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Nathaniel R Landau - One of the best experts on this subject based on the ideXlab platform.
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an ace2 Microbody containing a single immunoglobulin fc domain is a potent inhibitor of sars cov 2
Cell Reports, 2020Co-Authors: Takuya Tada, Chen Fan, R Kaur, Kenneth A Stapleford, Harry B Gristick, Crina M Nimigean, Jennifer S Chen, Belinda M Dcosta, Craig B Wilen, Nathaniel R LandauAbstract:Soluble forms of angiotensin-converting enzyme 2 (ACE2) have recently been shown to inhibit severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. We report on an improved soluble ACE2, termed a "Microbody," in which the ACE2 ectodomain is fused to Fc domain 3 of the immunoglobulin (Ig) heavy chain. The protein is smaller than previously described ACE2-Ig Fc fusion proteins and contains an H345A mutation in the ACE2 catalytic active site that inactivates the enzyme without reducing its affinity for the SARS-CoV-2 spike. The disulfide-bonded ACE2 Microbody protein inhibits entry of SARS-CoV-2 spike protein pseudotyped virus and replication of live SARS-CoV-2 in vitro and in a mouse model. Its potency is 10-fold higher than soluble ACE2, and it can act after virus bound to the cell. The Microbody inhibits the entry of s coronaviruses and virus with the variant D614G spike. The ACE2 Microbody may be a valuable therapeutic for coronavirus disease 2019 (COVID-19) that is active against viral variants and future coronaviruses.
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a soluble ace2 Microbody protein fused to a single immunoglobulin fc domain is a potent inhibitor of sars cov 2 infection in cell culture
bioRxiv, 2020Co-Authors: Takuya Tada, Chen Fan, R Kaur, Kenneth A Stapleford, Harry B Gristick, Crina M Nimigean, Nathaniel R LandauAbstract:Soluble forms of ACE2 have recently been shown to inhibit SARS-CoV-2 infection. We report on an improved soluble form of ACE2, termed a "Microbody" in which the ACE2 ectodomain is fused to Fc domain 3 of the immunoglobulin heavy chain. The protein is smaller than previously described ACE2-Ig Fc fusion proteins and contains an H345A mutation in the catalytic active site that inactivates the enzyme without reducing its affinity for the SARS-CoV-2 spike. The disulfide-bonded ACE2 Microbody inhibited entry of SARS-CoV-2 spike protein pseudotyped virus and live SARS-CoV-2 with a potency 10-fold higher than unmodified soluble ACE2 and retained activity even after the virus had bound to the cell. The ACE2 Microbody inhibited entry of ACE2-utilizing β coronaviruses and entry of viruses with the high infectivity variant D614G spike. The ACE2 Microbody may be a valuable therapeutic for COVID-19 that is active against SARS-CoV-2 variants and against coronaviruses that may arise in the future.
Takuya Tada - One of the best experts on this subject based on the ideXlab platform.
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an ace2 Microbody containing a single immunoglobulin fc domain is a potent inhibitor of sars cov 2
Cell Reports, 2020Co-Authors: Takuya Tada, Chen Fan, R Kaur, Kenneth A Stapleford, Harry B Gristick, Crina M Nimigean, Jennifer S Chen, Belinda M Dcosta, Craig B Wilen, Nathaniel R LandauAbstract:Soluble forms of angiotensin-converting enzyme 2 (ACE2) have recently been shown to inhibit severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. We report on an improved soluble ACE2, termed a "Microbody," in which the ACE2 ectodomain is fused to Fc domain 3 of the immunoglobulin (Ig) heavy chain. The protein is smaller than previously described ACE2-Ig Fc fusion proteins and contains an H345A mutation in the ACE2 catalytic active site that inactivates the enzyme without reducing its affinity for the SARS-CoV-2 spike. The disulfide-bonded ACE2 Microbody protein inhibits entry of SARS-CoV-2 spike protein pseudotyped virus and replication of live SARS-CoV-2 in vitro and in a mouse model. Its potency is 10-fold higher than soluble ACE2, and it can act after virus bound to the cell. The Microbody inhibits the entry of s coronaviruses and virus with the variant D614G spike. The ACE2 Microbody may be a valuable therapeutic for coronavirus disease 2019 (COVID-19) that is active against viral variants and future coronaviruses.
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a soluble ace2 Microbody protein fused to a single immunoglobulin fc domain is a potent inhibitor of sars cov 2 infection in cell culture
bioRxiv, 2020Co-Authors: Takuya Tada, Chen Fan, R Kaur, Kenneth A Stapleford, Harry B Gristick, Crina M Nimigean, Nathaniel R LandauAbstract:Soluble forms of ACE2 have recently been shown to inhibit SARS-CoV-2 infection. We report on an improved soluble form of ACE2, termed a "Microbody" in which the ACE2 ectodomain is fused to Fc domain 3 of the immunoglobulin heavy chain. The protein is smaller than previously described ACE2-Ig Fc fusion proteins and contains an H345A mutation in the catalytic active site that inactivates the enzyme without reducing its affinity for the SARS-CoV-2 spike. The disulfide-bonded ACE2 Microbody inhibited entry of SARS-CoV-2 spike protein pseudotyped virus and live SARS-CoV-2 with a potency 10-fold higher than unmodified soluble ACE2 and retained activity even after the virus had bound to the cell. The ACE2 Microbody inhibited entry of ACE2-utilizing β coronaviruses and entry of viruses with the high infectivity variant D614G spike. The ACE2 Microbody may be a valuable therapeutic for COVID-19 that is active against SARS-CoV-2 variants and against coronaviruses that may arise in the future.
Mikio Nishimura - One of the best experts on this subject based on the ideXlab platform.
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Microbody proliferation and segregation cycle in the single-Microbody alga Cyanidioschyzon merolae
Planta, 1999Co-Authors: Shin-ya Miyagishima, Ryuuichi Itoh, Kyoko Toda, Haruko Kuroiwa, Mikio Nishimura, Tsuneyoshi KuroiwaAbstract:The proliferation cycle of the Microbody was studied in the primitive red alga Cyanidioschyzon merolae, which contains one Microbody per cell. Cells were synchronized with a dark/light cycle, and the morphology of the Microbody and its interaction with other organelles were observed three-dimensionally by fluorescence microscopy, transmission electron microscopy, and computer-assisted three-dimensional reconstruction of serial thin sections. The Microbody in interphase cells is a sphere of 0.3 μm in diameter without a core. In M-phase, the Microbody passes through a series of irregular shapes, in the order rod, worm, branched, H-shaped and dumbbell, and symmetric fission occurs just before cytokinesis. The Microbody duplicates its volume in M-phase and three-dimensional quantitative analysis revealed that its surface area increases before its volume does. The Microbody touches the mitochondrion and the chloroplast throughout its proliferation cycle, except briefly in interphase cells, winding around the divisional plane of the mitochondrion at one phase. Immunocytochemical labeling of catalase as a marker of matrix proteins of the Microbody revealed that the duplication of catalase occurs in tandem with the volume increase. While no specific apparatus was identified in the Microbody divisional areas, we identified an electron-dense apparatus about 30–50 nm in diameter between the Microbody and the mitochondrion that may play a role in segregating the daughter microbodies. These results are the first characterization to show the morphological changes of one Microbody in a one-Microbody alga without proliferation-inducing substrates, which have been used in many studies, and clearly show that two daughter microbodies arise by binary fission of the pre-existing Microbody.
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Microbody defective mutants of arabidopsis
Journal of Plant Research, 1998Co-Authors: Mikio Nishimura, Akira Kato, Makoto Hayashi, Kanako Toriyama, Shoji Mano, Katsushi Yamaguchi, Maki Kondo, Hiroshi HayashiAbstract:In germinating fatty seedlings, microbodies are differentiated to leaf peroxisomes from glyoxysomes during greening, and then transformed to glyoxysomes from leaf peroxisomes during senescence. These transformations of microbodies are regulated at various level, such as gene expression, splicing of the mRNA and degradation of Microbody proteins. In order to clarify the regulatory mechanisms underlying these transformations of microbodies, we tried to obtain glyoxysome-deficient mutants of Arabidopsis. We screened 2,4-dichlorophenoxybutyric acid (2,4-DB) mutants of Arabidopsis which have defects in glyoxysomal fatty acid β-oxidation. Four mutants can be classified as carrying alleles at three independent loci, which we designatedped1, ped2, andped3, respectively (whereped stands for peroxisome defective). The characteristics of theseped mutants are described.
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Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin
Plant Molecular Biology, 1995Co-Authors: Akira Kato, Makoto Hayashi, Hitoshi Mori, Mikio NishimuraAbstract:A cDNA clone for glyoxysomal citrate synthase (gCS) was isolated from a λgt11 cDNA library prepared from etiolated pumpkin cotyledons. The cDNA of 1989 bp consisted of a 1548 bp open reading frame that encoded 516 amino acid residues. The deduced amino acid sequence of gCS did not have a typical peroxisomal targeting signal at its carboxyl terminal. A study of expression in vitro of the cDNA and an analysis of the amino-terminal sequence of the citrate synthase indicated that gCS is synthesized as a larger precursor that has a cleavable amino-terminal presequence of 43 amino acids. The predicted amino-terminal sequence of pumpkin gCS was highly homologous to those of other Microbody enzymes, such as 3-ketoacyl-CoA thiolase of rat and malate dehydrogenase of watermelon that are also synthesized as precursors of higher molecular mass. Immunoblot analysis showed that the level of gCS protein increased markedly during germination and decreased rapidly during the light-induced transition of microbodies from glyoxysomes to leaf peroxisomes. By contrast, the level of mRNA for gCS reached a maximum earlier than that of the protein and declined even in darkness. The level of the mRNA was low during the Microbody transition. These results indicate that the accumulation of the gCS protein does not correspond to that of the mRNA and that degradation of gCS is induced during the Microbody transition, suggesting that post-transcriptional regulation plays an important role in the Microbody transition.
Nanlin Tan - One of the best experts on this subject based on the ideXlab platform.
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The movement of the soil Microbody.
2019Co-Authors: Nanlin TanAbstract:The movement of the soil Microbody.
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The size of the soil Microbody.
2019Co-Authors: Nanlin TanAbstract:The size of the soil Microbody.
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The forces acted on the soil Microbody.
2019Co-Authors: Nanlin TanAbstract:The forces acted on the soil Microbody.
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The velocity vector between the soil Microbody and the blade.
2019Co-Authors: Nanlin TanAbstract:The velocity vector between the soil Microbody and the blade.
Crina M Nimigean - One of the best experts on this subject based on the ideXlab platform.
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an ace2 Microbody containing a single immunoglobulin fc domain is a potent inhibitor of sars cov 2
Cell Reports, 2020Co-Authors: Takuya Tada, Chen Fan, R Kaur, Kenneth A Stapleford, Harry B Gristick, Crina M Nimigean, Jennifer S Chen, Belinda M Dcosta, Craig B Wilen, Nathaniel R LandauAbstract:Soluble forms of angiotensin-converting enzyme 2 (ACE2) have recently been shown to inhibit severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. We report on an improved soluble ACE2, termed a "Microbody," in which the ACE2 ectodomain is fused to Fc domain 3 of the immunoglobulin (Ig) heavy chain. The protein is smaller than previously described ACE2-Ig Fc fusion proteins and contains an H345A mutation in the ACE2 catalytic active site that inactivates the enzyme without reducing its affinity for the SARS-CoV-2 spike. The disulfide-bonded ACE2 Microbody protein inhibits entry of SARS-CoV-2 spike protein pseudotyped virus and replication of live SARS-CoV-2 in vitro and in a mouse model. Its potency is 10-fold higher than soluble ACE2, and it can act after virus bound to the cell. The Microbody inhibits the entry of s coronaviruses and virus with the variant D614G spike. The ACE2 Microbody may be a valuable therapeutic for coronavirus disease 2019 (COVID-19) that is active against viral variants and future coronaviruses.
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a soluble ace2 Microbody protein fused to a single immunoglobulin fc domain is a potent inhibitor of sars cov 2 infection in cell culture
bioRxiv, 2020Co-Authors: Takuya Tada, Chen Fan, R Kaur, Kenneth A Stapleford, Harry B Gristick, Crina M Nimigean, Nathaniel R LandauAbstract:Soluble forms of ACE2 have recently been shown to inhibit SARS-CoV-2 infection. We report on an improved soluble form of ACE2, termed a "Microbody" in which the ACE2 ectodomain is fused to Fc domain 3 of the immunoglobulin heavy chain. The protein is smaller than previously described ACE2-Ig Fc fusion proteins and contains an H345A mutation in the catalytic active site that inactivates the enzyme without reducing its affinity for the SARS-CoV-2 spike. The disulfide-bonded ACE2 Microbody inhibited entry of SARS-CoV-2 spike protein pseudotyped virus and live SARS-CoV-2 with a potency 10-fold higher than unmodified soluble ACE2 and retained activity even after the virus had bound to the cell. The ACE2 Microbody inhibited entry of ACE2-utilizing β coronaviruses and entry of viruses with the high infectivity variant D614G spike. The ACE2 Microbody may be a valuable therapeutic for COVID-19 that is active against SARS-CoV-2 variants and against coronaviruses that may arise in the future.