Structural Investigations into Lysozymes from Trichomonas vaginalis

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dc.contributor.advisor Goldstone, D en
dc.contributor.author Reeves, David en
dc.date.accessioned 2019-09-20T02:24:16Z en
dc.date.issued 2019 en
dc.identifier.uri http://hdl.handle.net/2292/47842 en
dc.description Full Text is available to authenticated members of The University of Auckland only. en
dc.description.abstract Trichomonas vaginalis is the most common non-viral sexually transmitted infection in the world, with more than 143 million new infections each year. This obligate parasite of the human urogenital tract infects 5% of women and 0.6% of men worldwide causing trichomoniasis. Symptoms include urethritis, vaginal pruritus, and erythema. Most infections are asymptomatic but confer complications such as increased cervical and prostate cancer risk, male infertility, and a 2-3-fold increased risk of HIV acquisition. Infection requires adherence of the protozoa to the epithelial tissue of the urogenital tract, which is inhibited by the native microbiota. Treatment of T. vaginalis, limited to metronidazole and tinidazole, is becoming less frequently successful as drug resistant strains are on the rise. The T. vaginalis genome was published in 2007, which identified a highly expanded degradome. Previous work from our group characterised nine NlpC proteins, which demonstrate activity against bacterial cell wall peptidoglycan by cleaving the peptide cross links. To further explore the repertoire of peptidoglycan degrading enzymes in T. vaginalis, we searched the T. vaginalis genome for lysozyme-like proteins. We identified eight candidate lysozyme-like genes (Lys1-7). Sequence analysis revealed five contained arginine rich signal sequences very similar to those previously seen in NlpC proteins. The crystal structure of Lys3 was solved to 1.2Å. Structural analysis revealed a close relationship to the GH19 family of Lysozymes. Turbidity assays confirmed activity against bacterial peptidoglycan. en
dc.publisher ResearchSpace@Auckland en
dc.relation.ispartof Masters Thesis - University of Auckland en
dc.relation.isreferencedby UoA99265173005802091 en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. en
dc.rights Restricted Item. Full Text is available to authenticated members of The University of Auckland only. en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.rights.uri http://creativecommons.org/licenses/by-nc-sa/3.0/nz/ en
dc.title Structural Investigations into Lysozymes from Trichomonas vaginalis en
dc.type Thesis en
thesis.degree.discipline Biological Sciences en
thesis.degree.grantor The University of Auckland en
thesis.degree.level Masters en
dc.rights.holder Copyright: The author en
pubs.elements-id 781035 en
pubs.org-id Science en
pubs.org-id Biological Sciences en
pubs.record-created-at-source-date 2019-09-20 en


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http://creativecommons.org/licenses/by-nc-sa/3.0/nz/ Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/3.0/nz/

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