Master Degree / Yüksek Lisans Tezleri
Permanent URI for this collectionhttps://hdl.handle.net/11147/3008
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Master Thesis Investigation of the Proteins of Leishmania Tropica Causing Viscerotropism in Humans Using Mass Spectrometry(Izmir Institute of Technology, 2022) Beyaz, Merve; Yalçın, TalatLeishmaniasis is a neglected tropical disease in 98 countries and five continents worldwide. The most prevalent forms of this parasitic disease are Cutaneous, Mucocutaneous, and Visceral Leishmaniasis. While Cutaneous Leishmaniasis causes disfiguring skin conditions and lesions, Mucocutaneous Leishmaniasis damages the mucosal tissues of the mouth, nose, and throat. The visceral form of Leishmaniasis causes weight loss, fever, diarrhea, lymph nodes, and spleen or liver enlargement. Today, Leishmania tropica, one of the strains of the Leishmania parasite, no longer causes only Cutaneous Leishmaniasis (CL) but also Visceral Leishmaniasis (VL). The reason for this visceralism in L. tropica is not fully understood. Mass spectrometry has a vital place in proteomic analyses; it provides information about expression levels and the identification of proteins. In this study, the proteins of L. tropica causing CL and CL are analyzed using the mass spectrometric shotgun method. Off-line HPLC separation followed by LC-MS/MS analyses are performed, and differential proteins between CL and VL isolates of L. tropica are determined. Results indicate that among the differentially abundant proteins between two sample groups, paraflagellar rod proteins, elongation factor 1-alpha protein, and surface antigen proteins might play a role in avoiding immune recognition. Also, proteins with peroxidoxin function, cytochrome b5, and endoribonuclease might help parasite survival in macrophages. And finally, thiol-specific antioxidant protein may have a role in viscerotropism in L. tropica.Master Thesis Investigation of Heat Stress-Induced Proteins of Cold-Adapted Pseudomonas Marginals Using Proteomic Approach(Izmir Institute of Technology, 2008) Taşoğlu, Çağdaş; Yalçın, TalatTemperature alteration is known as a common environmental stress condition which all living organisms encounter and response by producing evolutionary wellconserved specific proteins called heat stress or heat shock proteins in the cell in order to adapt and survive. In the current study, the induction of heat stress proteins in a coldadapted bacterial strain of Pseudomonas marginalis cells grown under heat stress was investigated by proteomic approach. Five different temperatures, 5, 10, 15, 24, and 30C, were examined for the purpose of determining the optimum growth temperature for the bacterium. Consequently, 15°C was observed as optimum temperature for growth while 30C was established as heat stress temperature. Total proteins from Pseudomonas marginalis cells in the late exponential phase of growth at these two temperatures were extracted and separated by two-dimensional polyacrylamide gel electrophoresis. Totally 1391 protein spots were visualized for 15C and 1384 protein spots for 30C. After comparing with 15C, 13 protein spots that were differentially expressed in the cells exposed to heat stress (30C) were cut from the gel and fragmented into their peptides by in-gel digestion method. Finally, these proteins were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and database searching. Among them, ribosome recycling factor, universal stress protein family and chaperonin GroEL were established as direct sensors of heat stress. As a result, the genes encoding these two heat stress proteins can be isolated and cloned into any other useful microorganism such as bacteria used for detoxification of industrial waste or used in bioremediation but not capable of surviving at high temperatures so that they can be efficient at those temperatures, too.