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dc.contributor.authorKivumbi, Mark Tefero
dc.date.accessioned2021-03-30T09:50:15Z
dc.date.available2021-03-30T09:50:15Z
dc.date.issued2021-01
dc.identifier.urihttp://hdl.handle.net/20.500.12281/9923
dc.descriptionA Special Research Report Submitted to the College of Veterinary Medicine, Animal Resources and Biosecurity in Partial Fulfillment for the Award of a Bachelor’s Degree in Biomedical Laboratory Technology of Makerere University, Kampala .en_US
dc.description.abstractProtein secretion systems are essential for the growth of bacteria and are used in an array of processes. Bacterial secretion systems are protein complexes present on the cell membranes of bacteria for the secretion of substances. Specifically, they are th e cellular devices used by pathogenic bacteria to secrete their virulence factors like secreted proteins to invade the host cells. Proteins can be secreted through two major processes. One process is a onestep mechanism in which proteins from the cytoplas m of bacteria are transported and delivered directly through the cell membrane into the host cell. Another involves a twostep activity in which the proteins are first transported out of the inner cell membrane, then deposited in the periplasm, and finally through the outer cell membrane into the host cell. identification is key to understanding protein secretion. Structural Our study focused at evaluating the structural basis for the secretion of substances through Bacterial secretion systems. The analysis required the use of different commands and this was done using Jmol, which is a molecular viewer. The bacterial secretion systems were downloaded from the protein data bank. It was discovered that there are twelve proposed bacterial secretion systems name ly; SecA, the post translational pathway, SRP pathway, Tat system, T1SS, T2SS, T3SS, T4SS, T5SS, T6SS, T7SS, T8SS and T9SS. Two of these, T5SS and T8SS were not found in the PDB. Three of the bacteria secretion systems Tat, T6SS and T9SS had no nucleotide binding sites solved along with the structures. The remaining seven, SecA, SRP, T1SS, T2SS, T3SS, T4SS and T7SS had the nucleotide binding sites solved along with the structures. In a nutshell, all the bacterial secretion systems should be further studied and expressed and structures deposited in the Protein Data bank, all molecular viewers should be made accessible to ease the study of these molecules. These molecules sho freely uld further be studied to fully characterize the features and relate them to function.en_US
dc.language.isoenen_US
dc.publisherMakerere Universityen_US
dc.subjectBacteriaen_US
dc.subjectProteinen_US
dc.subjectCellular devicesen_US
dc.subjectVirulence factorsen_US
dc.titleEvaluating the structural basis for the secretion of substances through bacterial secretion systems.en_US
dc.typeThesisen_US


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