Готові списки джерел за темами / HIV; capsid; core stability

Добірка наукової літератури з теми "HIV; capsid; core stability"

Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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Статті в журналах з теми "HIV; capsid; core stability"

1

Guedán, Anabel, Callum D. Donaldson, Eve R. Caroe, Ophélie Cosnefroy, Ian A. Taylor, and Kate N. Bishop. "HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration." PLOS Pathogens 17, no. 9 (September 20, 2021): e1009484. http://dx.doi.org/10.1371/journal.ppat.1009484.

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Анотація:
The capsid (CA) lattice of the HIV-1 core plays a key role during infection. From the moment the core is released into the cytoplasm, it interacts with a range of cellular factors that, ultimately, direct the pre-integration complex to the integration site. For integration to occur, the CA lattice must disassemble. Early uncoating or a failure to do so has detrimental effects on virus infectivity, indicating that an optimal stability of the viral core is crucial for infection. Here, we introduced cysteine residues into HIV-1 CA in order to induce disulphide bond formation and engineer hyper-stable mutants that are slower or unable to uncoat, and then followed their replication. From a panel of mutants, we identified three with increased capsid stability in cells and found that, whilst the M68C/E212C mutant had a 5-fold reduction in reverse transcription, two mutants, A14C/E45C and E180C, were able to reverse transcribe to approximately WT levels in cycling cells. Moreover, these mutants only had a 5-fold reduction in 2-LTR circle production, suggesting that not only could reverse transcription complete in hyper-stable cores, but that the nascent viral cDNA could enter the nuclear compartment. Furthermore, we observed A14C/E45C mutant capsid in nuclear and chromatin-associated fractions implying that the hyper-stable cores themselves entered the nucleus. Immunofluorescence studies revealed that although the A14C/E45C mutant capsid reached the nuclear pore with the same kinetics as wild type capsid, it was then retained at the pore in association with Nup153. Crucially, infection with the hyper-stable mutants did not promote CPSF6 re-localisation to nuclear speckles, despite the mutant capsids being competent for CPSF6 binding. These observations suggest that hyper-stable cores are not able to uncoat, or remodel, enough to pass through or dissociate from the nuclear pore and integrate successfully. This, is turn, highlights the importance of capsid lattice flexibility for nuclear entry. In conclusion, we hypothesise that during a productive infection, a capsid remodelling step takes place at the nuclear pore that releases the core complex from Nup153, and relays it to CPSF6, which then localises it to chromatin ready for integration.
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2

Forshey, Brett M., Uta von Schwedler, Wesley I. Sundquist, and Christopher Aiken. "Formation of a Human Immunodeficiency Virus Type 1 Core of Optimal Stability Is Crucial for Viral Replication." Journal of Virology 76, no. 11 (June 1, 2002): 5667–77. http://dx.doi.org/10.1128/jvi.76.11.5667-5677.2002.

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Анотація:
ABSTRACT Virions of human immunodeficiency virus type 1 (HIV-1) and other lentiviruses contain conical cores consisting of a protein shell composed of the viral capsid protein (CA) surrounding an internal viral ribonucleoprotein complex. Although genetic studies have implicated CA in both early and late stages of the virus replication cycle, the mechanism of core disassembly following penetration of target cells remains undefined. Using quantitative assays for analyzing HIV-1 core stability in vitro, we identified point mutations in CA that either reduce or increase the stability of the HIV-1 core without impairing conical core formation in virions. Alterations in core stability resulted in severely attenuated HIV-1 replication and impaired reverse transcription in target cells with only minimal effects on viral DNA synthesis in permeabilized virions in vitro. We conclude that formation of a viral core of optimal stability is a prerequisite for efficient HIV-1 infection and suggest that disassembly of the HIV-1 core is a regulated step in infection that may be an attractive target for pharmacologic intervention.
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3

Schommers, P., G. Martrus, U. Matschl, M. Sirignano, M. Lütgehetmann, L. Richert, T. J. Hope, G. Fätkenheuer, and M. Altfeld. "Changes in HIV-1 Capsid Stability Induced by Common Cytotoxic-T-Lymphocyte-Driven Viral Sequence Mutations." Journal of Virology 90, no. 16 (June 8, 2016): 7579–86. http://dx.doi.org/10.1128/jvi.00867-16.

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ABSTRACTHIV-1-infected individuals with protective HLA class I alleles exhibit better control of viremia and slower disease progression. Virus control in these individuals has been associated with strong and potent HIV-1-specific cytotoxic-T-lymphocyte (CTL) responses restricted by protective HLA alleles, but control of viremia also occurs in the presence of selected CTL escape mutations. CTL escape mutations restricted by protective HLA class I molecules are frequently located in the conserved p24 Gag sequence of HIV-1 that encodes the conical capsid core and have been suggested to reduce viral replication capacity. In this study, the consequences of well-described CTL-associated p24 Gag sequence mutations for HIV-1 capsid stability were assessed using a cyclosporine (CsA) washout assay. The frequently occurring HLA-B57- and HLA-B27-associated CTL escape mutations T242N and R264K resulted in delayed capsid uncoating, suggesting modulation of capsid stability. The described compensatory mutations L268M and S173A observed in R264K viruses reconstituted the capsid-uncoating half-time. Interestingly, capsid stability was correlated with infectivity. Taken together, these data demonstrate that CTL-driven escape mutations within p24 Gag restricted by protective HLA class I alleles have a significant impact on capsid stability that might contribute to the persistent control of viral replication observed despite viral escape from CTL responses.IMPORTANCESequence mutations within p24 Gag selected by CTL responses restricted by protective HLA class I alleles have been associated with reduced viral fitness. However, the precise mechanisms underlying the reduced viral replication capacity and lower viral loads associated with these mutations remain unclear. Here, we demonstrate that dominant HLA-B27-associated CTL escape mutations within HIV-1 capsid lead to enhanced capsid rigidity, providing a possible mechanism for the reduced viral fitness of these variants.
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4

Newman, Margaret, Pong Kian Chua, Fan-Mei Tang, Pei-Yi Su, and Chiaho Shih. "Testing an Electrostatic Interaction Hypothesis of Hepatitis B Virus Capsid Stability by Using an In Vitro Capsid Disassembly/Reassembly System." Journal of Virology 83, no. 20 (August 5, 2009): 10616–26. http://dx.doi.org/10.1128/jvi.00749-09.

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ABSTRACT To test a previously coined “charge balance hypothesis” of human hepatitis B virus (HBV) capsid stability, we established an in vitro disassembly and reassembly system using bacterially expressed HBV capsids. Capsid disassembly can be induced by micrococcal nuclease digestion of encapsidated RNA. HBV core protein (HBc) mutants containing various amounts of arginine were constructed by serial truncations at the C terminus. Capsids containing smaller amounts of arginine (HBc 149, 154, and 157) remained intact after micrococcal nuclease digestion by native gel electrophoresis. Capsids containing larger amounts of arginine (HBc 159, 164, 169, and 171) exhibited reduced and more diffuse banding intensity and slightly upshifted mobility (HBc 159 and 164). Capsids containing the largest amounts of arginine (HBc 173, 175, and 183), as well as HBc 167, exhibited no detectable banding signal, indicating loss of capsid integrity or stability. Interestingly, capsid reassembly can be induced by polyanions, including oligonucleotides, poly-glutamic acid, and nonbiological polymer (polyacrylic acid). In contrast, polycations (polylysine and polyethylenimine) and low-molecular-weight anions (inositol triphosphate) induced no capsid reassembly. Results obtained by gel assay were confirmed by electron microscopy. Reassembled capsids comigrated with undigested parental capsids on agarose gels and cosedimented with undigested capsids by sucrose gradient ultracentrifugation. Taken together, the results indicate that HBV capsid assembly and integrity depend on polyanions, which probably can help minimize intersubunit charge repulsion caused mainly by arginine-rich domain III or IV in close contact. The exact structure of polyanions is not important for in vitro capsid reassembly. A large amount of independent experimental evidence for this newly coined “electrostatic interaction hypothesis” is discussed.
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5

Forshey, Brett M., and Christopher Aiken. "Disassembly of Human Immunodeficiency Virus Type 1 Cores In Vitro Reveals Association of Nef with the Subviral Ribonucleoprotein Complex." Journal of Virology 77, no. 7 (April 1, 2003): 4409–14. http://dx.doi.org/10.1128/jvi.77.7.4409-4414.2003.

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ABSTRACT The human immunodeficiency virus type 1 (HIV-1) virulence factor Nef enhances viral infectivity in single-cycle infection assays and accelerates HIV-1 replication in vitro. It has been reported that the effects of Nef are mediated early after viral entry and before the completion of reverse transcription, as viral DNA synthesis is strongly attenuated during infection by Nef-defective virions. Our previous work has demonstrated that Nef is associated with mature HIV-1 cores, implicating Nef in the regulation of HIV-1 core stability. Here we report a comparative analysis of HIV-1 cores isolated from wild-type and Nef-defective particles. We observed no effect of Nef on HIV-1 core structure or stability; however, Nef cosedimented with a subviral ribonucleoprotein complex following dissociation of CA. These results indicate that Nef interacts tightly with an internal component of the HIV-1 core. They further suggest that virion-associated Nef may facilitate an early step in HIV-1 infection following dissociation of the viral capsid in the target cell.
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6

Newman, Margaret, Fat-Moon Suk, Maria Cajimat, Pong Kian Chua, and Chiaho Shih. "Stability and Morphology Comparisons of Self-AssembledVirus-Like Particles from Wild-Type and Mutant Human Hepatitis B VirusCapsidProteins." Journal of Virology 77, no. 24 (December 15, 2003): 12950–60. http://dx.doi.org/10.1128/jvi.77.24.12950-12960.2003.

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ABSTRACT Instead of displaying the wild-type selective export of virions containing mature genomes, human hepatitis B virus (HBV) mutant I97L, changing from an isoleucine to a leucine at amino acid 97 of HBV core antigen (HBcAg), lost the high stringency of selectivity in genome maturity during virion export. To understand the structural basis of this so-called “immature secretion” phenomenon, we compared the stability and morphology of self-assembled capsid particles from the wild-type and mutant I97L HBV, in either full-length (HBcAg1-183) or truncated core protein contexts (HBcAg1-149 and HBcAg1-140). Using negative staining and electron microscopy, full-length particles appear as “thick-walled” spherical particles with little interior space, whereas truncated particles appear as“ thin-walled” spherical particles with a much larger inner space. We found no significant differences in capsid stability between wild-type and mutant I97L particles under denaturing pH and temperature in either full-length or truncated core protein contexts. In general, HBV capsid particles (HBcAg1-183, HBcAg1-149, and HBcAg1-140) are very robust but will dissociate at pH 2 or 14, at temperatures higher than 75°C, or in 0.1% sodium dodecyl sulfate (SDS). An unexpected upshift banding pattern of the SDS-treated full-length particles during agarose gel electrophoresis is most likely caused by disulfide bonding of the last cysteine of HBcAg. HBV capsids are known to exist in natural infection as dimorphic T=3 or T=4 icosahedral particles. No difference in the ratio between T=3 (78%) and T=4 particles (20.3%) are found between wild-type HBV and mutant I97L in the context of HBcAg1-140. In addition, we found no difference in capsid stability between T=3 and T=4 particles successfully separated by using a novel agarose gel electrophoresis procedure.
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7

Kang, Hang, Jaehoon Yu, and Guhung Jung. "Phosphorylation of hepatitis B virus core C-terminally truncated protein (Cp149) by PKC increases capsid assembly and stability." Biochemical Journal 416, no. 1 (October 28, 2008): 47–54. http://dx.doi.org/10.1042/bj20080724.

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The HBV (hepatitis B virus) core is a phosphoprotein whose assembly, replication, encapsidation and localization are regulated by phosphorylation. It is known that PKC (protein kinase C) regulates pgRNA (pregenomic RNA) encapsidation by phosphorylation of the C-terminus of core, which is a component packaged into capsid. Neither the N-terminal residue phosphorylated by PKC nor the role of the C-terminal phosphorylation have been cleary defined. In the present study we found that HBV Cp149 (core protein C-terminally truncated at amino acid 149) expressed in Escherichia coli was phosphorylated by PKC at Ser106. PKC-mediated phosphorylation increased core affinity, as well as assembly and capsid stability. In vitro phosphorylation with core mutants (S26A, T70A, S106A and T114A) revealed that the Ser106 mutation inhibited phosphorylation of core by PKC. CD analysis also revealed that PKC-mediated phosphorylation stabilized the secondary structure of capsid. When either pCMV/FLAG-Cp149[WT (wild-type)] or pCMV/FLAG-S106A Cp149 was transfected into Huh7 human hepatoma cells, mutant capsid level was decreased by 2.06-fold with the S106A mutant when compared with WT, although the same level of total protein was expressed in both cases. In addition, when pUC1.2x and pUC1.2x/S106A were transfected, mutant virus titre was decreased 2.31-fold compared with WT virus titre. In conclusion, PKC-mediated phosphorylation increased capsid assembly, stability and structural stability.
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8

Leschonsky, Bernd, Christine Ludwig, Kurt Bieler, and Ralf Wagner. "Capsid stability and replication of human immunodeficiency virus type 1 are influenced critically by charge and size of Gag residue 183." Journal of General Virology 88, no. 1 (January 1, 2007): 207–16. http://dx.doi.org/10.1099/vir.0.81894-0.

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Structural data support a model where – following proteolytic cleavage – the amino-terminal domain of human immunodeficiency virus type 1 (HIV-1) capsid protein refolds into a β-hairpin/helix tertiary structure that is stabilized by a buried salt bridge forming between the positively charged primary imino group of a proline residue and the negatively charged carboxyl group of a conserved aspartate. In order to evaluate the contribution of either side-chain length or charge to the formation of infectious virus capsids, aspartate 183 was substituted for glutamate or asparagine in the viral context. It was found that both modifications abolished infectivity of the corresponding viruses in permissive T lymphocytes, although none of particle assembly and release, RNA encapsidation, incorporation of Env glycoproteins and packaging of cyclophilin A were impaired. However, whereas biophysical analyses of mutant virions yielded wild-type-like particle sizes and densities, electron microscopy revealed aberrant core morphologies that could be attributed to either increased (D183N) or reduced (D183E) capsid stability. Although the two amino acid substitutions had opposing effects upon core stability, both mutants were shown to exhibit a severe block in early reverse transcription, underscoring the importance of correct salt-bridge formation for early steps of virus replication.
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9

Briones, Marisa S., Charles W. Dobard, and Samson A. Chow. "Role of Human Immunodeficiency Virus Type 1 Integrase in Uncoating of the Viral Core." Journal of Virology 84, no. 10 (March 10, 2010): 5181–90. http://dx.doi.org/10.1128/jvi.02382-09.

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ABSTRACT After membrane fusion with a target cell, the core of human immunodeficiency virus type 1 (HIV-1) enters into the cytoplasm, where uncoating occurs. The cone-shaped core is composed of the viral capsid protein (CA), which disassembles during uncoating. The underlying factors and mechanisms governing uncoating are poorly understood. Several CA mutations can cause changes in core stability and a block at reverse transcription, demonstrating the requirement for optimal core stability during viral replication. HIV-1 integrase (IN) catalyzes the insertion of the viral cDNA into the host genome, and certain IN mutations are pleiotropic. Similar to some CA mutants, two IN mutants, one with a complete deletion of IN (NL-ΔIN) and the other with a Cys-to-Ser substitution (NL-C130S), were noninfectious, with a replication block at reverse transcription. Compared to the wild type (WT), the cytoplasmic CA levels of the IN mutants in infected cells were reduced, suggesting accelerated uncoating. The role of IN during uncoating was examined by isolating and characterizing cores from NL-ΔIN and NL-C130S. Both IN mutants could form functional cores, but the core yield and stability were decreased. Also, virion incorporation of cyclophilin A (CypA), a cellular peptidyl-prolyl isomerase that binds specifically to CA, was decreased in the IN mutants. Cores isolated from WT virus depleted of CypA had an unstable-core phenotype, confirming a role of CypA in promoting optimal core stability. Taken together, our results indicate that IN is required during uncoating for maintaining CypA-CA interaction, which promotes optimal stability of the viral core.
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10

Welker, Reinhold, Heinrich Hohenberg, Uwe Tessmer, Carola Huckhagel, and Hans-Georg Kräusslich. "Biochemical and Structural Analysis of Isolated Mature Cores of Human Immunodeficiency Virus Type 1." Journal of Virology 74, no. 3 (February 1, 2000): 1168–77. http://dx.doi.org/10.1128/jvi.74.3.1168-1177.2000.

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ABSTRACT Mature human immunodeficiency virus type 1 (HIV-1) particles contain a cone-shaped core structure consisting of the internal ribonucleoprotein complex encased in a proteinaceous shell derived from the viral capsid protein. Because of their very low stability after membrane removal, HIV-1 cores have not been purified in quantities sufficient for structural and biochemical analysis. Based on our in vitro assembly experiments, we have developed a novel method for isolation of intact mature HIV-1 cores. Concentrated virus suspensions were briefly treated with nonionic detergent and immediately centrifuged in a microcentrifuge for short periods of time. The resuspended pellet was subsequently analyzed by negative-stain and thin-section electron microscopy and by immunoelectron microscopy. Abundant cone-shaped cores as well as tubular and aberrant structures were observed. Stereo images showed that core structures preserved their three-dimensional architecture and exhibited a regular substructure. Detailed analysis of 155 cores revealed an average length of ca. 103 nm, an average diameter at the base of ca. 52 nm, and an average angle of 21.3°. There was significant variability in all parameters, indicating that HIV cores are not homogeneous. Immunoblot analysis of core preparations allowed semiquantitative estimation of the relative amounts of viral and cellular proteins inside the HIV-1 core, yielding a model for the topology of various proteins inside the virion.
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Більше джерел

Дисертації з теми "HIV; capsid; core stability"

1

Abdurahman, Samir. "Studies on HIV-1 core assembly /." Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-363-4/.

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2

Donaldson, Callum. "Investigating the relationship between core stability and early life cycle events in HIV-1." Thesis, University College London (University of London), 2018. http://discovery.ucl.ac.uk/10053748/.

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HIV-1 capsid (CA) plays a vital role in the early stages of HIV-1 infection. The CA lattice surrounding the viral core is predominantly assembled from CA hexamers and stabilised by intra-hexamer and inter-hexamer interactions. Optimal stability of the lattice is known to be critical for efficient infection; however, a comprehensive screen of the effects of stabilising all lattice interfaces has not been performed. Disulphide cross-linking of residues across lattice interfaces has been used in vitro to stabilise CA assemblies. In this study, putatively stabilising cysteine CA mutations were designed at each interface of the CA lattice and their effects on early life cycle events, including reverse transcription and nuclear entry, assessed. The introduction of cysteine mutations at intra-hexamer (both NTD-NTD and NTD-CTD) and inter-hexamer (dimeric CTD-CTD only) lattice interfaces resulted in cross-linking and hyperstable viral cores in infected cells. These cores were minimally infectious and encountered sequential blocks to infectivity at reverse transcription, nuclear entry and post-nuclear entry. The infectivity defect of hyper-stable core mutant, A14C/E45C, was partially compensated – without an observable decrease in stability – by addition of mutations reported to perturb interactions with CPSF6. In contrast, Nup153 and CypA mutations were unable to compensate the infectivity defect suggesting that this was a CPSF6-specific effect. Proximal ligation assays were performed to visualise and quantify interactions between CA and host factors, indicating that hyper-stable cores encountered a block to nuclear entry in G1/S arrested cells. Overall, the results of this study suggest that mutations at different lattice interfaces can result in global changes to the intrinsic stability of the viral core and results in fitness defects at multiple stages of the HIV-1 early life cycle.
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3

Ford, Christopher Thomas [Verfasser], and Marcus [Akademischer Betreuer] Altfeld. "Consequences of CTL-mediated Immune Pressure for HIV-1 Capsid Stability and Innate Sensing / Christopher Thomas Ford ; Betreuer: Marcus Altfeld." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2019. http://d-nb.info/1198404051/34.

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4

Tan, Aaron Wai Kit [Verfasser], and John [Akademischer Betreuer] Briggs. "Structural insights into HIV-1 capsid assembly, maturation and stability by cryo-electron tomography / Aaron Wai Kit Tan ; Betreuer: John Briggs." Heidelberg : Universitätsbibliothek Heidelberg, 2020. http://d-nb.info/1223308332/34.

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5

Tan, Aaron Wai Kit [Verfasser], and John A. G. [Akademischer Betreuer] Briggs. "Structural insights into HIV-1 capsid assembly, maturation and stability by cryo-electron tomography / Aaron Wai Kit Tan ; Betreuer: John Briggs." Heidelberg : Universitätsbibliothek Heidelberg, 2020. http://nbn-resolving.de/urn:nbn:de:bsz:16-heidok-275271.

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6

Martin, Sarah Mary-Rose Connor. "Studies into the role of capsid serine/threonine residues in HIV core stability and virus replication." Thesis, 2013. http://hdl.handle.net/2440/84126.

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Disassembly of the HIV viral core describes the rearrangement and release of capsid (CA) from the core following entry into the host cell. In this process, while the conical shaped core may be lost, some CA remains associated with the resulting reverse transcription (RTC) and preintegration complexes (PIC). What triggers release of CA from the core is unknown. Cores from virus containing mutations in CA that show altered core stability, and release CA from the core at rates faster or slower than wild type (WT) virus demonstrate blocks in replication during reverse transcription and nuclear translocation. How the CA protein affects theses process is not understood, but intrinsic stability of the core is instrumental in regulating interactions with cellular factors. Evidence suggests that core disassembly is critical for the early steps in HIV replication and it may regulate replication in a cell type dependent fashion. Mutation of charged residues throughout CA results in viruses displaying altered core stability. Regulation of charge in the core, possibly by phosphorylation of CA, is one potential mechanism that may control core disassembly. Substitution of serine residues within CA illustrates five viruses, including three representing the major phospho-acceptor sites (S109, S149 and S178) that show altered replication profiles. To explore the role of these residues in core disassembly, the present study investigated the in vitro stability and the intracellular disassembly of the cores from these viruses. Chapter 3 describes the characterisation of viruses with mutations in CA at S41A, S109A, S146A, S149A, S178A and T188V to analyse the effect of substitution at these sites on viral replication. Substitution at S109, S149, S178 and T188 reduced replication competence and altered the production of reverse transcription intermediates. S41A and S146A demonstrated altered reverse transcription, but did not result in blocks in replication. Chapter 4 describes modification of an assay to examine viral core stability. Using this assay, CA mutant viruses (S109A, S149A and S178A) demonstrated reduced in vitro stability of the viral core in comparison with WT NL4-3 virus. Analysis of core disassembly following cell infection (Chapter 5) could not identify defects in core disassembly inside the cell, but suggested progressive changes occurred to viral complexes following infection. The results in this thesis suggest that substitution in CA at S109, S149 and S178 alters in vitro core stability in these viruses, and may impact on core disassembly during HIV replication.
Thesis (Ph.D.) -- University of Adelaide, School of Molecular and Biomedical Science, 2013
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Книги з теми "HIV; capsid; core stability"

1

Chiu, Simon. The cloning, expression, purification and crystallization of P24, the major core capsid protein of human immunodeficiency virus type (HIV-1). Ottawa: National Library of Canada, 1996.

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Частини книг з теми "HIV; capsid; core stability"

1

Misselwitz, R., G. Hausdorf, K. Welfle, W. E. Höhne, and H. Welfle. "Conformation and Stability of Recombinant HIV-1 Capsid Protein P24 (rp24)." In Spectroscopy of Biological Molecules, 101–2. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0371-8_46.

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Тези доповідей конференцій з теми "HIV; capsid; core stability"

1

Cocklin, Simon, Rama Karadsheh, and Megan Meuser. "Composition and orientation of the core region of novel HIV-1 entry inhibitors influences metabolic stability." In 6th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2020. http://dx.doi.org/10.3390/ecmc2020-07468.

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