scholarly journals Apicortin, a Constituent of Apicomplexan Conoid/Apical Complex and Its Tentative Role in Pathogen—Host Interaction

2021 ◽  
Vol 6 (3) ◽  
pp. 118
Author(s):  
Ferenc Orosz
Keyword(s):  
Plasmodium Falciparum ◽  
Toxoplasma Gondii ◽  
Therapeutic Target ◽  
In Silico ◽  
Free Living ◽  
Binding Properties ◽  
Host Interactions ◽  
Trichoplax Adhaerens ◽  
Host Interaction ◽  
Apical Complex

In 2009, apicortin was identified in silico as a characteristic protein of apicomplexans that also occurs in the placozoa, Trichoplax adhaerens. Since then, it has been found that apicortin also occurs in free-living cousins of apicomplexans (chromerids) and in flagellated fungi. It contains a partial p25-α domain and a doublecortin (DCX) domain, both of which have tubulin/microtubule binding properties. Apicortin has been studied experimentally in two very important apicomplexan pathogens, Toxoplasma gondii and Plasmodium falciparum. It is localized in the apical complex in both parasites. In T. gondii, apicortin plays a key role in shaping the structure of a special tubulin polymer, conoid. In both parasites, its absence or downregulation has been shown to impair pathogen–host interactions. Based on these facts, it has been suggested as a therapeutic target for treatment of malaria and toxoplasmosis.

scholarly journals PHISDetector: a tool to detect diverse in silico phage-host interaction signals for virome studies

2019 ◽  
Author(s):  
Fan Zhang ◽  
Fengxia Zhou ◽  
Rui Gan ◽  
Chunyan Ren ◽  
Yuqiang Jia ◽  
...  
Keyword(s):  
In Silico ◽  
Sequence Composition ◽  
Host Interactions ◽  
Protein Protein Interaction ◽  
Link Type ◽  
Host Interaction ◽  
Therapeutic Development ◽  
One Stop ◽  
Microbe Interactions ◽  
Machine Learning Models

AbstractPhage-microbe interactions not only are appealing systems to study coevolution but also have been increasingly emphasized due to their roles in human health, diseases, and novel therapeutic development. Meanwhile, their interactions leave diverse signals in bacterial and phage genomic sequences, defined as phage-host interaction signals (PHISs), such as sequence composition, CRISPR targeting, prophage, and protein-protein interaction signals. We infer that proper detection and integration of these diverse PHISs will allow us to predict phage-host interactions. Here, we developed PHISDetector, a novel tool to predict phage-host interactions by detecting and integrating diverse in silico PHISs and scoring the probability of phage-host interactions using machine-learning models based on PHIS features. PHISDetector is available as a one-stop web service version for general users to study individual inputs. A stand-alone software version is also provided to process massive phage contigs from virome studies. PHISDetector is freely available at http://www.microbiome-bigdata.com/PHISDetector/ and https://github.com/HIT-ImmunologyLab/PHISDector.

scholarly journals PHISDetector: a tool to detect diverse in  silico  phage-host interaction signals for virome studies

2020 ◽  
Author(s):  
Fengxia Zhou ◽  
Rui Gan ◽  
Fan Zhang ◽  
Chunyan Ren ◽  
Ling Yu ◽  
...  
Keyword(s):  
In Silico ◽  
Interaction Patterns ◽  
Detection Range ◽  
Sequence Composition ◽  
Host Interactions ◽  
Protein Protein Interaction ◽  
Host Interaction ◽  
Essential Questions ◽  
Therapeutic Development ◽  
User Friendly

Abstract Background: Phage-host interaction is one of the essential questions in microbial environments. These interactions not only are appealing systems to study coevolution but also have been increasingly emphasized due to their roles in human health, diseases, and novel therapeutic development. Meanwhile, molecular and ecological co-evolutionary processes of phages and microbe leave signals in their genomic sequences, defined as phage-host interaction signals (PHISs) in this study, which allow us to predict microbe-phage interactions in silico . Results: We developed PHISDetector, which utilizes sophisticated bioinformatics methods to detect comprehensive in silico PHISs, including sequence composition, CRISPR targeting, prophage, and protein-protein interaction signals, further systematically integrates various categories of PHISs, and carries out machine-learning modeling to predict phage-host interactions. PHISDetector captures phage-host associations in a data-driven manner and reflects various phage-microbe interaction patterns or mechanisms so that users can easily compare the results from different approaches to better understand phage-microbe coevolution. We present it as a software pipeline for phage-host interaction identification, annotation and analysis in a comprehensive and user-friendly manner. PHISDetector can be run either as a web-server (http://www.microbiome-bigdata.com/PHISDetector/) or as a stand-alone version especially designed for virome studies.Conclusions: PHISDetector is a unique tool capable of incorporating all five categories of PHISs for comprehensive prediction of global phage-host interactions. PHISDetector outperforms currently available tools which are limited by accuracy, effective detection range, types of interacting signals, and the capability to apply for high-throughput virome studies.

In silico assessment of kinetics and state dependent binding properties of drugs causing acquired LQTS

2016 ◽  
Vol 120 (1-3) ◽  
pp. 89-99 ◽  
Author(s):  
William Lee ◽  
Stefan A. Mann ◽  
Monique J. Windley ◽  
Mohammad S. Imtiaz ◽  
Jamie I. Vandenberg ◽  
...  
Keyword(s):  
In Silico ◽  
Binding Properties ◽  
State Dependent

Actomyosin motor in the merozoite of the malaria parasite, Plasmodium falciparum: implications for red cell invasion

1998 ◽  
Vol 111 (13) ◽  
pp. 1831-1839 ◽  
Author(s):  
J.C. Pinder ◽  
R.E. Fowler ◽  
A.R. Dluzewski ◽  
L.H. Bannister ◽  
F.M. Lavin ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Toxoplasma Gondii ◽  
Malaria Parasite ◽  
Cellular Protein ◽  
Red Cell ◽  
Parasite Protein ◽  
Ionic Detergent ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

The genome of the malaria parasite, Plasmodium falciparum, contains a myosin gene sequence, which bears a close homology to one of the myosin genes found in another apicomplexan parasite, Toxoplasma gondii. A polyclonal antibody was generated against an expressed polypeptide of molecular mass 27,000, based on part of the deduced sequence of this myosin. The antibody reacted with the cognate antigen and with a component of the total parasite protein on immunoblots, but not with vertebrate striated or smooth muscle myosins. It did, however, recognise two components in the cellular protein of Toxoplasma gondii. The antibody was used to investigate stage-specificity of expression of the myosin (here designated Pf-myo1) in P. falciparum. The results showed that the protein is synthesised in mature schizonts and is present in merozoites, but vanishes after the parasite enters the red cell. Pf-myo1 was found to be largely, though not entirely, associated with the particulate parasite cell fraction and is thus presumably mainly membrane bound. It was not solubilised by media that would be expected to dissociate actomyosin or myosin filaments, or by non-ionic detergent. Immunofluorescence revealed that in the merozoite and mature schizont Pf-myo1 is predominantly located around the periphery of the cell. Immuno-gold electron microscopy also showed the presence of the myosin around almost the entire parasite periphery, and especially in the region surrounding the apical prominence. Labelling was concentrated under the plasma membrane but was not seen in the apical prominence itself. This suggests that Pf-myo1 is associated with the plasma membrane or with the outer membrane of the subplasmalemmal cisterna, which forms a lining to the plasma membrane, with a gap at the apical prominence. The results lead to a conjectural model of the invasion mechanism.

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