{"id":{"repo_id":"utmb","oai_identifier":"oai:utmb-ir.tdl.org:2152.3/11208"},"canonical_url":"https://search.dev.ndltd.org/etd/utmb/oai:utmb-ir.tdl.org:2152.3/11208","repository":{"repo_id":"utmb","name":"University of Texas Medical Branch","base_url":"https://utmb-ir.tdl.org/server/oai/request"},"display":{"title":"Ehrlichia chaffeensis Type 1 Secreted Effector TRP47 is a Novel SUMOylated Nucleomodulin","abstract":"Ehrlichia chaffeensis secretes immunodominant and immunoprotective protein effectors into the host cell using a type I secretion system. The best-characterized of these effectors are the tandem repeat proteins (TRPs). In this study, E. chaffeensis TRP47 was identified as a target for host cell SUMOylation and as a novel nucleomodulin with DNA-binding activity and host nuclear localization. Using a microfluidic chip peptide array, a SUMOylation site in the TRP47 N-terminal domain was identified. A SUMO-2 modification was further confirmed using an in vitro SUMOylation assay with recombinant TRP47, and native polySUMOylated TRP47 was immunoprecipitated from E. chaffeensis-infected cell lysates. TRP47 was detected in host cell nuclei primarily at 24 and 48 hours post-infection by immunofluorescence microscopy. A domain in the N-terminal portion of the protein containing a variant MYND-binding motif was identified as the region responsible for TRP47 nuclear localization using ectopically expressed GFP-tagged TRP47 truncation constructs. Recombinant TRP47 also binds human genomic DNA in an electrophoretic mobility shift assay. Taken together, these data demonstrate that E. chaffeensis TRP47 is a nucleomodulin with DNA-binding activity and a non-canonical nuclear localization signal, and is post-translationally modified by SUMOylation, which is a novel modification among bacteria.","abstract_html":"Ehrlichia chaffeensis secretes immunodominant and immunoprotective protein effectors into the host cell using a type I secretion system. The best-characterized of these effectors are the tandem repeat proteins (TRPs). In this study, E. chaffeensis TRP47 was identified as a target for host cell SUMOylation and as a novel nucleomodulin with DNA-binding activity and host nuclear localization. Using a microfluidic chip peptide array, a SUMOylation site in the TRP47 N-terminal domain was identified. A SUMO-2 modification was further confirmed using an in vitro SUMOylation assay with recombinant TRP47, and native polySUMOylated TRP47 was immunoprecipitated from E. chaffeensis-infected cell lysates. TRP47 was detected in host cell nuclei primarily at 24 and 48 hours post-infection by immunofluorescence microscopy. A domain in the N-terminal portion of the protein containing a variant MYND-binding motif was identified as the region responsible for TRP47 nuclear localization using ectopically expressed GFP-tagged TRP47 truncation constructs. Recombinant TRP47 also binds human genomic DNA in an electrophoretic mobility shift assay. Taken together, these data demonstrate that E. chaffeensis TRP47 is a nucleomodulin with DNA-binding activity and a non-canonical nuclear localization signal, and is post-translationally modified by SUMOylation, which is a novel modification among bacteria.","abstract_has_math":false,"creators":["Milligan, Sarah L"],"institution":"The University of Texas Medical Branch at Galveston","degree_name":"Experimental Pathology (Masters)","degree_level":"Masters","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["McBride, Jere W"],"committee_chairs":[],"committee_members":["Walker, David H","Sahni, Sanjeev K"],"year":null,"date_issued":"","date_published":null,"updated_at":"2026-07-24T05:51:04Z","subjects":["Ehrlichia","nucleomodulin","SUMOylation"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/2152.3/11208","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["McBride, Jere W"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Walker, David H","Sahni, Sanjeev K"]},{"key":"dc:creator","label":"Author","values":["Milligan, Sarah L"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2019-03-13T20:47:26Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2019-03-13T20:47:26Z"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Experimental Pathology (Masters)"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["The University of Texas Medical Branch at Galveston"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Ehrlichia","nucleomodulin","SUMOylation"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/2152.3/11208"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Ehrlichia chaffeensis secretes immunodominant and immunoprotective protein effectors into the host cell using a type I secretion system. The best-characterized of these effectors are the tandem repeat proteins (TRPs). In this study, E. chaffeensis TRP47 was identified as a target for host cell SUMOylation and as a novel nucleomodulin with DNA-binding activity and host nuclear localization. Using a microfluidic chip peptide array, a SUMOylation site in the TRP47 N-terminal domain was identified. A SUMO-2 modification was further confirmed using an in vitro SUMOylation assay with recombinant TRP47, and native polySUMOylated TRP47 was immunoprecipitated from E. chaffeensis-infected cell lysates. TRP47 was detected in host cell nuclei primarily at 24 and 48 hours post-infection by immunofluorescence microscopy. A domain in the N-terminal portion of the protein containing a variant MYND-binding motif was identified as the region responsible for TRP47 nuclear localization using ectopically expressed GFP-tagged TRP47 truncation constructs. Recombinant TRP47 also binds human genomic DNA in an electrophoretic mobility shift assay. Taken together, these data demonstrate that E. chaffeensis TRP47 is a nucleomodulin with DNA-binding activity and a non-canonical nuclear localization signal, and is post-translationally modified by SUMOylation, which is a novel modification among bacteria."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Ehrlichia chaffeensis Type 1 Secreted Effector TRP47 is a Novel SUMOylated Nucleomodulin"]}]}],"canonical_facts":{"dc:contributor.advisor":["McBride, Jere W"],"dc:contributor.committeemember":["Walker, David H","Sahni, Sanjeev K"],"dc:creator":["Milligan, Sarah L"],"dc:date.accessioned":["2019-03-13T20:47:26Z"],"dc:date.available":["2019-03-13T20:47:26Z"],"dc:description.abstract":["Ehrlichia chaffeensis secretes immunodominant and immunoprotective protein effectors into the host cell using a type I secretion system. The best-characterized of these effectors are the tandem repeat proteins (TRPs). In this study, E. chaffeensis TRP47 was identified as a target for host cell SUMOylation and as a novel nucleomodulin with DNA-binding activity and host nuclear localization. Using a microfluidic chip peptide array, a SUMOylation site in the TRP47 N-terminal domain was identified. A SUMO-2 modification was further confirmed using an in vitro SUMOylation assay with recombinant TRP47, and native polySUMOylated TRP47 was immunoprecipitated from E. chaffeensis-infected cell lysates. TRP47 was detected in host cell nuclei primarily at 24 and 48 hours post-infection by immunofluorescence microscopy. A domain in the N-terminal portion of the protein containing a variant MYND-binding motif was identified as the region responsible for TRP47 nuclear localization using ectopically expressed GFP-tagged TRP47 truncation constructs. Recombinant TRP47 also binds human genomic DNA in an electrophoretic mobility shift assay. Taken together, these data demonstrate that E. chaffeensis TRP47 is a nucleomodulin with DNA-binding activity and a non-canonical nuclear localization signal, and is post-translationally modified by SUMOylation, which is a novel modification among bacteria."],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["https://hdl.handle.net/2152.3/11208"],"dc:subject":["Ehrlichia","nucleomodulin","SUMOylation"],"dc:title":["Ehrlichia chaffeensis Type 1 Secreted Effector TRP47 is a Novel SUMOylated Nucleomodulin"],"dc:type":["Thesis"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Experimental Pathology (Masters)"],"thesis:institution_name":["The University of Texas Medical Branch at Galveston"]},"updated_at":"2026-07-24T05:51:04Z"}