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Structural and Functional Analysis of Listeria Adhesion Protein

Dissertation (MSc (Biochemistry))--University of Pretoria, 2022.

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Other Authors: Schubert, Wolf-Dieter
Format: Thesis
Language:English
Published: University of Pretoria 2022
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access_status_str Open Access
author2 Schubert, Wolf-Dieter
author_browse Schubert, Wolf-Dieter
author_facet Schubert, Wolf-Dieter
collection Thesis
dc_rights_str_mv © 2022 University of Pretoria. All rights reserved. The copyright in this work vests in the University of Pretoria. No part of this work may be reproduced or transmitted in any form or by any means, without the prior written permission of the University of Pretoria.
description Dissertation (MSc (Biochemistry))--University of Pretoria, 2022.
format Thesis
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institution University of Pretoria (South Africa)
language English
last_indexed 2026-06-10T12:37:51.914Z
license_str Other — see source repository
provenance_str_mv Harvested via OAI-PMH from UPSpace — University of Pretoria Institutional Repository
publishDate 2022
publishDateRange 2022
publishDateSort 2022
publisher University of Pretoria
publisherStr University of Pretoria
record_format dspace
source_str UPSpace — University of Pretoria Institutional Repository
spelling oai:repository.up.ac.za:2263/86142 Structural and Functional Analysis of Listeria Adhesion Protein Schubert, Wolf-Dieter boswell.clare@gmail.com Boswell, Clare Anne UCTD Dissertation (MSc (Biochemistry))--University of Pretoria, 2022. Listera monocytogenes (Lm) is a gram-positive opportunistic foodborne pathogen. It is responsible for the disease listeriosis, which though rare, causes high morbidity and mortality. The pathogen targets the intestine for systemic entry. Lm uses several membrane proteins to breach the intestinal barrier and to translocate for systemic distribution. Additionally, the pathogen utilizes a normally cytosolic protein for translocation: bifunctional acetaldehyde alcohol dehydrogenase, which moonlights as Listeria adhesion protein (LAP). LAP has been reported to interact with mitochondrial heat shock protein 60 (Hsp60) presented on intestinal epithelial cells. The interaction allows for paracellular translocation, avoiding intracellular host immunity. LAP was cloned, produced and purified for downstream experimentation. The purified protein was characterized with enzyme activity assays and electron microscopy. The acetaldehyde dehydrogenase and alcohol dehydrogenase domains of LAP have Vmax values of 0.56 mM.min-1 and 1.17 mM.min-1 respectively. LAP was also found to oligomerise into filaments potentially needed for activity. START Grant NRF Biochemistry, Genetics and Microbiology (BGM) MSc (Biochemistry) Unrestricted 2022-07-13T11:41:06Z 2022-07-13T11:41:06Z 2022-09-24 2022 Dissertation Boswell, CA, 2022, Structural and Functional Analysis of Listeria Adhesion Protein, University of Pretoria, viewed yymmdd https://repository.up.ac.za/handle/2263/86142 S2022 https://repository.up.ac.za/handle/2263/86142 https://doi.org/10.25403/UPresearchdata.20236746 en © 2022 University of Pretoria. All rights reserved. The copyright in this work vests in the University of Pretoria. No part of this work may be reproduced or transmitted in any form or by any means, without the prior written permission of the University of Pretoria. application/pdf University of Pretoria
spellingShingle UCTD
Structural and Functional Analysis of Listeria Adhesion Protein
title Structural and Functional Analysis of Listeria Adhesion Protein
title_full Structural and Functional Analysis of Listeria Adhesion Protein
title_fullStr Structural and Functional Analysis of Listeria Adhesion Protein
title_full_unstemmed Structural and Functional Analysis of Listeria Adhesion Protein
title_short Structural and Functional Analysis of Listeria Adhesion Protein
title_sort structural and functional analysis of listeria adhesion protein
topic UCTD
url https://repository.up.ac.za/handle/2263/86142
https://doi.org/10.25403/UPresearchdata.20236746