The Experts below are selected from a list of 231 Experts worldwide ranked by ideXlab platform
Shaun Heaphy - One of the best experts on this subject based on the ideXlab platform.
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A study of the dimerization of Rous sarcoma virus RNA in vitro and in vivo.
Virology, 1995Co-Authors: Andrew L. Lear, Malcolm Haddrick, Shaun HeaphyAbstract:Abstract The Rous sarcoma virus dimer linkage site (DLS) has been located by electron microscopy at position 511 ± 28 nucleotides. We have studied the dimerization of RNAs encompassing the first 634 nucleotides of Rous sarcoma virus and conclude that there are at least two dimerization signals. One is located between nucleotides 531 and 634 and may involve Watson-Crick pairing of an imperfect inverted repeat. The other signal is located between nucleotides 496 and 530. A tetraguanine sequence at nucleotides 523-526 is required for dimerization of this domain. The guanines are not involved in an identifiable Watson-Crick interaction or in guanine tetrad formation. Either dimerization domain can initiate the dimerization of RNA 1-634. It is possible that these domains are two parts of a single dimerization signal. Interstrand RNA contacts within the virion are not limited to the DLS but occur along the length of the genome. Nascent virions contain monomeric RNA which slowly associates to form an RNA dimer. The limiting step in dimerization is not proteolytic cleavage of the gag precursor because only the mature capsid Protein P27 can be detected in these nascent virions.
Andrew L. Lear - One of the best experts on this subject based on the ideXlab platform.
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A study of the dimerization of Rous sarcoma virus RNA in vitro and in vivo.
Virology, 1995Co-Authors: Andrew L. Lear, Malcolm Haddrick, Shaun HeaphyAbstract:Abstract The Rous sarcoma virus dimer linkage site (DLS) has been located by electron microscopy at position 511 ± 28 nucleotides. We have studied the dimerization of RNAs encompassing the first 634 nucleotides of Rous sarcoma virus and conclude that there are at least two dimerization signals. One is located between nucleotides 531 and 634 and may involve Watson-Crick pairing of an imperfect inverted repeat. The other signal is located between nucleotides 496 and 530. A tetraguanine sequence at nucleotides 523-526 is required for dimerization of this domain. The guanines are not involved in an identifiable Watson-Crick interaction or in guanine tetrad formation. Either dimerization domain can initiate the dimerization of RNA 1-634. It is possible that these domains are two parts of a single dimerization signal. Interstrand RNA contacts within the virion are not limited to the DLS but occur along the length of the genome. Nascent virions contain monomeric RNA which slowly associates to form an RNA dimer. The limiting step in dimerization is not proteolytic cleavage of the gag precursor because only the mature capsid Protein P27 can be detected in these nascent virions.
Myron Essex - One of the best experts on this subject based on the ideXlab platform.
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Vpx of simian immunodeficiency virus is localized primarily outside the virus core in mature virions.
Journal of Virology, 1993Co-Authors: Xiao Fang Yu, Zene Matsuda, Qian-chun Yu, Myron EssexAbstract:Human immunodeficiency virus type 2 and the related simian immunodeficiency virus (SIV) contain a unique regulatory gene, vpx. The Vpx Protein is packaged in mature virions and is required for efficient viral replication in peripheral blood lymphocytes and macrophages. To study the localization of Vpx in mature virions, conical and bar-shaped core structures of SIV from macaques (SIVmac) were purified. The SIVmac core has a density of approximately 1.25 g/cm3, compared with 1.16 g/cm3 for an intact virion. The relative proportions of major capsid Protein (P27) and reverse transcriptase activity were similar for intact virions and core structures. The majority of matrix Protein (p14) was removed from the purified core structure, suggesting its association with the viral membrane. Similarly, most of the Vpx Protein was absent from the purified core structure. This result suggests that as with the matrix Protein, the majority of Vpx Proteins are localized outside the virus core. The localization of Vpx suggests that it may be involved in virus entry such as penetration or uncoating.
Malcolm Haddrick - One of the best experts on this subject based on the ideXlab platform.
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A study of the dimerization of Rous sarcoma virus RNA in vitro and in vivo.
Virology, 1995Co-Authors: Andrew L. Lear, Malcolm Haddrick, Shaun HeaphyAbstract:Abstract The Rous sarcoma virus dimer linkage site (DLS) has been located by electron microscopy at position 511 ± 28 nucleotides. We have studied the dimerization of RNAs encompassing the first 634 nucleotides of Rous sarcoma virus and conclude that there are at least two dimerization signals. One is located between nucleotides 531 and 634 and may involve Watson-Crick pairing of an imperfect inverted repeat. The other signal is located between nucleotides 496 and 530. A tetraguanine sequence at nucleotides 523-526 is required for dimerization of this domain. The guanines are not involved in an identifiable Watson-Crick interaction or in guanine tetrad formation. Either dimerization domain can initiate the dimerization of RNA 1-634. It is possible that these domains are two parts of a single dimerization signal. Interstrand RNA contacts within the virion are not limited to the DLS but occur along the length of the genome. Nascent virions contain monomeric RNA which slowly associates to form an RNA dimer. The limiting step in dimerization is not proteolytic cleavage of the gag precursor because only the mature capsid Protein P27 can be detected in these nascent virions.
Xiao Fang Yu - One of the best experts on this subject based on the ideXlab platform.
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Vpx of simian immunodeficiency virus is localized primarily outside the virus core in mature virions.
Journal of Virology, 1993Co-Authors: Xiao Fang Yu, Zene Matsuda, Qian-chun Yu, Myron EssexAbstract:Human immunodeficiency virus type 2 and the related simian immunodeficiency virus (SIV) contain a unique regulatory gene, vpx. The Vpx Protein is packaged in mature virions and is required for efficient viral replication in peripheral blood lymphocytes and macrophages. To study the localization of Vpx in mature virions, conical and bar-shaped core structures of SIV from macaques (SIVmac) were purified. The SIVmac core has a density of approximately 1.25 g/cm3, compared with 1.16 g/cm3 for an intact virion. The relative proportions of major capsid Protein (P27) and reverse transcriptase activity were similar for intact virions and core structures. The majority of matrix Protein (p14) was removed from the purified core structure, suggesting its association with the viral membrane. Similarly, most of the Vpx Protein was absent from the purified core structure. This result suggests that as with the matrix Protein, the majority of Vpx Proteins are localized outside the virus core. The localization of Vpx suggests that it may be involved in virus entry such as penetration or uncoating.
