Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain:
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| Beschreibung: | XIV, 142 Seiten Illustrationen, Diagramme |
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| 245 | 1 | 0 | |a Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |c von Katja E. Boysen |
| 264 | 1 | |a Berlin |c 2013 | |
| 300 | |a XIV, 142 Seiten |b Illustrationen, Diagramme | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 502 | |b Dissertation |c Humboldt-Universität zu Berlin |d 2013 | ||
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| 776 | 0 | 8 | |i Reproduziert als |a Boysen, Katja E. |t Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |d Ketsch bei Mannheim : Mikroform Dissertation, 2013 |h 3 Mikrofiches |w (DE-604)BV041708365 |
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| adam_text | IMAGE 1
TABLE OF CONTENTS
SUMMARY I
ZUSAMMENFASSUNG II
ABBREVIATIONS XII
1 INTRODUCTION 1
1.1 THE MITOCHONDRION IN PLASMODIUM SPP. ; 1
1.1.1 STRUCTURE OF THE MITOCHONDRION THROUGHOUT THE PLASMODIAL LIFE
CYCLE 2
1.1.2 COMPONENTS OF THE MITOCHONDRION 4
1.2 METABOLIC PATHWAYS IN THE MITOCHONDRION 5
1.2.1 LIPOIC ACID SCAVENGING 5
1.2.2 TRANSCRIPTION AND TRANSLATION 6
1.2.3 IRON-SULFUR CLUSTER BIOSYNTHESIS 7
1.2.4 HEME BIOSYNTHESIS 8
1.2.5 FOLATE METABOLISM 9
1.2.6 COENYZME Q BIOSYNTHESIS 10
1.2.7 TCA CYCLE 11
1.3 MITOCHONDRIAL ELECTRON TRANSPORT CHAIN 15
1.3.1 NADH DEHYDROGENASE 16
1.3.2 DIHYDROOROTATE DEHYDROGENASE 18
1.3.3 SUCCINATE DEHYDROGENASE 19
1.3.4 MALATE DEHYDROGENASE AND MALATE:QUINONE OXIDOREDUCTASE 21
1.3.5 GLYCEROL-3-PHOSPHATE DEHYDROGENASE 23
1.4 AIMS OF THIS STUDY ; 24
2 MATERIAL AND METHODS 26
2.1 MATERIAL 26
2.1.1 BIOLOGICAL RESOURCES 26
2.1.2 LABORATORY EQUIPMENT 26
2.1.3 LABORATORY MATERIAL 27
2.1.3.1 MISCELLANEOUS 27
2.1.3.2 CHEMICALS 27
2.1.4 COMMERCIAL KITS 28
2.1.5 ENZYMES 29
2.1.6 MEDIA 29
2.1.7 STOCK AND WORKING SOLUTIONS 29
2.1.8 BUFFERS 30
IV
HTTP://D-NB.INFO/1043003126
IMAGE 2
2.1.9 ANTIBODIES 30
2.1.10 MOLECULAR CLONING 31
2.1.10.1 PLASMODIUM BERGHEI TRANSFECTION VECTOR 31
2.1.10.2 SOFTWARE AND DATABASES 31
2.2 METHODS 32
2.2.1 MOLECULAR BIOLOGICAL METHODS 32
2.2.1.1 POLYMERASE CHAIN REACTION (PCR) 32
2.2.1.2 COMPLEMENTARY DNA (CDNA) SYNTHESIS BY REVERSE TRANSCRIPTION (RT)
33
2.2.1.3 REAL TIME PCR (RT-PCR) 33
2.2.1.4 AGAROSE GEL ELECTROPHORESIS 33
2.2.1.5 PHENOL-CHLOROFORM EXTRACTION OF DNA 34
2.2.1.6 ETHANOL PRECIPITATION OF DNA 34
2.2.1.7 GEL EXTRACTION OF DNA 34
2.2.1.8 PURIFICATION OF DNA WITH MINELUTE PCR PURIFICATION KIT (QIAGEN)
34
2.2.1.9 QUANTITATION OF DNA BY SPECTROPHOTOMETRY 34
2.2.1.10 PREPARATION OF GDNA FOR SOUTHERN BLOT 34
2.2.1.11 SOUTHERN BLOT 35
2.2.1.12 PREPARATION OF VECTOR AND INSERT 35
2.2.1.13 LIGATION OF DNA FRAGMENTS 35
2.2.1.14 ISOLATION OF PLASMIDS 36
2.2.1.15 SEQUENCING OF PLASMIDS 36
2.2.2 MICROBIOLOGICAL METHODS 36
2.2.2.1 METHODS FOR ESCHERICHIA COLI 36
2.2.2.2 TRANSFORMATION OF ESCHERICHIA COLI (. COLI) 36
2.2.2.3 CULTURING E. COLI ON AGAR PLATES 37
2.2.2.4 CULTURING E. COLI IN LIQUID MEDIUM 37
2.2.2.5 METHODS FOR PLASMODIUM BERGHEI 37
2.2.2.6 SCHIZONT CULTURE 37
2.2.2.7 SCHIZONT ISOLATION 37
2.2.2.8 TRANSFECTION OF P. BERGHEI MEROZOITES BY ELECTROPORATION 38
2.2.2.9 POSITIVE SELECTION OF RECOMBINANT PARASITES 38
2.2.2.10 LONG-TERM STORAGE OF BLOOD STAGE PARASITES 38
2.2.2.11 DETERMINATION OF PARASITEMIA WITH GIEMSA-STAINED BLOOD SMEARS
38
2.2.2.12 PURIFICATION OF BLOOD STAGE PARASITES 38
2.2.2.13 ISOLATION OF PARASITE GENOMIC DNA (GDNA) 39
2.2.2.14 ISOLATION OF PARASITE MESSENGER RNA (MRNA) 39
2.2.2.15 PARASITE CLONING BY LIMITING DILUTION 39
2.2.2.16 QUANTIFICATION OF EXFLAGELLATION CENTRES 39
2.2.2.17 ENRICHMENT AND PURIFICATION OF GAMETOCYTES 40
V
IMAGE 3
2.2.2.18 EXPRESSION PROFILING BY MICROARRAY 40
2.2.2.19 INFECTION OF MOSQUITOES WITH P. BERGHEI 41
2.2.2.20 OOKINETE CULTURE UND PURIFICATION 41
2.2.2.21 OOKINETE MOTILITY ASSAY 42
2.2.2.22 PROPAGATION OF ANOPHELES STEPHENSI MOSQUITOES 42
2.2.2.23 ISOLATION OF MOSQUITO MIDGUTS AND DETERMINATION OF INFECTIVITY
42
2.2.2.24 ISOLATION OF MOSQUITO BLOOD BOLUS 42
2.2.2.25 PREPARATION OF MOSQUITO MIDGUTS FOR TRANSMISSION ELECTRON
MICROSCOPY (TEM) 43
2.2.2.26 TRANSMISSION ELECTRON MICROSCOPY (TEM) ON MIDGUT ASSOCIATED
OOCYSTS 43
2.2.2.27 QUANTIFICATION OF OOCYST NUMBERS AND OCCYST SIZE 43
2.2.2.28 ISOLATION OF MIDGUT AND SALIVARY GLAND SPOROZOITES 43
2.2.2.29 TRANSMISSION OF SPOROZOITES TO MICE 43
2.2.2.30 PROPAGATION OF MAMMALIAN CELLS 44
2.2.2.31 INFECTION OF HUH7 CELLS AND IN VITRO CULTURING OF P. BERGHEI
EXOERYTHROCYTIC FORMS
(EEFS) 44
2.2.2.32 FIXATION OF EEFS 44
2.2.2.33 IMMUNOFLUORESCENCE ASSAY (IFA) ON BLOOD STAGES, OOKINETES,
OOCYSTS, SPOROZOITES
AND EEFS ; 44
2.2.2.34 ANALYSIS OF THE PARASITE MITOCHONDRIAL MEMBRANE POTENTIAL WITH
JC-1 45
2.2.2.35 CO-LOCALISATION STUDIES WITH MITOTRACKER 45
2.2.2.36 QUANTIFICATION OF FUMARATE IN BLOOD STAGE PARASITES 45
3 RESULTS 47
3.1 NADH.QUINONE OXIDOREDUCTASE (NDH2) 47
3.1.1 NDH2 TRANSCRIPTS CAN BE DETECTED THROUGHOUT THE LIFECYCLE 47
3.1.2 NDH2 CAN BE REPLACED WITH AN A/DH2MCHERRY FUSION PROTEIN 47
3.1.3 NDH2 LOCALIZES TO THE MITOCHONDRION 50
3.1.4 NDH2 IS DISPENSABLE IN ASEXUAL BLOOD STAGES 50
3.1.5 DELETION OF NDH2 DOES NOT AFFECT THE EXPRESSION LEVEL OF SELECTED
DEHYDROGENASES IN THE
MITOCHONDRIAL ELECTRON TRANSPORT CHAIN 51
3.1.6 NDH2{-) PARASITES SHOW NORMAL DEVELOPMENT IN BLOOD STAGES 52
3.1.7 NDH2 IS ESSENTIAL FOR COMPLETION OF THE ENTIRE PARASITIC LIFE
CYCLE 53
3.1.8 NDH2 IS DISPENSABLE FOR MOUSE-TO-MOSQUITO HOST SWITCH 54
3.1.9 DELETION OF NDH2 DOES NOT ABOLISH THE MITOCHONDRIAL MEMBRANE
POTENTIAL IN OOKINETES 54
3.1.10 NDH2 DEFICIENT OOKINETES DISPLAY NORMAL MOTILITY IN VITRO 55
3.1.11 NDH2 DEFICIENT PARASITES DO NOT DEVELOP INTO SPOROZOITES 56
3.1.12 NDH2(-) PARASITES SUCCESSFULLY COLONIZE MOSQUITO MIDGUTS 57
3.1.13 ARRESTED OOCYST DEVELOPMENT IN NDH2(-) PARASITES 59
3.1.14 NDH2 IS VITAL FOR MULTIPLE DEVELOPMENTAL PROCESSES DURING OOCYST
MATURATION 60
VI
IMAGE 4
3.1.15 NDH2{-) PARASITES CAN COMPLETE THE LIFE CYCLE WHEN COMPLEMENTED
DURING OOCYST
MATURATION AND SPOROGONY. 62
3.1.16 DETECTION OF HETEROZYGOUS OOCYSTS WITH EPIFLUORESCENCE MICROSCOPY
64
3.1.17 DELETION OF NDH2 DOES NOT CONFER SENSITIVITY TO HDQ 65
3.1.18 DELETION OF NDH2 DOES NOT CONFER RESISTANCE TO THE ARTEMISININ
DERIVATE ARTESUNATE 67
3.2 SUCCINATE DEHYDROGENASE 69
3.2.1 SDH1 AND SDH2 CAN BE TAGGED WITH MCHERRY 69
3.2.2 SDHFRNCHERRY PARASITES SHOW DEFECTIVE OOCYST MATURATION 71
3.2.3 SDH1 AND SDH2 LOCALISE TO THE MITOCHONDRION. 72
3.2.4 SDH1 AND SDH2 ARE DISPENSABLE IN BLOOD STAGES 73
3.2.5 SDH1 AND SDH2 DEFICIENT PARASITES SHOW NORMAL GROWTH IN THE
MAMMALIAN HOST 74
3.2.6 DELETION OF SDH2 DOES NOT CONFER INCREASED CHLOROQUINE SENSITIVITY
75
3.2.7 SDH2 DEFICIENT PARASITES DO NOT DEVELOP SPOROZOITES 76
3.2.8 ABLATION OF SDH1 OR SDH2 LEADS TO DECREASED EXFLAGELLATION OF MALE
GAMETES 77
3.2.9 SDH1 AND SDH2 ARE ESSENTIAL FOR OOCYST DEVELOPMENT 78
3.2.10 SDH2 DEFICIENT OOKINETES INVADE BUT DO NOT TRAVERSE MIDGUT
EPITHELIAL CELLS 80
3.2.11 DELETION OF SDH2(-) RESULTS IN A DECREASE OF FUMARATE IN BLOOD
STAGE PARASITES 83
3.2.12 DELETION OF SDH2 DOES NOT RESULT IN UPREGULATION OF SOD
EXPRESSION 84
3.2.13 MICROARRAY ANALYSIS OF GENE EXPRESSION IN WT AND SDH2(-)
GAMETOCYTES 85
3.2.13.1 DIFFERENTIAL EXPRESSION OF GENES IN SDH2(-) VS WT GAMETOCYTES
85
3.2.13.2 MEMBERS OF THE BIR GENE FAMILY ARE DOWNREGULATED UPON DELETION
OF SDH2 87
3.2.13.3 UPREGULATION OF GENES CODING FOR APICOPLAST PROTEINS IN SDH2(-)
GAMETOCYTES 90
3.2.13.4 TRANSCRIPTIONAL AND TRANSLATIONAL CONTROL IS ALTERED IN SDH2(-)
PARASITES 92
3.3 MALATE:QUINONE OXIDOREDUCTASE AND MALATE DEHYDROGENASE 94
3.3.1 MALATE: QUINONE OXIDOREDUCTASE (MQO) CAN BE TAGGED WITH AN MCHERRY
FUSION PROTEIN _
94
3.3.2 MQO IS LOCALISED TO THE MITOCHONDRION 95
3.3.3 MQO IS NOT ESSENTIAL IN BLOOD STAGES 95
3.3.4 MQO IS ESSENTIAL FOR OOCYST DEVELOPMENT 96
3.3.5 MQO{-) PARASITES CAN BE RESCUED BY WT 97
3.3.6 MALATE DEHYDROGENASE IS NOT ESSENTIAL IN BLOOD STAGES 98
3.3.7 MDH IS NOT ESSENTIAL FOR COMPLETION OF THE PARASITIC LIFE CYCLE 98
3.4 DIHYDROOROTATE DEHYDROGENASE 100
3.4.1 DHOD LOCALIZES TO THE MITOCHONDRION 100
3.4.2 DHOD CAN NOT BE DELETED FROM A BLOOD STAGE PARASITE POPULATION 101
3.5 GLYCEROL-3-PHOSPHATE DEHYDROGENASES 103
3.5.1 LOCALISATION OF THE THREE PLASMODIAL GLYCEROL-3-PHOSPHATATE
DEHYDROGENASES 103
3.5.2 FAD-GPDH IS LOCALISED TO THE MITOCHONDRION 104
VII
IMAGE 5
3.5.3 NAD-GPDH IS A CYTOPLASMIC ENZYME 105
3.5.4 GPDH IS A SPOROZOITE AND LIVER STAGE - SPECIFIC PROTEIN 105
3.5.5 GLYCEROL-3-PHOSPHATE DEHYDROGENASES ARE DISPENSABLE IN BLOOD
STAGES 106
3.5.6 FAD-GPDH AND NAD-GPDH, BUT POSSIBLY NOT GPDH ARE DISPENSABLE
THROUGHOUT THE LIFE
CYCLE 108
DISCUSSION 109
3.6 RELEVANCE OF THE MITETC AS SOURCE OF ATP IN MOSQUITO STAGES 110
3.7 EVIDENCE FOR A GLYCEROL-3-PHOSPHATE SHUTTLE IN P. BERGHEI 111
3.8 APICOPLAST LOCALISATION OF GPDH 112
3.9 TWO MALATE DEHYDROGENASES - INTER- OR INDEPENDENCE? 113
3.10 DHOD - A VALIDATED BUT ENIGMATIC DRUG TARGET 115
3.11 NDH2 - A CASE FOR DRUG TARGET VALIDATION BY REVERSE GENETICS 117
3.12 THE EXAMPLE OF COMPLEX II - THE MITETC AS GUARDIAN OF METABOLIC
HOMEOSTATIS? 118
3.13 CONCLUSION ; ^ 120
REFERENCES 122
SUPPLEMENT 138
ACKNOWLEDGEMENT 139
CURRICULUM VITAE 140
EIDESSTATTLICHE ERKLARUNG 142
VIII
|
| any_adam_object | 1 |
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| dewey-tens | 570 - Biology |
| discipline | Biologie |
| format | Thesis Book |
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| spelling | Boysen, Katja E. 1980- Verfasser (DE-588)1036909026 aut Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain von Katja E. Boysen Berlin 2013 XIV, 142 Seiten Illustrationen, Diagramme txt rdacontent n rdamedia nc rdacarrier Dissertation Humboldt-Universität zu Berlin 2013 (DE-588)4113937-9 Hochschulschrift gnd-content Reproduziert als Boysen, Katja E. Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain Ketsch bei Mannheim : Mikroform Dissertation, 2013 3 Mikrofiches (DE-604)BV041708365 DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=026110001&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Boysen, Katja E. 1980- Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |
| subject_GND | (DE-588)4113937-9 |
| title | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |
| title_auth | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |
| title_exact_search | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |
| title_full | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain von Katja E. Boysen |
| title_fullStr | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain von Katja E. Boysen |
| title_full_unstemmed | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain von Katja E. Boysen |
| title_short | Plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |
| title_sort | plasmodium berghei dehydrogenases in the mitochondrial electron transport chain |
| topic_facet | Hochschulschrift |
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