Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
6.4
4.5
Journals
Microorganisms
Special Issues
Plasmodium falciparum: Host-Parasite Interaction
share announcement

Plasmodium falciparum: Host-Parasite Interaction

A special issue of Microorganisms (ISSN 2076-2607). This special issue belongs to the section "Parasitology".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 13600

Special Issue Editors

Prof. Dr. Iris Bruchhaus

E-Mail Website
Guest Editor
Bernhard Nocht Institute for Tropical Medicine, 20359 Hamburg, Germany
Interests: Plasmodium falciparum; Entamoeba histolytica; parasitology; pathogenicity; host-parasite interaction; cell biology; gene expression; pathogenicity factors; peptidases
Dr. Nahla Galal Metwally

E-Mail Website
Guest Editor
Bernhard Nocht Institute for Tropical Medicine, 20359 Hamburg, Germany
Interests: Plasmodium falciparum; NGS; mRNA; miRNA; extracellular vesicles; endothelial cells; bioinformatics; parasitology; immunology and host-parasite interactions

Special Issue Information

Dear Colleagues,

Despite great progress through control programs, malaria remains one of the most important infectious diseases with about 400,000 deaths per year. The complications caused by malaria infection are multifactorial in origin; both the parasite and the host contribute. Of central importance is the cytoadhesion of erythrocytes infected with Plasmodium falciparum to endothelial cell receptors of the vessels of vital organs. In addition to blocking the capillaries, endothelial dysfunction and inflammation occur in the affected tissue. In order to enable new therapeutic approaches, it is, therefore, of great importance to understand in detail the interaction between the parasite Plasmodium falciparum and its human host.

This Special Issue of Microorganisms invites researchers to present recent reviews and new original research on "Plasmodium falciparum: Host-Parasite Interaction", including pathogenicity, parasitology, immunology, cell biology and gene expression.

Excellent submissions on other species of malaria parasites are also welcome in this special edition.

Prof. Dr. Iris Bruchhaus
Dr. Nahla Galal Metwally
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Microorganisms is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (5 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

21 pages, 4305 KiB  
Article
Arsinothricin Inhibits Plasmodium falciparum Proliferation in Blood and Blocks Parasite Transmission to Mosquitoes
by Masafumi Yoshinaga, Guodong Niu, Kunie Yoshinaga-Sakurai, Venkadesh S. Nadar, Xiaohong Wang, Barry P. Rosen and Jun Li
Microorganisms 2023, 11(5), 1195; https://doi.org/10.3390/microorganisms11051195 - 03 May 2023
Viewed by 3077
Abstract
Malaria, caused by Plasmodium protozoal parasites, remains a leading cause of morbidity and mortality. The Plasmodium parasite has a complex life cycle, with asexual and sexual forms in humans and Anopheles mosquitoes. Most antimalarials target only the symptomatic asexual blood stage. However, to [...] Read more.
Malaria, caused by Plasmodium protozoal parasites, remains a leading cause of morbidity and mortality. The Plasmodium parasite has a complex life cycle, with asexual and sexual forms in humans and Anopheles mosquitoes. Most antimalarials target only the symptomatic asexual blood stage. However, to ensure malaria eradication, new drugs with efficacy at multiple stages of the life cycle are necessary. We previously demonstrated that arsinothricin (AST), a newly discovered organoarsenical natural product, is a potent broad-spectrum antibiotic that inhibits the growth of various prokaryotic pathogens. Here, we report that AST is an effective multi-stage antimalarial. AST is a nonproteinogenic amino acid analog of glutamate that inhibits prokaryotic glutamine synthetase (GS). Phylogenetic analysis shows that Plasmodium GS, which is expressed throughout all stages of the parasite life cycle, is more closely related to prokaryotic GS than eukaryotic GS. AST potently inhibits Plasmodium GS, while it is less effective on human GS. Notably, AST effectively inhibits both Plasmodium erythrocytic proliferation and parasite transmission to mosquitoes. In contrast, AST is relatively nontoxic to a number of human cell lines, suggesting that AST is selective against malaria pathogens, with little negative effect on the human host. We propose that AST is a promising lead compound for developing a new class of multi-stage antimalarials. Full article
(This article belongs to the Special Issue Plasmodium falciparum: Host-Parasite Interaction)
►▼ Show Figures

Figure 1

22 pages, 6026 KiB  
Article
Identification of Exported Plasmodium falciparum Proteins That Bind to the Erythrocyte Cytoskeleton
by Bikash Shakya, Geoffrey Kimiti Kilili, Ling Wang, Ernesto S. Nakayasu and Douglas J. LaCount
Microorganisms 2022, 10(7), 1438; https://doi.org/10.3390/microorganisms10071438 - 16 Jul 2022
Cited by 1 | Viewed by 1985
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Plasmodium falciparum: Host-Parasite Interaction)
►▼ Show Figures

Figure 1

25 pages, 3014 KiB  
Article
Plasmodium falciparum S-Adenosylmethionine Synthetase Is Essential for Parasite Survival through a Complex Interaction Network with Cytoplasmic and Nuclear Proteins
by Jean Pierre Musabyimana, Ute Distler, Juliane Sassmannshausen, Christina Berks, Janice Manti, Sandra Bennink, Lea Blaschke, Paul-Christian Burda, Ansgar Flammersfeld, Stefan Tenzer, Che Julius Ngwa and Gabriele Pradel
Microorganisms 2022, 10(7), 1419; https://doi.org/10.3390/microorganisms10071419 - 14 Jul 2022
Cited by 5 | Viewed by 3001
Abstract
S-adenosylmethionine synthetase (SAMS) is a key enzyme for the synthesis of the lone methyl donor S-adenosyl methionine (SAM), which is involved in transmethylation reactions and hence required for cellular processes such as DNA, RNA, and histone methylation, but also polyamine biosynthesis and proteostasis. [...] Read more.
S-adenosylmethionine synthetase (SAMS) is a key enzyme for the synthesis of the lone methyl donor S-adenosyl methionine (SAM), which is involved in transmethylation reactions and hence required for cellular processes such as DNA, RNA, and histone methylation, but also polyamine biosynthesis and proteostasis. In the human malaria parasite Plasmodium falciparum, PfSAMS is encoded by a single gene and has been suggested to be crucial for malaria pathogenesis and transmission; however, to date, PfSAMS has not been fully characterized. To gain deeper insight into the function of PfSAMS, we generated a conditional gene knockdown (KD) using the glmS ribozyme system. We show that PfSAMS localizes to the cytoplasm and the nucleus of blood-stage parasites. PfSAMS-KD results in reduced histone methylation and leads to impaired intraerythrocytic growth and gametocyte development. To further determine the interaction network of PfSAMS, we performed a proximity-dependent biotin identification analysis. We identified a complex network of 1114 proteins involved in biological processes such as cell cycle control and DNA replication, or transcription, but also in phosphatidylcholine and polyamine biosynthesis and proteasome regulation. Our findings highlight the diverse roles of PfSAMS during intraerythrocytic growth and sexual stage development and emphasize that PfSAMS is a potential drug target. Full article
(This article belongs to the Special Issue Plasmodium falciparum: Host-Parasite Interaction)
►▼ Show Figures

Figure 1

17 pages, 4157 KiB  
Article
Ectopic Expression of Plasmodium vivax vir Genes in P. falciparum Affects Cytoadhesion via Increased Expression of Specific var Genes
by Torben Rehn, Pedro Lubiana, Thi Huyen Trang Nguyen, Eva Pansegrau, Marius Schmitt, Lisa Katharina Roth, Jana Brehmer, Thomas Roeder, Dániel Cadar, Nahla Galal Metwally and Iris Bruchhaus
Microorganisms 2022, 10(6), 1183; https://doi.org/10.3390/microorganisms10061183 - 09 Jun 2022
Cited by 3 | Viewed by 1864
Abstract
Plasmodium falciparum-infected erythrocytes (PfIEs) adhere to endothelial cell receptors (ECRs) of blood vessels mainly via PfEMP1 proteins to escape elimination via the spleen. Evidence suggests that P. vivax-infected reticulocytes (PvIRs) also bind to ECRs, presumably enabled [...] Read more.
Plasmodium falciparum-infected erythrocytes (PfIEs) adhere to endothelial cell receptors (ECRs) of blood vessels mainly via PfEMP1 proteins to escape elimination via the spleen. Evidence suggests that P. vivax-infected reticulocytes (PvIRs) also bind to ECRs, presumably enabled by VIR proteins, as shown by inhibition experiments and studies with transgenic P. falciparum expressing vir genes. To test this hypothesis, our study investigated the involvement of VIR proteins in cytoadhesion using vir gene-expressing P. falciparum transfectants. Those VIR proteins with a putative transmembrane domain were present in Maurer’s clefts, and some were also present in the erythrocyte membrane. The VIR protein without a transmembrane domain (PVX_050690) was not exported. Five of the transgenic P. falciparum cell lines, including the one expressing PVX_050690, showed binding to CD36. We observed highly increased expression of specific var genes encoding PfEMP1s in all CD36-binding transfectants. These results suggest that ectopic vir expression regulates var expression through a yet unknown mechanism. In conclusion, the observed cytoadhesion of P. falciparum expressing vir genes depended on PfEMP1s, making this experimental unsuitable for characterizing VIR proteins. Full article
(This article belongs to the Special Issue Plasmodium falciparum: Host-Parasite Interaction)
►▼ Show Figures

Figure 1

Review

Jump to: Research

16 pages, 3406 KiB  
Review
CD36—A Host Receptor Necessary for Malaria Parasites to Establish and Maintain Infection
by Anna Bachmann, Nahla Galal Metwally, Johannes Allweier, Jakob Cronshagen, Maria del Pilar Martinez Tauler, Agnes Murk, Lisa Katharina Roth, Hanifeh Torabi, Yifan Wu, Thomas Gutsmann and Iris Bruchhaus
Microorganisms 2022, 10(12), 2356; https://doi.org/10.3390/microorganisms10122356 - 29 Nov 2022
Cited by 5 | Viewed by 1917
Abstract
Plasmodium falciparum-infected erythrocytes (PfIEs) present P. falciparum erythrocyte membrane protein 1 proteins (PfEMP1s) on the cell surface, via which they cytoadhere to various endothelial cell receptors (ECRs) on the walls of human blood vessels. This prevents the parasite [...] Read more.
Plasmodium falciparum-infected erythrocytes (PfIEs) present P. falciparum erythrocyte membrane protein 1 proteins (PfEMP1s) on the cell surface, via which they cytoadhere to various endothelial cell receptors (ECRs) on the walls of human blood vessels. This prevents the parasite from passing through the spleen, which would lead to its elimination. Each P. falciparum isolate has about 60 different PfEMP1s acting as ligands, and at least 24 ECRs have been identified as interaction partners. Interestingly, in every parasite genome sequenced to date, at least 75% of the encoded PfEMP1s have a binding domain for the scavenger receptor CD36 widely distributed on host endothelial cells and many other cell types. Here, we discuss why the interaction between PfIEs and CD36 is optimal to maintain a finely regulated equilibrium that allows the parasite to multiply and spread while causing minimal harm to the host in most infections. Full article
(This article belongs to the Special Issue Plasmodium falciparum: Host-Parasite Interaction)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-5
Back to TopTop