A Study of Multiband Indoor Radio Distribution System

The mobile indoor traffic are increasing exponentially which is the current challenge inindoor coverage and design for most of the researchers and business companies todevelop further. There are different trade-off to provide different indoor services withthe use of different repeater system, distributed antenna network (active and passive),macro cells indoor penetrations and many more. As the use of energy effective materialsfor construction of buildings have made a blockage of RF signals from macro cells,usually a separate installations are done to provide indoor coverage for differentservices such as TRTRA, GSM, UNTS, LTE and WLAN in indoor environments forlarge campuses, industrial complex, sports arena, tunnels and office buildings. Thisseparate installations increases the cost, installation space and time which can be solvedusing the same infrastructure to provide multiple of mobile indoor solutions using smartintegrated solutions where many mobile services can be distributed indoor using thesame distributed antenna network using active and passive networks.This thesis investigates the advantage and disadvantage of different types of active andpassive distributed antenna system with the integrated antenna network to compare thecoverage and cost analysis. The coverage analysis was done to compare the RSSI levelby adding different frequency bands into the indoor network for both active and passiveDAS design. Different types of sample design model was used to verify the coverageanalysis. It can be seen from the coverage analysis that an integrated system with all inone solution also has a better coverage compared to typical active and passive designwhich can be used in future in building design as One Net Solution. Also the costanalysis was done for both CAPEX and OPEX to find the cost estimation for differentindoor models. It showed that the integrated solution is the most expensive solution butif it has a case of large design venues, then integrate active solution can be the onlysolutions. Passive design cannot cover large scale areas. It is suitable only for small andmedium sized venues

Understanding Anchoring of Plasmodium Falciparum Exported Proteins to the Erythrocyte Cytoskeleton and Investigating Their Function

Plasmodium falciparum causes the most severe form of human malaria and is responsible for most malaria-associated deaths. In 2015, about 214 million cases of malaria occurred worldwide, killing 438,000 people, mostly children. The remodeling of parasite-infected red blood cells contributes to the pathogenesis of falciparum malaria. P. falciparum extensively modifies the infected red blood cell (iRBC), resulting in changes in iRBC deformability, shape and surface properties. These alterations suggest that the red blood cell (RBC) cytoskeleton is a major target for modifications during infection. These modifications are attributed to the actions of hundreds of proteins that are exported by the parasite to iRBC. However, the cytoskeletal binding partners of most of these exported proteins are not known. This dissertation summarizes the findings from the studies designed to identify and investigate protein-protein interactions between P. falciparum exported proteins and erythrocyte cytoskeletal proteins. A large-scale screening using the split luciferase assay was performed to identify the cytoskeletal targets of twenty-four parasite-exported proteins, which yielded cytoskeletal binding partners for 15 parasite proteins. In total, 56 interactions were identified between 15 parasite proteins and 14 RBC cytoskeletal protein fragments. Seventeen of the above interactions were confirmed using protein co-precipitation assays. The polyhelical interspersed subtelomeric (PHIST) domain-containing proteins (PFD0090c, PF14_0018, MAL8P1.163 and PFD0095c) interacted with both ankyrin 1 (ANK1) and band 4.1 (4.1R). Out of these four proteins, PF14_0018 and PFD0095c also contained the MESA erythrocyte cytoskeletal (MEC) binding motif. These MEC motif proteins including MESA and PF10_0381 targeted the ANK1 fragment composed of spectrin binding domain. Yeast two hybrid assays and split-luciferase assays were used to investigate the minimum-binding region of MESA and PF14_0018. The MEC motif was sufficient for the interaction of MESA and PF14_0018 with the ANK1 fragment and in absence of the MEC motifs, the interactions were obliterated. Similarly, protein co-purification assays were used to identify the minimum-binding domain of ANK1 repeats targeted by parasite proteins. I found that the parasite proteins that targeted the ANK1 repeats interacted with D2 subdomain of the ANK1 repeats, suggesting that the interaction may disrupt the interaction between ANK1 and band 3 in the iRBC membrane. In order to assess the role of parasite proteins in host cell rigidity, I performed microsphiltration assays by loading erythrocyte ghosts with the parasite proteins and testing their retention rate in a matrix composed of metal beads. Ghost erythrocytes loaded with RESA, PF14_0018 and PFD0090c were retained at a significantly higher rate than control samples, suggesting the possible role of these parasite proteins in host cell rigidity. In summary, the research reported in this thesis identified and characterized protein-protein interactions between P. falciparum exported proteins and erythrocyte cytoskeletal proteins and began to define their roles in altering host cell rigidity

Identification of Exported <i>Plasmodium falciparum</i> Proteins That Bind to the Erythrocyte Cytoskeleton

Plasmodium proteins are exported to the erythrocyte cytoplasm to create an environment that supports parasite replication. Although hundreds of proteins are predicted to be exported through Plasmodium export element (PEXEL)-dependent and -independent mechanisms, the functions of exported proteins are largely uncharacterized. In this study, we used a biochemical screening approach to identify putative exported P. falciparum proteins that bound to inside-out vesicles prepared from erythrocytes. Out of 69 P. falciparum PEXEL-motif proteins tested, 18 bound to inside-out vesicles (IOVs) in two or more independent assays. Using co-affinity purifications followed by mass spectrometry, pairwise co-purification experiments, and the split-luciferase assay, we identified 31 putative protein–protein interactions between erythrocyte cytoskeletal proteins and predicted exported P. falciparum proteins. We further showed that PF3D7_1401600 binds to the spectrin-binding domain of erythrocyte ankyrin via its MESA erythrocyte cytoskeleton binding (MEC) motif and to the N-terminal domains of ankyrin and 4.1R through a fragment that required an intact Plasmodium helical interspersed sub-telomeric (PHIST) domain. Introduction of PF3D7_1401600 into erythrocyte ghosts increased retention in the microsphiltration assay, consistent with previous data that reported a reduction of rigidity in red blood cells infected with PF3D7_1401600-deficient parasites

Multiparametric biophysical profiling of red blood cells in malaria infection

Deshmukh et al. combine microscale magnetic levitation with minute density and magnetic susceptibility differences to enhance biophysical separation of cells. They demonstrate the feasibility of this approach on cells infected with malaria parasites, which simultaneously decrease host cell density and increase its magnetic susceptibility

Multiparametric biophysical profiling of red blood cells in malaria infection.

Biophysical separation promises label-free, less-invasive methods to manipulate the diverse properties of live cells, such as density, magnetic susceptibility, and morphological characteristics. However, some cellular changes are so minute that they are undetectable by current methods. We developed a multiparametric cell-separation approach to profile cells with simultaneously changing density and magnetic susceptibility. We demonstrated this approach with the natural biophysical phenomenon of Plasmodium falciparum infection, which modifies its host erythrocyte by simultaneously decreasing density and increasing magnetic susceptibility. Current approaches have used these properties separately to isolate later-stage infected cells, but not in combination. We present biophysical separation of infected erythrocytes by balancing gravitational and magnetic forces to differentiate infected cell stages, including early stages for the first time, using magnetic levitation. We quantified height distributions of erythrocyte populations-27 ring-stage synchronized samples and 35 uninfected controls-and quantified their unique biophysical signatures. This platform can thus enable multidimensional biophysical measurements on unique cell types