{"id":{"repo_id":"lsu-thes","oai_identifier":"oai:repository.lsu.edu:gradschool_dissertations-1446"},"canonical_url":"https://search.dev.ndltd.org/etd/lsu-thes/oai:repository.lsu.edu:gradschool_dissertations-1446","repository":{"repo_id":"lsu-thes","name":"Lousiana State University","base_url":"https://repository.lsu.edu/do/oai/"},"display":{"title":"OspC in the pathogenesis of Borrelia burgdorferi","abstract":"Lyme disease is a multisystem disorder caused by the tick vector Borrelia burgdorferi. During its life cycle between the tick vector and the mammalian host, Borrelia up- and down-regulates the expression of its surface lipoproteins. Of its many surface lipoproteins, the Outer surface protein C (OspC) is crucial for initial mammalian infection. OspC has a common role shared with other lipoproteins of protection against host innate defences and a unique function in facilitating the dissemination of B. burgdorferi in the murine host. The structure of OspC was solved in 2001 and the lipoprotein was found to be predominantly alpha-helical with 5 alpha helices and 2 beta sheets interconnected by 6 loops, and an N- and C-terminus. Not much is known as to how the OspC structure relates to the function of the lipoprotein and/or possible regulation. The up-and down-regulation of OspC is achieved by the rpoS alternative sigma factor and by an unidentified repressor, respectively. Several truncated versions of OspC were tested in an OspC-deficient background to better understand the role of the amino acid sequences deleted. Structural deletions of 5 to 8-AA made within the OspC core, resulted in loss of infectivity. Longer deletions of 10- and 13 AA towards the N- and C-terminus of OspC, respectively, also resulted in loss of infectivity. Interestingly, a deletion of only 5-AA of the N-terminus of OspC did not affect the role of OspC in evasion but caused inefficient dissemination of B. burgdorferi in SCID mice. Interestingly, whereas the deletion of N-terminus 5-AA of OspC resulted in upregulation, a deletion of 6- and 9-AA of the C-terminus of OspC resulted in downregulation of ospC mRNA in joints, indicating that OspC may be involved in self-regulation. This hypothesis was confirmed by the use of monoclonal antibody treatment. Deletion of 6-AA of the C-terminus of OspC resulted in lower spirochete burdens in heart and joint, whereas deletion of 9-AA resulted in higher spirochete burden in skin, indicating the tissue-dependent effects resulting from the deletion of the C-terminal sequence. Taken together, these results indicate that OspC is involved in the pathogenesis of B. burgdorferi.","abstract_html":"Lyme disease is a multisystem disorder caused by the tick vector Borrelia burgdorferi. During its life cycle between the tick vector and the mammalian host, Borrelia up- and down-regulates the expression of its surface lipoproteins. Of its many surface lipoproteins, the Outer surface protein C (OspC) is crucial for initial mammalian infection. OspC has a common role shared with other lipoproteins of protection against host innate defences and a unique function in facilitating the dissemination of B. burgdorferi in the murine host. The structure of OspC was solved in 2001 and the lipoprotein was found to be predominantly alpha-helical with 5 alpha helices and 2 beta sheets interconnected by 6 loops, and an N- and C-terminus. Not much is known as to how the OspC structure relates to the function of the lipoprotein and/or possible regulation. The up-and down-regulation of OspC is achieved by the rpoS alternative sigma factor and by an unidentified repressor, respectively. Several truncated versions of OspC were tested in an OspC-deficient background to better understand the role of the amino acid sequences deleted. Structural deletions of 5 to 8-AA made within the OspC core, resulted in loss of infectivity. Longer deletions of 10- and 13 AA towards the N- and C-terminus of OspC, respectively, also resulted in loss of infectivity. Interestingly, a deletion of only 5-AA of the N-terminus of OspC did not affect the role of OspC in evasion but caused inefficient dissemination of B. burgdorferi in SCID mice. Interestingly, whereas the deletion of N-terminus 5-AA of OspC resulted in upregulation, a deletion of 6- and 9-AA of the C-terminus of OspC resulted in downregulation of ospC mRNA in joints, indicating that OspC may be involved in self-regulation. This hypothesis was confirmed by the use of monoclonal antibody treatment. Deletion of 6-AA of the C-terminus of OspC resulted in lower spirochete burdens in heart and joint, whereas deletion of 9-AA resulted in higher spirochete burden in skin, indicating the tissue-dependent effects resulting from the deletion of the C-terminal sequence. Taken together, these results indicate that OspC is involved in the pathogenesis of B. burgdorferi.","abstract_has_math":false,"creators":["Seemanapalli, Sunita V"],"institution":"Veterinary Medical Sciences - Pathobiological Sciences","degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Veterinary Pathology and Pathobiology","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-01-01T08:00:00Z","date_published":"2010-01-01T08:00:00Z","updated_at":"2026-07-24T02:57:39Z","subjects":["Vector-borne disease","Spirochetes"],"languages":[],"rights":["unrestricted","Release the entire work immediately for access worldwide."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["etd-02202010-133406","https://repository.lsu.edu/gradschool_dissertations/447"],"render_values":[{"text":"etd-02202010-133406","href":null,"code":true},{"text":"https://repository.lsu.edu/gradschool_dissertations/447","href":"https://repository.lsu.edu/gradschool_dissertations/447","code":true}]}]},"links":{"outbound_url":"https://doi.org/10.31390/gradschool_dissertations.447","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Seemanapalli, Sunita V"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2010-01-13"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2022-05-12T23:08:51Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Veterinary Pathology and Pathobiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Veterinary Medical Sciences - Pathobiological Sciences"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Vector-borne disease","Spirochetes"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["unrestricted","Release the entire work immediately for access worldwide."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["etd-02202010-133406","10.31390/gradschool_dissertations.447","https://repository.lsu.edu/gradschool_dissertations/447"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Lyme disease is a multisystem disorder caused by the tick vector Borrelia burgdorferi. During its life cycle between the tick vector and the mammalian host, Borrelia up- and down-regulates the expression of its surface lipoproteins. Of its many surface lipoproteins, the Outer surface protein C (OspC) is crucial for initial mammalian infection. OspC has a common role shared with other lipoproteins of protection against host innate defences and a unique function in facilitating the dissemination of B. burgdorferi in the murine host. The structure of OspC was solved in 2001 and the lipoprotein was found to be predominantly alpha-helical with 5 alpha helices and 2 beta sheets interconnected by 6 loops, and an N- and C-terminus. Not much is known as to how the OspC structure relates to the function of the lipoprotein and/or possible regulation. The up-and down-regulation of OspC is achieved by the rpoS alternative sigma factor and by an unidentified repressor, respectively. Several truncated versions of OspC were tested in an OspC-deficient background to better understand the role of the amino acid sequences deleted. Structural deletions of 5 to 8-AA made within the OspC core, resulted in loss of infectivity. Longer deletions of 10- and 13 AA towards the N- and C-terminus of OspC, respectively, also resulted in loss of infectivity. Interestingly, a deletion of only 5-AA of the N-terminus of OspC did not affect the role of OspC in evasion but caused inefficient dissemination of B. burgdorferi in SCID mice. Interestingly, whereas the deletion of N-terminus 5-AA of OspC resulted in upregulation, a deletion of 6- and 9-AA of the C-terminus of OspC resulted in downregulation of ospC mRNA in joints, indicating that OspC may be involved in self-regulation. This hypothesis was confirmed by the use of monoclonal antibody treatment. Deletion of 6-AA of the C-terminus of OspC resulted in lower spirochete burdens in heart and joint, whereas deletion of 9-AA resulted in higher spirochete burden in skin, indicating the tissue-dependent effects resulting from the deletion of the C-terminal sequence. Taken together, these results indicate that OspC is involved in the pathogenesis of B. burgdorferi."]},{"key":"dc:title","label":"Title","values":["OspC in the pathogenesis of Borrelia burgdorferi"]}]}],"canonical_facts":{"dc:creator":["Seemanapalli, Sunita V"],"dc:date":["2010-01-13"],"dc:date.available":["2022-05-12T23:08:51Z"],"dc:description.abstract":["Lyme disease is a multisystem disorder caused by the tick vector Borrelia burgdorferi. During its life cycle between the tick vector and the mammalian host, Borrelia up- and down-regulates the expression of its surface lipoproteins. Of its many surface lipoproteins, the Outer surface protein C (OspC) is crucial for initial mammalian infection. OspC has a common role shared with other lipoproteins of protection against host innate defences and a unique function in facilitating the dissemination of B. burgdorferi in the murine host. The structure of OspC was solved in 2001 and the lipoprotein was found to be predominantly alpha-helical with 5 alpha helices and 2 beta sheets interconnected by 6 loops, and an N- and C-terminus. Not much is known as to how the OspC structure relates to the function of the lipoprotein and/or possible regulation. The up-and down-regulation of OspC is achieved by the rpoS alternative sigma factor and by an unidentified repressor, respectively. Several truncated versions of OspC were tested in an OspC-deficient background to better understand the role of the amino acid sequences deleted. Structural deletions of 5 to 8-AA made within the OspC core, resulted in loss of infectivity. Longer deletions of 10- and 13 AA towards the N- and C-terminus of OspC, respectively, also resulted in loss of infectivity. Interestingly, a deletion of only 5-AA of the N-terminus of OspC did not affect the role of OspC in evasion but caused inefficient dissemination of B. burgdorferi in SCID mice. Interestingly, whereas the deletion of N-terminus 5-AA of OspC resulted in upregulation, a deletion of 6- and 9-AA of the C-terminus of OspC resulted in downregulation of ospC mRNA in joints, indicating that OspC may be involved in self-regulation. This hypothesis was confirmed by the use of monoclonal antibody treatment. Deletion of 6-AA of the C-terminus of OspC resulted in lower spirochete burdens in heart and joint, whereas deletion of 9-AA resulted in higher spirochete burden in skin, indicating the tissue-dependent effects resulting from the deletion of the C-terminal sequence. Taken together, these results indicate that OspC is involved in the pathogenesis of B. burgdorferi."],"dc:identifier":["etd-02202010-133406","10.31390/gradschool_dissertations.447","https://repository.lsu.edu/gradschool_dissertations/447"],"dc:rights":["unrestricted","Release the entire work immediately for access worldwide."],"dc:subject":["Vector-borne disease","Spirochetes"],"dc:title":["OspC in the pathogenesis of Borrelia burgdorferi"],"thesis:degree_discipline":["Veterinary Pathology and Pathobiology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"],"thesis:institution_name":["Veterinary Medical Sciences - Pathobiological Sciences"]},"updated_at":"2026-07-24T02:57:39Z"}