Academic literature on the topic 'Minor capsid proteins'
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Journal articles on the topic "Minor capsid proteins"
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Podgorski, Jennifer, Joshua Calabrese, Lauren Alexandrescu, Deborah Jacobs-Sera, Welkin Pope, Graham Hatfull, and Simon White. "Structures of Three Actinobacteriophage Capsids: Roles of Symmetry and Accessory Proteins." Viruses 12, no. 3 (March 8, 2020): 294. http://dx.doi.org/10.3390/v12030294.
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Here, we describe the structure of three actinobacteriophage capsids that infect Mycobacterium smegmatis. The capsid structures were resolved to approximately six angstroms, which allowed confirmation that each bacteriophage uses the HK97-fold to form their capsid. One bacteriophage, Rosebush, may have a novel variation of the HK97-fold. Four novel accessory proteins that form the capsid head along with the major capsid protein were identified. Two of the accessory proteins were minor capsid proteins and showed some homology, based on bioinformatic analysis, to the TW1 bacteriophage. The remaining two accessory proteins are decoration proteins that are located on the outside of the capsid and do not resemble any previously described bacteriophage decoration protein. SDS-PAGE and mass spectrometry was used to identify the accessory proteins and bioinformatic analysis of the accessory proteins suggest they are used in many actinobacteriophage capsids.
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Guan, Zhanwen, Ling Zhong, Chunyan Li, Wenbi Wu, Meijin Yuan, and Kai Yang. "The Autographa californica Multiple Nucleopolyhedrovirusac54Gene Is Crucial for Localization of the Major Capsid Protein VP39 at the Site of Nucleocapsid Assembly." Journal of Virology 90, no. 8 (February 10, 2016): 4115–26. http://dx.doi.org/10.1128/jvi.02885-15.
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ABSTRACTBaculovirus DNAs are synthesized and inserted into preformed capsids to form nucleocapsids at a site in the infected cell nucleus, termed the virogenic stroma. Nucleocapsid assembly ofAutographa californicamultiple nucleopolyhedrovirus (AcMNPV) requires the major capsid protein VP39 and nine minor capsid proteins, including VP1054. However, how VP1054 participates in nucleocapsid assembly remains elusive. In this study, the VP1054-encoding gene (ac54) was deleted to generate theac54-knockout AcMNPV (vAc54KO). In vAc54KO-transfected cells, nucleocapsid assembly was disrupted, leading to the formation of abnormally elongated capsid structures. Interestingly, unlike cells transfected with AcMNPV mutants lacking other minor capsid proteins, in which capsid structures were distributed within the virogenic stroma,ac54ablation resulted in a distinctive location of capsid structures and VP39 at the periphery of the nucleus. The altered distribution pattern of capsid structures was also observed in cells transfected with AcMNPV lacking BV/ODV-C42 or in cytochalasind-treated AcMNPV-infected cells. BV/ODV-C42, along with PP78/83, has been shown to promote nuclear filamentous actin (F-actin) formation, which is another requisite for nucleocapsid assembly. Immunofluorescence using phalloidin indicated that the formation and distribution of nuclear F-actin were not affected byac54deletion. However, immunoelectron microscopy revealed that BV/ODV-C42, PP78/83, and 38K failed to integrate into capsid structures in the absence of VP1054, and immunoprecipitation further demonstrated that in transient expression assays, VP1054 interacted with BV/ODV-C42 and VP80 but not VP39. Our findings suggest that VP1054 plays an important role in the transport of capsid proteins to the nucleocapsid assembly site prior to the process of nucleocapsid assembly.IMPORTANCEBaculoviruses are large DNA viruses whose replication occurs within the host nucleus. The localization of capsids into the capsid assembly site requires virus-induced nuclear F-actin; the inhibition of nuclear F-actin formation results in the retention of capsid structures at the periphery of the nucleus. In this paper, we note that the minor capsid protein VP1054 is essential for the localization of capsid structures, the major capsid protein VP39, and the minor capsid protein 38K into the capsid assembly site. Moreover, VP1054 is crucial for correct targeting of the nuclear F-actin factors BV/ODV-C42 and PP78/83 for capsid maturation. However, the formation and distribution of nuclear F-actin are not affected by the lack of VP1054. We further reveal that VP1054 interacts with BV/ODV-C42 and a capsid transport-related protein, VP80. Taken together, our findings suggest that VP1054 plays a unique role in the pathway(s) for transport of capsid proteins.
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Burkert, Oliver, Susanne Kreßner, Ludwig Sinn, Sven Giese, Claudia Simon, and Hauke Lilie. "Biophysical characterization of polyomavirus minor capsid proteins." Biological Chemistry 395, no. 7-8 (July 1, 2014): 871–80. http://dx.doi.org/10.1515/hsz-2014-0114.
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Abstract The murine polyomavirus encodes three structural proteins, VP1, VP2 and VP3, which together form the viral capsid. The outer shell of this capsid is composed of the major capsid protein VP1, the inner shell consists of VP2 and its N-terminally truncated form VP3. These two minor capsid proteins interact with their identical C-terminal part in the central cavity of VP1 pentamers, building the capsid assembly unit. While the VP1 structure and functions are well studied, VP2 and VP3 are poorly understood. In order to get a detailed insight into the structure and function of the minor capsid proteins, they were produced recombinantly in Escherichia coli as inclusion bodies and refolded in vitro. The success of refolding was strictly dependent on the presence of detergent in the refolding buffer. VP2 and VP3 are monomeric and their structures exhibit a high α-helical content. The function of both proteins could be monitored by complex formation with VP1. Furthermore, we could demonstrate a hemolytic activity of VP2/VP3 in vitro, which fits well into a postulated membrane interaction of VP2 during viral infection.
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Vellinga, Jort, Stephanie Van der Heijdt, and Rob C. Hoeben. "The adenovirus capsid: major progress in minor proteins." Journal of General Virology 86, no. 6 (June 1, 2005): 1581–88. http://dx.doi.org/10.1099/vir.0.80877-0.
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Human adenoviruses have been the subject of intensive investigation since their discovery in the early 1950s: they have served as model pathogens, as probes for studying cellular processes and, more recently, as efficient gene-delivery vehicles for experimental gene therapy. As a result, a detailed insight into many aspects of adenovirus biology is now available. The capsid proteins and in particular the hexon, penton-base and fibre proteins (the so-called major capsid proteins) have been studied extensively and their structure and function in the virus capsid are now well-defined. On the other hand, the minor proteins in the viral capsid, i.e. proteins IIIa, VI, VIII and IX, have received much less attention. Only the last few years have witnessed a sharp increase in the number of studies on their structure and function. Here, a review of the minor capsid proteins is provided, with a focus on new insights into their position and role in the capsid and the opportunities that they provide for improving human adenovirus-derived gene-delivery vectors.
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Copeland, Anna Maria, William W. Newcomb, and Jay C. Brown. "Herpes Simplex Virus Replication: Roles of Viral Proteins and Nucleoporins in Capsid-Nucleus Attachment." Journal of Virology 83, no. 4 (December 10, 2008): 1660–68. http://dx.doi.org/10.1128/jvi.01139-08.
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ABSTRACT Replication of herpes simplex virus type 1 (HSV-1) involves a step in which a parental capsid docks onto a host nuclear pore complex (NPC). The viral genome then translocates through the nuclear pore into the nucleoplasm, where it is transcribed and replicated to propagate infection. We investigated the roles of viral and cellular proteins in the process of capsid-nucleus attachment. Vero cells were preloaded with antibodies specific for proteins of interest and infected with HSV-1 containing a green fluorescent protein-labeled capsid, and capsids bound to the nuclear surface were quantified by fluorescence microscopy. Results showed that nuclear capsid attachment was attenuated by antibodies specific for the viral tegument protein VP1/2 (UL36 gene) but not by similar antibodies specific for UL37 (a tegument protein), the major capsid protein (VP5), or VP23 (a minor capsid protein). Similar studies with antibodies specific for nucleoporins demonstrated attenuation by antibodies specific for Nup358 but not Nup214. The role of nucleoporins was further investigated with the use of small interfering RNA (siRNA). Capsid attachment to the nucleus was attenuated in cells treated with siRNA specific for either Nup214 or Nup358 but not TPR. The results are interpreted to suggest that VP1/2 is involved in specific attachment to the NPC and/or in migration of capsids to the nuclear surface. Capsids are suggested to attach to the NPC by way of the complex of Nup358 and Nup214, with high-resolution immunofluorescence studies favoring binding to Nup358.
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Sheaffer, Amy K., William W. Newcomb, Jay C. Brown, Min Gao, Sandra K. Weller, and Daniel J. Tenney. "Evidence for Controlled Incorporation of Herpes Simplex Virus Type 1 UL26 Protease into Capsids." Journal of Virology 74, no. 15 (August 1, 2000): 6838–48. http://dx.doi.org/10.1128/jvi.74.15.6838-6848.2000.
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ABSTRACT Herpes simplex virus type 1 (HSV-1) capsids are initially assembled with an internal protein scaffold. The scaffold proteins, encoded by overlapping in-frame UL26 and UL26.5 transcripts, are essential for formation and efficient maturation of capsids. UL26 encodes an N-terminal protease domain, and its C-terminal oligomerization and capsid protein-binding domains are identical to those of UL26.5. The UL26 protease cleaves itself, releasing minor scaffold proteins VP24 and VP21, and the more abundant UL26.5 protein, releasing the major scaffold protein VP22a. Unlike VP21 and VP22a, which are removed from capsids upon DNA packaging, we demonstrate that VP24 (containing the protease domain) is quantitatively retained. To investigate factors controlling UL26 capsid incorporation and retention, we used a mutant virus that fails to express UL26.5 (ΔICP35 virus). Purified ΔICP35 B capsids showed altered sucrose gradient sedimentation and lacked the dense scaffold core seen in micrographs of wild-type B capsids but contained capsid shell proteins in wild-type amounts. Despite C-terminal sequence identity between UL26 and UL26.5, ΔICP35 capsids lacking UL26.5 products did not contain compensatory high levels of UL26 proteins. Therefore, HSV capsids can be maintained and/or assembled on a minimal scaffold containing only wild-type levels of UL26 proteins. In contrast to UL26.5, increased expression of UL26 did not compensate for the ΔICP35growth defect. While indirect, these findings are consistent with the view that UL26 products are restricted from occupying abundant UL26.5 binding sites within the capsid and that this restriction is not controlled by the level of UL26 protein expression. Additionally, ΔICP35 capsids contained an altered complement of DNA cleavage and packaging proteins, suggesting a previously unrecognized role for the scaffold in this process.
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Wang, Nan, Dongming Zhao, Jialing Wang, Yangling Zhang, Ming Wang, Yan Gao, Fang Li, et al. "Architecture of African swine fever virus and implications for viral assembly." Science 366, no. 6465 (October 17, 2019): 640–44. http://dx.doi.org/10.1126/science.aaz1439.
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African swine fever virus (ASFV) is a giant and complex DNA virus that causes a highly contagious and often lethal swine disease for which no vaccine is available. Using an optimized image reconstruction strategy, we solved the ASFV capsid structure up to 4.1 angstroms, which is built from 17,280 proteins, including one major (p72) and four minor (M1249L, p17, p49, and H240R) capsid proteins organized into pentasymmetrons and trisymmetrons. The atomic structure of the p72 protein informs putative conformational epitopes, distinguishing ASFV from other nucleocytoplasmic large DNA viruses. The minor capsid proteins form a complicated network below the outer capsid shell, stabilizing the capsid by holding adjacent capsomers together. Acting as core organizers, 100-nanometer-long M1249L proteins run along each edge of the trisymmetrons that bridge two neighboring pentasymmetrons and form extensive intermolecular networks with other capsid proteins, driving the formation of the capsid framework. These structural details unveil the basis of capsid stability and assembly, opening up new avenues for African swine fever vaccine development.
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Gasparovic, M. L., G. V. Gee, and W. J. Atwood. "JC Virus Minor Capsid Proteins Vp2 and Vp3 Are Essential for Virus Propagation." Journal of Virology 80, no. 21 (November 1, 2006): 10858–61. http://dx.doi.org/10.1128/jvi.01298-06.
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ABSTRACT Virus-encoded capsid proteins play a major role in the life cycles of all viruses. The JC virus capsid is composed of 72 pentamers of the major capsid protein Vp1, with one of the minor coat proteins Vp2 or Vp3 in the center of each pentamer. Vp3 is identical to two-thirds of Vp2, and these proteins share a DNA binding domain, a nuclear localization signal, and a Vp1-interacting domain. We demonstrate here that both the minor proteins and the myristylation site on Vp2 are essential for the viral life cycle, including the proper packaging of its genome.
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Wills, Elizabeth, Luella Scholtes, and Joel D. Baines. "Herpes Simplex Virus 1 DNA Packaging Proteins Encoded by UL6, UL15, UL17, UL28, and UL33 Are Located on the External Surface of the Viral Capsid." Journal of Virology 80, no. 21 (August 18, 2006): 10894–99. http://dx.doi.org/10.1128/jvi.01364-06.
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ABSTRACT Studies to localize the herpes simplex virus 1 portal protein encoded by UL6, the putative terminase components encoded by UL15, UL 28, and UL33, the minor capsid proteins encoded by UL17, and the major scaffold protein ICP35 were conducted. ICP35 in B capsids was more resistant to trypsin digestion of intact capsids than pUL6, pUL15, pUL17, pUL28, or pUL33. ICP35 required sectioning of otherwise intact embedded capsids for immunoreactivity, whereas embedding and/or sectioning decreased the immunoreactivities of pUL6, pUL17, pUL28, and pUL33. Epitopes of pUL15 were recognized roughly equally well in both sectioned and unsectioned capsids. These data indicate that pUL6, pUL17, pUL28, pUL33, and at least some portion of pUL15 are located at the external surface of the capsid.
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Pawlowski, Alice, Anni M. Moilanen, Ilona A. Rissanen, Juha A. E. Määttä, Vesa P. Hytönen, Janne A. Ihalainen, and Jaana K. H. Bamford. "The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions." Journal of Virology 89, no. 15 (May 13, 2015): 7593–603. http://dx.doi.org/10.1128/jvi.00262-15.
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ABSTRACTThermus thermophilusbacteriophage P23-77 is the type member of a new virus family of icosahedral, tailless, inner-membrane-containing double-stranded DNA (dsDNA) viruses infecting thermophilic bacteria and halophilic archaea. The viruses have a unique capsid architecture consisting of two major capsid proteins assembled in various building blocks. We analyzed the function of the minor capsid protein VP11, which is the third known capsid component in bacteriophage P23-77. Our findings show that VP11 is a dynamically elongated dimer with a predominantly α-helical secondary structure and high thermal stability. The high proportion of basic amino acids in the protein enables electrostatic interaction with negatively charged molecules, including nucleic acid and large unilamellar lipid vesicles (LUVs). The plausible biological function of VP11 is elucidated by demonstrating the interactions of VP11 withThermus-derived LUVs and with the major capsid proteins by means of the dynamic-light-scattering technique. In particular, the major capsid protein VP17 was able to link VP11-complexed LUVs into larger particles, whereas the other P23-77 major capsid protein, VP16, was unable to link VP11-comlexed LUVs. Our results rule out a previously suggested penton function for VP11. Instead, the electrostatic membrane association of VP11 triggers the binding of the major capsid protein VP17, thus facilitating a controlled incorporation of the two different major protein species into the assembling capsid.IMPORTANCEThe study of thermophilic viruses with inner membranes provides valuable insights into the mechanisms used for stabilization and assembly of protein-lipid systems at high temperatures. Our results reveal a novel way by which an internal membrane and outer capsid shell are linked in a virus that uses two different major protein species for capsid assembly. We show that a positive protein charge is important in order to form electrostatic interactions with the lipid surface, thereby facilitating the incorporation of other capsid proteins on the membrane surface. This implies an alternative function for basic proteins present in the virions of other lipid-containing thermophilic viruses, whose proposed role in genome packaging is based on their capability to bind DNA. The unique minor capsid protein of bacteriophage P23-77 resembles in its characteristics the scaffolding proteins of tailed phages, though it constitutes a substantial part of the mature virion.
Dissertations / Theses on the topic "Minor capsid proteins"
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Bockstall, Katy Elizabeth. "Mutation-function analysis in vivo of the nuclear localization signals of L2 minor capsid proteins of high risk HPV16 and low risk HPV11." Thesis, Boston College, 2008. http://hdl.handle.net/2345/539.
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Thesis advisor: Junona MoroianuDuring the papillomavirus replication cycle, the L2 minor capsid protein enters the nucleus in the initial phase after uncoating of the incoming virions and in the productive phase when L2 together with L1 major capsid protein mediate the encapsidation of the newly replicated viral genome. L2 proteins of both high risk HPV16 L2 and low risk HPV11 L2 have two nuclear localization signals (NLSs): one at the N-terminus (nNLS) and one at the C terminus (cNLS). The purpose of these experiments is to determine the minimal mutations necessary to inhibit the function of the NLSs. In this study, subcellular localization of enhanced green fluorescent protein (EGFP) fusions with full length L2 and L2 mutants lacking either the cNLS (EGFP-L2ΔC), nNLS (EGFP-L2ΔN), or both NLSs (EGFP-L2ΔNΔC) was analyzed in HeLa cell transfection assays. Full length HPV16 L2 and HPV11 L2 proteins localize to the nucleus. For both HPV16 and 11 L2, each NLS could independently mediate nuclear import in vivo. EGFP fusions were also made with mutated nNLS (EGFP-L2ΔCSbN) or mutated cNLS (EGFP-L2ΔNSbC). Transfected HeLa cells were examined by fluorescence microscopy and quantitative studies were done. In both HPV16 and 11 L2 proteins, mutation of basic residues in either NLS inhibited its nuclear import ability
Thesis (BS) — Boston College, 2008
Submitted to: Boston College. College of Arts and Sciences
Discipline: Biology
Discipline: College Honors Program
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Halista, Courtney Ellen. "Characterization of the Nuclear Export Signal of Human Papillomavirus 16 L2 Minor Capsid Protein." Thesis, Boston College, 2011. http://hdl.handle.net/2345/bc-ir:104425.
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Thesis advisor: Junona MoroianuThe L2 minor capsid protein of human papillomavirus is one of two structural proteins that comprise the icosahedral shell. Two potential, leucine-rich nuclear export signals (NESs) had been identified in the HPV16 L2 sequence, one in the n-terminus (51MGVFFGGLGI60) and one in the c-terminus (462LPYFFDSVSL471). DNA primers for mutant L2 proteins were designed to specifically target these two potential NES regions. Two primers had mutations in the n-terminal located NES (nNES), while the other two primers had mutations in the c-terminal NES (cNES). L2 nuclear retention mutants, RR297AA (“MS4”) and RTR313AAA (“MS5”), served as the templates for these NES mutations. Using mutagenesis, the desired secondary mutations were introduced into the mutant L2 genes in order to create four, distinct mutants: RR297AA + P463_ (“MS4 T1”), RR297AA + V469_ (“MS4 T2), RTR313AAA + P463_ (“MS5 T1”), and RTR313AAA + V469_ (“MS5 T2”). In contrast to the pancellular localization of the MS4 and MS5 L2 mutants, the “MS4 T1,” “MS4 T2,” “MS5 T1”, and “MS5 T2” mutants were all localized nuclearly. These results suggest that deletion of the cNES inhibits nuclear export of the HPV16 L2 minor capsid protein
Thesis (BS) — Boston College, 2011
Submitted to: Boston College. College of Arts and Sciences
Discipline: College Honors Program
Discipline: Biology Honors Program
Discipline: Biology
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Odenwald, Caroline [Verfasser], and Martin [Akademischer Betreuer] Müller. "Identification of Cellular Interaction Candidates of Human Papillomavirus Minor Capsid Protein L2 / Caroline Odenwald ; Betreuer: Martin Müller." Heidelberg : Universitätsbibliothek Heidelberg, 2015. http://d-nb.info/1180735374/34.
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Corjon, Stéphanie. "Targeting of adenovirus gene transfer vectors via combined geneti-chemical modification of the minor capsid protein IX." [S.l. : s.n.], 2008. http://nbn-resolving.de/urn:nbn:de:bsz:289-vts-65186.
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Okoye, Afam Amobi. "The effect of the HPV-16 minor capsid protein L2 on the HPV-16 viral transcription regulator E2." Thesis, University of Glasgow, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.407715.
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Li, Shuaizhi. "Cytosolic Glutathione Reducing Potential is Important for Membrane Penetration of HPV16 at the Trans-Golgi Network." Thesis, The University of Arizona, 2016. http://hdl.handle.net/10150/612410.
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High-risk human papillomaviruses (HPVs) cause 5% of all human cancers worldwide. The HPV capsid consists of 72 disulfide-linked pentamers of major capsid protein L1 and up to 72 molecules of minor capsid protein L2. The viral genome (vDNA) is 8KB circular dsDNA, condensed with histones and complexed with L2. HPV infection requires the virion particle to get access to basal layer keratinocytes, binding and entry of the cells, uncoating, and transport of the viral genomes to the host cell nucleus. During infection, L2 is important for transport of the viral genome from membrane bound vesicular compartments, through the cytosol and into the host cell nucleus. Previous work has identified a conserved disulfide bond between Cys22 and Cys28, which is necessary for HPV16 infection. We hypothesize that endosomal reduction of this disulfide might be important for L2 conformational changes that allow a hydrophobic transmembrane-like region in L2 to span across endosomal membranes, exposing sorting adaptor binding motifs within L2 to the cytosol. Prior research suggests that cytosolic glutathione (GSH) redox potential is important for reduction of disulfide-linked proteins within the lumen of endosomes. This is achieved by endosomal influx of cytosolic reduced cysteine, where it can reduce disulfide bonds in lumenal proteins. Cytosolic GSH regenerates the pool of reduced cysteine needed to maintain endosomal redox potential. Here we studied the relationship between cytosolic GSH and HPV16 infection. siRNA knockdown of critical enzymes of the GSH biosynthesis pathway or the endosomal cystine efflux pump cystinosin caused partial abrogation of HPV16 infection. Likewise, inhibition of the GSH biosynthesis pathway with L-buthionine sulfoximine (L-BSO) blocked HPV16 infection in multiple cell types, suggesting that cytosolic GSH redox may be important for HPV16 infection. Further studies have revealed that the decrease of HPV16 infection is not because of defects in binding, entry, L2 cleavage or capsid uncoating, but rather is due to inefficient cytosolic translocation of L2/viral genome from the trans-Golgi network (TGN). Contrary to our initial hypothesis, we show that L2 is able to span the endosomal membrane and direct TGN localization in the presence of BSO. Lack of cytosolic GSH causes L2/viral genome to become trapped in the TGN lumen. This suggests that there are redox-sensitive viral or cellular factors necessary for L2/viral genome translocation at the TGN. Future research will focus on the redox state of the Cys22-Cys28 disulfide bond during infection of normal and GSH-depleted cells.
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Yang, Fan [Verfasser], and Frank [Akademischer Betreuer] Rösl. "Re-engineering a Nanoparticle Human Papillomavirus Prophylactic Vaccine Antigen Based on the Minor Capsid Protein L2 / Fan Yang ; Betreuer: Frank Rösl." Heidelberg : Universitätsbibliothek Heidelberg, 2020. http://d-nb.info/121816798X/34.
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Aydin, Inci, Ruth Villalonga-Planells, Lilo Greune, Matthew P. Bronnimann, Christine M. Calton, Miriam Becker, Kun-Yi Lai, Samuel K. Campos, M. Alexander Schmidt, and Mario Schelhaas. "A central region in the minor capsid protein of papillomaviruses facilitates viral genome tethering and membrane penetration for mitotic nuclear entry." PUBLIC LIBRARY SCIENCE, 2017. http://hdl.handle.net/10150/624633.
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Incoming papillomaviruses (PVs) depend on mitotic nuclear envelope breakdown to gain initial access to the nucleus for viral transcription and replication. In our previous work, we hypothesized that the minor capsid protein L2 of PVs tethers the incoming vDNA to mitotic chromosomes to direct them into the nascent nuclei. To re-evaluate how dynamic L2 recruitment to cellular chromosomes occurs specifically during prometaphase, we developed a quantitative, microscopy-based assay for measuring the degree of chromosome recruitment of L2-EGFP. Analyzing various HPV16 L2 truncation-mutants revealed a central chromosome-binding region (CBR) of 147 amino acids that confers binding to mitotic chromosomes. Specific mutations of conserved motifs (IVAL286AAAA, RR302/5AA, and RTR313EEE) within the CBR interfered with chromosomal binding. Moreover, assembly-competent HPV16 containing the chromosome-binding deficient L2(RTR313EEE) or L2 (IVAL286AAAA) were inhibited for infection despite their ability to be transported to intracellular compartments. Since vDNA and L2 were not associated with mitotic chromosomes either, the infectivity was likely impaired by a defect in tethering of the vDNA to mitotic chromosomes. However, L2 mutations that abrogated chromatin association also compromised translocation of L2 across membranes of intracellular organelles. Thus, chromatin recruitment of L2 may in itself be a requirement for successful penetration of the limiting membrane thereby linking both processes mechanistically. Furthermore, we demonstrate that the association of L2 with mitotic chromosomes is conserved among the alpha, beta, gamma, and iota genera of Papillomaviridae. However, different binding patterns point to a certain variance amongst the different genera. Overall, our data suggest a common strategy among various PVs, in which a central region of L2 mediates tethering of vDNA to mitotic chromosomes during cell division thereby coordinating membrane translocation and delivery to daughter nuclei.
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Bílková, Eva. "Studium vlastností minoritních strukturních proteinů myšího polyomaviru." Master's thesis, 2014. http://www.nusl.cz/ntk/nusl-332400.
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Murine polyomavirus (MPyV) is a member of the Polyomaviridae family. Its capsid is composed of the major capsid protein, VP1, and the minor proteins, VP2 and VP3. The minor capsid proteins probably assure delivery of the viral genome through the endoplasmic reticulum membrane to the nucleus during early phase of infection. However, precise mechanism is not known. Expression plasmids encoding mutated VP2 or VP3 fused with EGFP have been constructed to study the interaction of VP2 and VP3 with membranes. The mutated proteins have deletions in the predicted hydrophobic domains. In this thesis, cell localisation of mutated proteins was followed. The study revealed that the hydrophobic domain 2 is the most important for association of VP2 and VP3 with membranes, while domains 1 and 3 are rather expendable. Further, nature of VP2 and VP3 isoforms has been studied. Isoforms with different electrophoretic mobility were separated on SDS-PAGE. Consequent mass spectrometry analysis showed that they differ in deamidation of asparagine, present at both minor proteins (position 253 of VP2 and 137 of VP3). Previously, acetylation of VP3 N-terminal alanine has been identified. To elucidate the function of these modifications, mutated viruses were constructed with substitution of these amino acids. Pilot...
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Škvára, Petr. "Příprava a charakterizace modifikovaných virových částic odvozených od myšího polyomaviru pro přepravu genů za účelem zvýšení účinnosti transdukce." Master's thesis, 2020. http://www.nusl.cz/ntk/nusl-435892.
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Viral particles derived from mouse polyomavirus can be potentially used as a delivery system for therapeutic genes and drugs into target cells. This thesis focuses on preparation and characterization of polyomaviral particles that are modified with cell-penetrating peptides in order to increase efficiency of transduction of reporter genes into human cells. Viral particles that are composed of major capsid protein VP1 in combination with minor capsid protein VP2 and minor capsid protein VP3 that is modified with octaarginine, LAH4 peptide or with transduction domain of adenoviral protein VI are analysed in transduction assays. The thesis also provides information about the effect of the modification on encapsidation of heterologous DNA. The results of transduction assays performed with modified particles containing encapsidated luciferase gene revealed that efficiency of transduction did not increase but decreased in comparison with unmodified particles. These findings help to elucidate the role of polyomaviral minor capsid proteins in gene transfer mediated by viral particles and contribute to the design of new strategies for modifications of viral particles derived from mouse polyomavirus for their successful application in nanomedicine. Key words: mouse polyomavirus, pseudovirions, virus-like...
Book chapters on the topic "Minor capsid proteins"
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Rani, Manisha, Sushma Rajyalakshmi, Sunitha Pakalapaty, and Nagamani Kammilli. "Norovirus Structure and Classification." In Norovirus. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98216.
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Norovirus are a major cause of acute gastroenteritis worldwide. Diarrheal disease is now the fourth common cause of mortality children under the age of 5 years but remain the 2nd most cause of morbidity. NoV are associated with 18% diarrheal diseases worldwide where rotavirus vaccinations has been successfully introduced. NoV has become major cause of gastroenteritis in children. NoV belong to family caliciviridae. They are non-enveloped, single stranded positive sense RNA Viruses. The genome consists of 3 Open reading frames, ORF-1 codes for non-structural protein, ORF-2 codes for major capsid protein VP1 and ORF-3 for minor capsid protein VP2. Based on sequence difference of the capsid gene (VP1), NoV have been classified in to seven genogroup GI-GVII with over 30 genotypes. Genogroups I, II, IV are associated with human infection. Despite this extensive diversity a single genotype GII.4 has been alone to be the more prevalent. Basic epidemiological disease burden data are generated from developing countries. NoV are considered fast evolving viruses and present an extensive diversity that is driven by acquisition of point mutations and recombinations. Immunity is strain or genotype specific with little or no protection conferred across genogroups. Majority of outbreaks and sporadic norovirus cases worldwide are associated with a single genotype, GII.4 which was responsible for 62% of reported NoV outbreaks in 5 continents from 2001 to 2007. GII.4 variants have been reported as major cause of global gastroenteritis pandemics starting in 1995 frequent emergence of novel GII.4 variants is known to be due to rapid evolution and antigenic variation in response to herd immunity. Novel GII.4 variants appear almost every 2 years. Recent GII.4 variant reported include Lordsdale 1996, Farmington Hills 2002, Hunter 2004, Yerseke 2006a, Den Haag 2006b, Apeldoon 2007, New Orleans 2009,most recently Sydney 2012. Detailed molecular epidemiologic investigation of NoV is associated for understanding the genetic diversity of NoV strain and emergence of novel NoV variants. However, reports have revealed that not all individuals develop symptoms and a significant proportion remains asymptomatic after NoV infections.