@phdthesis{Dahmani2021,
  author    = {Dahmani, Ismail},
  title     = {Influenza A virus matrix protein M1},
  doi       = {10.25932/publishup-52740},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-527409},
  school      = {Universit{\"a}t Potsdam},
  pages     = {XI, 147},
  year      = {2021},
  abstract  = {Influenza A virus (IAV) is a pathogen responsible for severe seasonal epidemics threatening human and animal populations every year. During the viral assembly process in the infected cells, the plasma membrane (PM) has to bend in localized regions into a vesicle towards the extracellular side. Studies in cellular models have proposed that different viral proteins might be responsible for inducing membrane curvature in this context (including M1), but a clear consensus has not been reached. M1 is the most abundant protein in IAV particles. It plays an important role in virus assembly and budding at the PM. M1 is recruited to the host cell membrane where it associates with lipids and other viral proteins. However, the details of M1 interactions with the cellular PM, as well as M1-mediated membrane bending at the budozone, have not been clarified. In this work, we used several experimental approaches to analyze M1-lipids and M1-M1 interactions. By performing SPR analysis, we quantified membrane association for full-length M1 and different genetically engineered M1 constructs (i.e., N- and C-terminally truncated constructs and a mutant of the polybasic region). This allowed us to obtain novel information on the protein regions mediating M1 binding to membranes. By using fluorescence microscopy, cryogenic transmission electron microscopy (cryo-TEM), and three-dimensional (3D) tomography (cryo-ET), we showed that M1 is indeed able to cause membrane deformation on vesicles containing negatively-charged lipids, in the absence of other viral components. Further, sFCS analysis proved that simple protein binding is not sufficient to induce membrane restructuring. Rather, it appears that stable M1-M1 interactions and multimer formation are required to alter the bilayer three-dimensional structure through the formation of a protein scaffold. Finally, to mimic the budding mechanism in cells that arise by the lateral organization of the virus membrane components on lipid raft domains, we created vesicles with lipid domains. Our results showed that local binding of M1 to spatial confined acidic lipids within membrane domains of vesicles led to local M1 inward curvature.},
  language  = {en}
}
@article{WangHuangSachseetal.2016,
  author    = {Wang, Xinxin and Huang, Xianyu and Sachse, Dirk and Hu, Yu and Xue, Jiantao and Meyers, Philip A.},
  title     = {Comparisons of lipid molecular and carbon isotopic compositions in two particle-size fractions from surface peat and their implications for lipid preservation},
  series = {Environmental earth sciences},
  volume    = {75},
  journal   = {Environmental earth sciences},
  publisher = {Springer},
  address   = {New York},
  issn      = {1866-6280},
  doi       = {10.1007/s12665-016-5960-3},
  pages     = {375 -- 385},
  year      = {2016},
  abstract  = {Knowledge of the possible impacts of early diagenesis on lipid biomarkers in geologic settings is important for robust applications of lipid proxies for paleoclimate reconstructions. In this study, molecular distributions and carbon isotopic compositions of lipids were compared in two particle-size fractions (<0.3 mm and >0.3 mm) of twelve surface peat samples collected from Dajiuhu peatland, central China. The average chain length (ACL) values of long-chain n-alkanes, n-fatty alcohols, n-fatty acids and n-alkan-2-ones show no significant differences between the finer and coarser fractions. In contrast, the carbon preference index values of long-chain n-alkanes, n-fatty alcohols and n-alkan-2-ones have relatively smaller values in the finer fractions than in the coarser ones. Stanols were also more abundant in the finer fractions. In addition, the delta C-13 values of odd-numbered n-alkanes (C-23-C-33) were generally less negative in the finer fractions. Our results indicate that (1) the finer fractions probably experienced stronger degradation than the coarser fractions; (2) the less negative delta(CC)-C-13 values of odd-numbered n-alkanes (C-23-C-33) in the finer fractions were largely a result of greater heterotrophic reworking during degradation; (3) ACL values of long-chain n-alkyl lipids (n-alkanes, n-fatty alcohols and n-fatty acids, n-alkan-2-ones) appear to be reliable proxies to trace lipid sources and their associated paleoenvironmental signals in peat deposits.},
  language  = {en}
}