{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T19:57:57Z","timestamp":1791230277014,"version":"4.1.0"},"reference-count":31,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2017,8,29]],"date-time":"2017-08-29T00:00:00Z","timestamp":1503964800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2017,9,6]],"date-time":"2017-09-06T00:00:00Z","timestamp":1504656000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI095094"],"award-info":[{"award-number":["AI095094"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM102779"],"award-info":[{"award-number":["GM102779"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM007491"],"award-info":[{"award-number":["GM007491"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"MEXT | Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["26-7030"],"award-info":[{"award-number":["26-7030"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2017,9,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    In immunocompromised hosts, latent infection with\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    can reactivate from tissue cysts, leading to encephalitis. A characteristic of\n                    <jats:italic>T.\u00a0gondii<\/jats:italic>\n                    bradyzoites in tissue cysts is the presence of amylopectin granules. The regulatory mechanisms and role of amylopectin accumulation in this organism are not fully understood. The\n                    <jats:italic>T.\u00a0gondii<\/jats:italic>\n                    genome encodes a putative glycogen phosphorylase (TgGP), and mutants were constructed to manipulate the activity of TgGP and to evaluate the function of TgGP in amylopectin storage. Both a stop codon mutant (Pru\/TgGP\n                    <jats:sup>S25stop<\/jats:sup>\n                    [expressing a Ser-to-stop codon change at position 25 in TgGP]) and a phosphorylation null mutant (Pru\/TgGP\n                    <jats:sup>S25A<\/jats:sup>\n                    [expressing a Ser-to-Ala change at position 25 in TgGp]) mutated at Ser25 displayed amylopectin accumulation, while the phosphorylation-mimetic mutant (Pru\/TgGP\n                    <jats:sup>S25E<\/jats:sup>\n                    [expressing a Ser-to-Glu change at position 25 in TgGp]) had minimal amylopectin accumulation under both tachyzoite and bradyzoite growth conditions. The expression of active TgGP\n                    <jats:sup>S25S<\/jats:sup>\n                    or TgGP\n                    <jats:sup>S25E<\/jats:sup>\n                    restored amylopectin catabolism in Pru\/TgGP\n                    <jats:sup>S25A<\/jats:sup>\n                    . To understand the relation between GP and calcium-dependent protein kinase 2 (CDPK2), which was recently reported to regulate amylopectin consumption, we knocked out CDPK2 in these mutants. Pru\n                    <jats:italic>\u0394cdpk2<\/jats:italic>\n                    \/TgGP\n                    <jats:sup>S25E<\/jats:sup>\n                    had minimal amylopectin accumulation, whereas the\n                    <jats:italic>\u0394cdpk2<\/jats:italic>\n                    phenotype in the other GP mutants and parental lines displayed amylopectin accumulation. Both the inactive S25A and hyperactive S25E mutant produced brain cysts in infected mice, but the numbers of cysts produced were significantly less than the number produced by the S25S wild-type GP parasite. Complementation that restored amylopectin regulation restored brain cyst production to the control levels seen in infected mice. These data suggest that\n                    <jats:italic>T.\u00a0gondii<\/jats:italic>\n                    requires tight regulation of amylopectin expression for efficient production of cysts and persistent infections and that GP phosphorylation is a regulatory mechanism involved in amylopectin storage and utilization.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>IMPORTANCE<\/jats:bold>\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    is an obligate intracellular parasite that causes disease in immune-suppressed individuals, as well as a fetopathy in pregnant women who acquire infection for the first time during pregnancy. This parasite can differentiate between tachyzoites (seen in acute infection) and bradyzoites (seen in latent infection), and this differentiation is associated with disease relapse. A characteristic of bradyzoites is that they contain cytoplasmic amylopectin granules. The regulatory mechanisms and the roles of amylopectin granules during latent infection remain to be elucidated. We have identified a role of\n                    <jats:italic>T.\u00a0gondii<\/jats:italic>\n                    glycogen phosphorylase (TgGP) in the regulation of starch digestion and a role of posttranslational modification of TgGP, i.e., phosphorylation of Ser25, in the regulation of amylopectin digestion. By manipulating TgGP activity in the parasite with genome editing, we found that the digestion and storage of amylopectin due to TgGP activity are both important for latency in the brain.\n                  <\/jats:p>","DOI":"10.1128\/mbio.01289-17","type":"journal-article","created":{"date-parts":[[2017,8,29]],"date-time":"2017-08-29T20:10:24Z","timestamp":1504037424000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":67,"title":["<i>Toxoplasma gondii<\/i>\n                    Requires Glycogen Phosphorylase for Balancing Amylopectin Storage and for Efficient Production of Brain Cysts"],"prefix":"10.1128","volume":"8","author":[{"given":"Tatsuki","family":"Sugi","sequence":"first","affiliation":[{"name":"Department of Pathology, Albert Einstein College of Medicine, Bronx, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent","family":"Tu","sequence":"additional","affiliation":[{"name":"Department of Pathology, Albert Einstein College of Medicine, Bronx, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yanfen","family":"Ma","sequence":"additional","affiliation":[{"name":"Department of Pathology, Albert Einstein College of Medicine, Bronx, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tadakimi","family":"Tomita","sequence":"additional","affiliation":[{"name":"Department of Pathology, Albert Einstein College of Medicine, Bronx, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0357-7396","authenticated-orcid":false,"given":"Louis M.","family":"Weiss","sequence":"additional","affiliation":[{"name":"Department of Pathology, Albert Einstein College of Medicine, Bronx, New York, USA"},{"name":"Department of Medicine, Albert Einstein College of Medicine, Bronx, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","volume-title":"Toxoplasma gondii: the model apicomplexan\u2014perspectives and methods","author":"Weiss LM","year":"2014","unstructured":"Weiss LM Kim K (ed). 2014. 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