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Proteinski profil bakterije vrste Listeria monocytogenes v biofilmu
ID
Vörös, Dimitrij
(
Author
),
ID
Jamnik, Polona
(
Mentor
)
More about this mentor...
,
ID
Jeršek, Barbka
(
Comentor
)
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MD5: F96D9428AA199E6A9E94E1AB1575E678
PID:
20.500.12556/rul/87973730-48dc-4990-9503-20f9c9cf0c8d
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Abstract
Cilj magistrske naloge je primerjati proteinski profil površinskih proteinov celic različnih sevov bakterij vrste Listeria monocytogenes v planktonski kulturi in biofilmu ter ugotoviti vlogo flagela pri adheziji bakterij vrste L. monocytogenes na abiotske površine. Uporabili smo tri seve bakterij vrste L. monocytogenes iz katerih smo izolirali površinske proteine in jih analizirali z dvodimenzionalno poliakrialmidno gelsko elektroforezo. Diferencialno izražene proteine smo nato identificirali s masno spektrometrijo. Po analizi slik profilov površinskih proteinov je med sevi v planktonski kulturi bilo moč zaznati le manjše razlike, nekoliko večje so bile v biofilmu v primeru seva bakterij vrste L. monocytogenes ŽM 603. Nato smo za vsak sev posebej primerjali profil površinskih proteinov celic biofilma s profilom površinskih proteinov planktonskih celic. Profil površinskih proteinov celic v biofilmu se je razlikoval od profila celic v planktonski kulturi pri vseh treh sevih. Med identificiranimi diferencialno izraženimi proteini so bili tudi proteini z več različnimi funkcijami (ang. moonlight proteins, MLP). Izmed vseh treh sevov je bilo največ povečano izraženih MLP v biofilmu pri sevu L. monocytogenes ŽM 603. V vseh treh sevih je bila v biofilmski kulturi povišana raven encima piruvat dehidrogenaza. Kljub okvari in odsotnosti bička sta seva L. monocytogenes ŽM 603 in ŽM 600 tvorila biofilme, kar posredno nakazuje, da flagel direktno ne prispeva k adheziji in posledično tvorbi biofilma.
Language:
Slovenian
Keywords:
bakterije
,
Listeria monocytogenes
,
biofilm
,
površinski proteini
,
proteomika
,
dvodimenzionalna poliakrialmidna gelska elektroforeza
Work type:
Master's thesis/paper
Typology:
2.09 - Master's Thesis
Organization:
BF - Biotechnical Faculty
Publisher:
[D. Vörös]
Year:
2017
PID:
20.500.12556/RUL-95605
UDC:
577.112:579.2:57.088
COBISS.SI-ID:
4819320
Publication date in RUL:
21.09.2017
Views:
2430
Downloads:
689
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VÖRÖS, Dimitrij, 2017,
Proteinski profil bakterije vrste Listeria monocytogenes v biofilmu
[online]. Master’s thesis. D. Vörös. [Accessed 17 May 2025]. Retrieved from: https://repozitorij.uni-lj.si/IzpisGradiva.php?lang=eng&id=95605
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Language:
English
Title:
Protein profile of Listeria monocytogenes in biofilm
Abstract:
The aim of this thesis was to compare the protein profile of surface proteins from different strains of Listeria monocytogenes in planktonic culture and biofilm and also to determine the role of flagellum in the adhesion of L. monocytogenes to abiotic surfaces. Within master thesis we used three strains from which we remove surface proteins and then analysing those proteins with two-dimensional polyacrilamide electrophoresis. Differentially expressed proteins were then identified with mass spectrometry. After analyzing images of surface proteins profiles, we detected small differences in planktonic culture and slightly higher in biofilm in the case of strain L. monocytogenes ŽM 603. Comparison of the profile of surface proteins of biofilm cells with the profile of surface proteins of planktonic cells showed differences in each strain. Amongst identified differentially expressed proteins were also moonlight proteins (MLP). Amongst all three strains, the highest number of expressed MLP in biofilm was observed in the L. monocyotgenes ŽM 603 strain. In all three strains, the level of the pyruvate dehydrogenase enzyme was increased in the biofilm culture. Despite of the defect and absence of flagellum, both strains, L. monocytogenes ŽM 603 and ŽM 600, formed biofilms, which indirectly indicates that flagellum does not contribute to adhesion and consequently in the process of forming the biofilm.
Keywords:
bacteria
,
Listeria monocoytogenes
,
biofilm
,
surface proteins
,
proteomics
,
two-dimensional polyacrilamide electrophoresis
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