@phdthesis{Nerlich2007,
  author    = {Nerlich, Annika},
  title     = {Die Rolle der Phosphatidylserin Decarboxylase f{\"u}r die mitochondriale Phospholipid-Biosynthese in Arabidopsis thaliana},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-14522},
  school      = {Universit{\"a}t Potsdam},
  year      = {2007},
  abstract  = {Die durch Phosphatidylserin Decarboxylase (PSD) katalysierte Decarboxylierung von Phosphatidylserin (PS) zu Phosphatidylethanolamin (PE) ist f{\"u}r Mitochondrien in Hefe und M{\"a}usen von essentieller Bedeutung. Im Rahmen der vorliegenden Dissertation wurde erstmals die Rolle dieses PE-Syntheseweges in Pflanzen untersucht. Die drei in Arabidopsis identifizierten PSD Gene atPSD1, atPSD2, atPSD3 codieren f{\"u}r Enzyme, die in Membranen der Mitochondrien (atPSD1), der Tonoplasten (atPSD2) und des Endoplasmatischen Retikulums (atPSD3) lokalisiert sind. Der Beitrag der einzelnen PSDs zur PE-Synthese wurde anhand von psd Null-Mutanten untersucht. Dabei stellte sich atPSD3 als das Enzym mit der h{\"o}chsten Aktivit{\"a}t heraus. Alternativ zum PSD-Weg wird in Arabidopsis PE auch mittels Aminoalkohol-phosphotransferase synthetisiert. Der Verlust der gesamten PSD-Aktivit{\"a}t, wie es in der erzeugten psd Dreifachmutante der Fall ist, wirkt sich ausschließlich auf die Lipidzusammensetzung in der Mitochondrienmembran aus. Demzufolge wird extramitochondriales PE haupts{\"a}chlich {\"u}ber die Aminoalkoholphosphotransferase synthetisiert. Die ver{\"a}nderte Lipidzusammensetzung der Mitochondrienmembran hatte jedoch keinen Einfluss auf die Anzahl, Gr{\"o}ße und Ultrastruktur der Mitochondrien sowie auf das ADP/ATP-Verh{\"a}ltnis und die Respiration. Neben der Bereitstellung von Reduktions{\"a}quivalenten beeinflusst die Funktionalit{\"a}t der Mitochondrien auch die Bildung von Bl{\"u}ten- und Staubbl{\"a}ttern. Diese Bl{\"u}tenorgane waren in der psd Dreifachmutante stark ver{\"a}ndert, und der Bl{\"u}tenph{\"a}notyp {\"a}hnelte der APETALA3-Mutante. Dieses hom{\"o}otische Gen ist f{\"u}r die Ausbildung von Bl{\"u}ten- und Staubbl{\"a}ttern verantwortlich. F{\"u}r die Erzeugung der Mutanten psd2-1 und psd3-1 wurde ein T-DNA Vektor verwendet, der den Promotor des APETALA3 Gens enthielt, welcher in den Mutanten psd2-1, psd3-1 sowie psd2-1psd3-1 und der psd1psd2-1psd3-1 Dreifachmutante eine vergleichbare Co-Suppression des APETALA3 Gens hervorruft. Der Bl{\"u}tenph{\"a}notyp trat jedoch nur in der psd Dreifachmutante auf, da nur in ihr die Kombination von geringen Funktionst{\"o}rungen der Mitochondrien, hervorgerufen durch ver{\"a}nderte Lipidzusammensetzung, mit der Co-Suppression von APETALA3 auftritt.},
  language  = {de}
}
@article{BoboneHilschStormetal.2017,
  author    = {Bobone, Sara and Hilsch, Malte and Storm, Julian and Dunsing, Valentin and Herrmann, Andreas and Chiantia, Salvatore},
  title     = {Phosphatidylserine Lateral Organization Influences the Interaction of Influenza Virus Matrix Protein 1 with Lipid Membranes},
  series = {Journal of virology},
  volume    = {91},
  journal   = {Journal of virology},
  publisher = {American Society for Microbiology},
  address   = {Washington},
  issn      = {0022-538X},
  doi       = {10.1128/JVI.00267-17},
  pages     = {15},
  year      = {2017},
  abstract  = {Influenza A virus matrix protein 1 (M1) is an essential component involved in the structural stability of the virus and in the budding of new virions from infected cells. A deeper understanding of the molecular basis of virion formation and the budding process is required in order to devise new therapeutic approaches. We performed a detailed investigation of the interaction between M1 and phosphatidylserine (PS) (i.e., its main binding target at the plasma membrane [PM]), as well as the distribution of PS itself, both in model membranes and in living cells. To this end, we used a combination of techniques, including Forster resonance energy transfer (FRET), confocal microscopy imaging, raster image correlation spectroscopy, and number and brightness (N\&B) analysis. Our results show that PS can cluster in segregated regions in the plane of the lipid bilayer, both in model bilayers constituted of PS and phosphatidylcholine and in living cells. The viral protein M1 interacts specifically with PS-enriched domains, and such interaction in turn affects its oligomerization process. Furthermore, M1 can stabilize PS domains, as observed in model membranes. For living cells, the presence of PS clusters is suggested by N\&B experiments monitoring the clustering of the PS sensor lactadherin. Also, colocalization between M1 and a fluorescent PS probe suggest that, in infected cells, the matrix protein can specifically bind to the regions of PM in which PS is clustered. Taken together, our observations provide novel evidence regarding the role of PS-rich domains in tuning M1-lipid and M1-M1 interactions at the PM of infected cells. IMPORTANCE Influenza virus particles assemble at the plasma membranes (PM) of infected cells. This process is orchestrated by the matrix protein M1, which interacts with membrane lipids while binding to the other proteins and genetic material of the virus. Despite its importance, the initial step in virus assembly (i.e., M1-lipid interaction) is still not well understood. In this work, we show that phosphatidylserine can form lipid domains in physical models of the inner leaflet of the PM. Furthermore, the spatial organization of PS in the plane of the bilayer modulates M1-M1 interactions. Finally, we show that PS domains appear to be present in the PM of living cells and that M1 seems to display a high affinity for them.},
  language  = {en}
}
@article{KolyvushkoLatzkeDahmanietal.2020,
  author    = {Kolyvushko, Oleksandr and Latzke, Juliane and Dahmani, Ismail and Osterrieder, Nikolaus and Chiantia, Salvatore and Azab, Walid},
  title     = {Differentially-charged liposomes interact with alphaherpesviruses and interfere with virus entry},
  series = {Pathogens},
  volume    = {9},
  journal   = {Pathogens},
  number    = {5},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2076-0817},
  doi       = {10.3390/pathogens9050359},
  pages     = {9},
  year      = {2020},
  abstract  = {Exposure of phosphatidylserine (PS) in the outer leaflet of the plasma membrane is induced by infection with several members of the Alphaherpesvirinae subfamily. There is evidence that PS is used by the equine herpesvirus type 1 (EHV-1) during entry, but the exact role of PS and other phospholipids in the entry process remains unknown. Here, we investigated the interaction of differently charged phospholipids with virus particles and determined their influence on infection. Our data show that liposomes containing negatively charged PS or positively charged DOTAP (N-[1-(2,3-Dioleoyloxy)propyl]-N,N,N-trimethylammonium) inhibited EHV-1 infection, while neutral phosphatidylcholine (PC) had no effect. Inhibition of infection with PS was transient, decreased with time, and was dose dependent. Our findings indicate that both cationic and anionic phospholipids can interact with the virus and reduce infectivity, while, presumably, acting through different mechanisms. Charged phospholipids were found to have antiviral effects and may be used to inhibit EHV-1 infection.},
  language  = {en}
}
@misc{KolyvushkoLatzkeDahmanietal.2020,
  author    = {Kolyvushko, Oleksandr and Latzke, Juliane and Dahmani, Ismail and Osterrieder, Nikolaus and Chiantia, Salvatore and Azab, Walid},
  title     = {Differentially-charged liposomes interact with alphaherpesviruses and interfere with virus entry},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1088},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47189},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-471895},
  pages     = {11},
  year      = {2020},
  abstract  = {Exposure of phosphatidylserine (PS) in the outer leaflet of the plasma membrane is induced by infection with several members of the Alphaherpesvirinae subfamily. There is evidence that PS is used by the equine herpesvirus type 1 (EHV-1) during entry, but the exact role of PS and other phospholipids in the entry process remains unknown. Here, we investigated the interaction of differently charged phospholipids with virus particles and determined their influence on infection. Our data show that liposomes containing negatively charged PS or positively charged DOTAP (N-[1-(2,3-Dioleoyloxy)propyl]-N,N,N-trimethylammonium) inhibited EHV-1 infection, while neutral phosphatidylcholine (PC) had no effect. Inhibition of infection with PS was transient, decreased with time, and was dose dependent. Our findings indicate that both cationic and anionic phospholipids can interact with the virus and reduce infectivity, while, presumably, acting through different mechanisms. Charged phospholipids were found to have antiviral effects and may be used to inhibit EHV-1 infection.},
  language  = {en}
}