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You searched for subject:(Virus Solubilization). Showing records 1 – 2 of 2 total matches.

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Indian Institute of Science

1. Subhashri, R. Role Of Matrix Protein Of Rinderpest Virus In Viral Morphogenesis.

Degree: 2006, Indian Institute of Science

Rinderpest virus is an enveloped Nonsegmented Negative Stranded RNA Virus (NNSV) belonging to the genus Morbillivirus in the Family Paramyxoviridae and the causative organism for “cattle plague”. The virion has a transport component and a replication component. The transport component consists of a lipid membrane with two external membrane-anchored glycoproteins, namely Hemagglutinin (H) and Fusion (F) proteins that are necessary for cell entry and release of newly formed virus particles. The replication component consists of viral genomic RNA encapsidated by the nucleoprotein (N) and a RNA polymerase complex (Large subunit L and phosphoprotein P). These two components are linked together by the matrix protein (M) that is believed to play a crucial role in the assembly and maturation of the virion particle by bringing the two major viral components together at the budding site in the host cell. To perform this function, M protein should be able to interact with the host cellular membrane, especially the plasma membrane in the case of Rinderpest virus, should be able to interact with itself to form multimers as well as with the nucleocapsid core. The function might include the interaction of M protein with the cytoplasmic tail of the other two envelope proteins namely F and H. To understand the role of matrix protein in Rinderpest virus life cycle, the following functions were characterized – 1) Matrix protein association with the host cell membrane. 2) Matrix protein association with nucleocapsid protein. Matrix protein association cellular membranes in rinderpest virus infected cells could be a result of its interaction with the cytoplasmic tails of the viral glycoproteins. Hence, this association was characterized in the absence of other viral proteins. In transiently transfected cells, M protein existed in two isoforms namely the soluble cytosolic form and membrane-bound form. The membrane-bound M protein associated stably with the membranes, most likely by a combination of electrostatic and hydrophobic interactions, which is inhibited at high salt or high pH, but not completely. Confocal microscopy analysis showed the presence of M protein in plasma membrane protrusions. When GFP was tagged with this protein, GFP was absent from nucleus and was present predominantly in the cytosol and the plasma membrane protrusions. However, M protein expression did not result in the release of membrane vesicles (Virus-like particles) into the culture supernatant implicating the requirement of other viral proteins in envelope acquisition. Matrix protein of RPV has been shown to co-sediment with nucleocapsid during mild preparation of RNP from virus-infected cells. This association was further investigated by virus solubilization. The matrix protein could be solubilised completely from virion only in the presence of detergent and high salt. This is in agreement with the previous observation from the laboratory that the purified matrix protein remained soluble in the presence of detergent and 1M NaCl. This… Advisors/Committee Members: Shaila, M S.

Subjects/Keywords: Glycoproteins; Lipid Membranes; Viral Morphogenesis; Rinderpest Virus; Virus Solubilization; Viral Proteins; Cattle Plague; Matrix Protein; Microbiology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Subhashri, R. (2006). Role Of Matrix Protein Of Rinderpest Virus In Viral Morphogenesis. (Thesis). Indian Institute of Science. Retrieved from http://hdl.handle.net/2005/382

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Subhashri, R. “Role Of Matrix Protein Of Rinderpest Virus In Viral Morphogenesis.” 2006. Thesis, Indian Institute of Science. Accessed July 07, 2020. http://hdl.handle.net/2005/382.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Subhashri, R. “Role Of Matrix Protein Of Rinderpest Virus In Viral Morphogenesis.” 2006. Web. 07 Jul 2020.

Vancouver:

Subhashri R. Role Of Matrix Protein Of Rinderpest Virus In Viral Morphogenesis. [Internet] [Thesis]. Indian Institute of Science; 2006. [cited 2020 Jul 07]. Available from: http://hdl.handle.net/2005/382.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Subhashri R. Role Of Matrix Protein Of Rinderpest Virus In Viral Morphogenesis. [Thesis]. Indian Institute of Science; 2006. Available from: http://hdl.handle.net/2005/382

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Virginia Tech

2. Matanin, Brad Matthew. Purification of the major envelope protein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) from native virions.

Degree: MS, Biological Systems Engineering, 2007, Virginia Tech

Porcine reproductive and respiratory syndrome virus (PRRSV) is the cause of a pandemic that has been devastating the U.S. and global swine industry for more than twenty years. PRRSV vaccine development is challenging due to virus heterogeneity. Evidence indicates that the major envelope protein, GP5, is the primary target for a subunit vaccine. In native virions GP5 primarily exists as a disulfide linked complex with the membrane protein, M, which also possesses immunogenic properties. Recent studies report that the GP5/M complex is a more significant vaccine candidate. Currently, no bulk purification methods have been reported for PRRSV proteins. The objective of this research was to develop a purification process for GP5 or GP5/M from native virions. PRRS virions were isolated and concentrated through sucrose cushion ultracentrifugation and target envelope proteins were solubilized with Triton X-100 detergent for further processing. GP5/M was not consistently identified in samples and was therefore abandoned. GP5 was identified by Western blot throughout processing with a αORF5 antibody. Cation exchange chromatography (CEX) was utilized for partial fractionation of GP5, although the viral nucleocapsid protein, N, was a major impurity in CEX elution fractions. As a second chromatographic step, hydrophobic interaction chromatography (HIC) further purified GP5 by means of a two-stage elution scheme. Pure GP5 was eluted from the HIC resin in the second HIC elution stage by Triton X-100 displacement; however the protein is present as a homodimeric/tetrameric aggregate. This process will be useful in PRRSV vaccine development and the purified GP5 product could be used as much needed positive controls in animal studies. Advisors/Committee Members: Zhang, Chenming Mike (committeechair), Meng, Xiang-Jin (committee member), Mallikarjunan, Parameswarakumar (committee member).

Subjects/Keywords: detergent solubilization; protein purification; GP5; chromatography; PRRSV; virus culture

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Matanin, B. M. (2007). Purification of the major envelope protein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) from native virions. (Masters Thesis). Virginia Tech. Retrieved from http://hdl.handle.net/10919/33194

Chicago Manual of Style (16th Edition):

Matanin, Brad Matthew. “Purification of the major envelope protein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) from native virions.” 2007. Masters Thesis, Virginia Tech. Accessed July 07, 2020. http://hdl.handle.net/10919/33194.

MLA Handbook (7th Edition):

Matanin, Brad Matthew. “Purification of the major envelope protein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) from native virions.” 2007. Web. 07 Jul 2020.

Vancouver:

Matanin BM. Purification of the major envelope protein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) from native virions. [Internet] [Masters thesis]. Virginia Tech; 2007. [cited 2020 Jul 07]. Available from: http://hdl.handle.net/10919/33194.

Council of Science Editors:

Matanin BM. Purification of the major envelope protein GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) from native virions. [Masters Thesis]. Virginia Tech; 2007. Available from: http://hdl.handle.net/10919/33194

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