetry. It is important to put in evidence here, that the nucleocapsides of the coated helical viruses are very flexible since it is the entire capsid and not only the nucleic acid that wraps inside the coating. This leads to a loose structure that can leave glimpses of exposed genetic material. In these viruses, it is the pericapsid coating that constitutes a barrier for nucleases and disinfectants (Backer 2010; Dulbecco and Ginsberg 1990). Thus, the destabilization or decomposition of the pericapsid is the key process to inactivate and even destroy a coronavirus (and other viruses with pericapsids) (Dulbecco and Ginsberg 1990; Knight 1975). The purpose of this work is to show that ozone is able to destabilize easily the phospholipids composing the pericapsid, using model phospholipidic compounds. Once the pericapsid is broken, then the coronavirus is inactivated (Dulbecco and Ginsberg 1990; Knight 1975), because we already know that the RNA is extremely sensitive to ozone oxidation (Cataldo 2005, 2006a, 2006b; Theruvathu et al. 2001; Von Sonntag and Von Gunten 2012). Very recently, Young et al. (2020), have shown that RNA human enteroviruses are inactivated by the action of ozone and other agents like UV light and chlorine.