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Life
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Cellular Interactions between Protozoan Pathogens and Hosts
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Cellular Interactions between Protozoan Pathogens and Hosts

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Cell Biology and Tissue Engineering".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 15384

Special Issue Editor

Dr. Mark F. Wiser

E-Mail Website
Guest Editor
Department of Tropical Medicine, Tulane University School of Public Health and Tropical Medicine, New Orleans, LA, USA
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protozoan pathogens are responsible for several important human and animal diseases. Included among these diseases are malaria, African trypanosomiasis, Chagas disease, leishmaniasis, amebiasis, giardiasis, trichomoniasis, toxoplasmosis, cryptosporidiosis, and other coccidioses. Even though protozoa are single-cell eukaryotic organisms, these various pathogenic protozoa are quite distinct from each other in regards to their genetics and cell biology, and many exhibit unique cellular features not found in their hosts. Some of these unique features are highly specialized mechanisms by which they interact with their hosts, and in some cases vectors. These specialized adaptations facilitate infection of the host, survival within the host, and transmission to other hosts. Quite often these interactions involve cell-cell accociations between the protozoan and host via unique structures or proteins, which may also contribute to disease pathogenesis. A better understanding of these host-pathogen interactions at a cellular and molecular levels may facilitate the development of novel therapeutic approaches in treating and controlling these diseases.

This special issue will explore cellular interactions between protozoan pathogens and their hosts. This can include characterization of interactions at the ultrastructural or molecular levels, as well as the genes involved in these interactions. Interactions can include adherence between host and pathogen, modification of the host by the pathogen, or damage to the host caused by the pathogen.

You may choose our Joint Special Issue in Tropical Medicine and Infectious Disease.

Dr. Mark F. Wiser
Guest Editor

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. Life 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 2600 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.

Keywords

  • Protozoa
  • Protozoal disease
  • Host-parasite interaction
  • Adherence
  • Invasion
  • Secretion
  • Receptor-ligand interactions
  • Pathogenesis

Published Papers (4 papers)

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Research

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13 pages, 4367 KiB  
Article
Computational Insights into the Interaction between Cytoadherence Receptor gC1qR and the DBLβ12 Domain of a Plasmodium falciparum PfEMP1 Ligand
by Rowaida Bakri, Mohd Rehan, Hina Shamshad and Abdul Hafiz
Life 2021, 11(9), 993; https://doi.org/10.3390/life11090993 - 21 Sep 2021
Cited by 2 | Viewed by 1850
Abstract
Human receptor gC1qR is a 32 kD protein that mediates the cytoadherence of Plasmodium falciparum-infected erythrocytes (IEs) to human brain microvascular endothelial cells (HBMEC) and platelets. The cytoadherence of IEs to gC1qR has been associated with severe malaria symptoms. The cytoadherence to [...] Read more.
Human receptor gC1qR is a 32 kD protein that mediates the cytoadherence of Plasmodium falciparum-infected erythrocytes (IEs) to human brain microvascular endothelial cells (HBMEC) and platelets. The cytoadherence of IEs to gC1qR has been associated with severe malaria symptoms. The cytoadherence to gC1qR is mediated by the Duffy binding-like β12 (DBLβ12) domain of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), PFD0020c. Here, we report the structural insights into the binding of the DBLβ12 domain of PfEMP1 with the human receptor gC1qR using computational methods. A molecular model of the DBLβ12 domain was generated and used for protein–protein docking with the host receptor gC1qR. The protein–protein docking revealed that the DBLβ12 asymmetrically interacts with two subunits of the gC1qR trimer at the solution face of gC1qR. A total of 21 amino acid residues of DBLβ12 interact with 26 amino acid residues in the gC1qR trimer through 99 nonbonding interactions and 4 hydrogen bonds. Comparative analysis of binding sites on the DBL domain fold for the two receptors gC1qR and ICAM1 showed that the two sites are distinct. This is the first study that provides structural insights into DBLβ12 binding with its receptor gC1qR and may help in designing novel antisevere malaria interventions. Full article
(This article belongs to the Special Issue Cellular Interactions between Protozoan Pathogens and Hosts)
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10 pages, 3811 KiB  
Article
Entamoeba histolytica Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin
by Jesus Pérez-Hernández, Clarisa Retana-González, Espiridión Ramos-Martínez, José Cruz-Colín, Andrés Saralegui-Amaro, Gabriela Baltazar-Rosario, Concepción Gutiérrez-Ruíz, Gerardo Aristi-Urista and Rosario López-Vancell
Life 2021, 11(9), 923; https://doi.org/10.3390/life11090923 - 06 Sep 2021
Cited by 2 | Viewed by 2995
Abstract
Amoebiasis in humans is caused by the protozoan parasite Entamoeba histolytica, which cytotoxic activity has been demonstrated on a wide variety of target cells. The process involves the adherence of the parasite to the cell, and such adherence is mediated by an amoebic [...] Read more.
Amoebiasis in humans is caused by the protozoan parasite Entamoeba histolytica, which cytotoxic activity has been demonstrated on a wide variety of target cells. The process involves the adherence of the parasite to the cell, and such adherence is mediated by an amoebic surface lectin, known as Gal/GalNAc lectin. It is composed of heavy, intermediate, and light subunits. The carbohydrate recognition domain (CRD) has been identified within a cysteine-rich region in the lectin heavy subunit and has an amino acid sequence identity to the receptor-binding domain of hepatocyte growth factor (HGF). Recombinant CRD has been previously shown to compete with HGF for binding to the c-Met receptor IgG fusion protein. In the present study, we searched for evidence of interaction between the Gal/GalNAc lectin at the surface of trophozoites with the c-Met receptor expressed at the surface of HepG2 in coculture assays. Immunoprecipitation of the coculture lysate indicated interaction of the c-Met with a 60 kDa peptide recognized by antiamoebic lectin antibody. Colocalization of both molecules was detected by fluorescence confocal microscopy. Incubation of HepG2 cells with HGF before coculture with trophozoites prevents the cytotoxic effect caused by the parasites but not their adherence to the cells. Our results point to Gal/GalNAc lectin as a ligand of the c-Met receptor at the surface of HepG2 cells. Full article
(This article belongs to the Special Issue Cellular Interactions between Protozoan Pathogens and Hosts)
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Review

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23 pages, 2303 KiB  
Review
Unique Endomembrane Systems and Virulence in Pathogenic Protozoa
by Mark F. Wiser
Life 2021, 11(8), 822; https://doi.org/10.3390/life11080822 - 12 Aug 2021
Cited by 8 | Viewed by 4276
Abstract
Virulence in pathogenic protozoa is often tied to secretory processes such as the expression of adhesins on parasite surfaces or the secretion of proteases to assisted in tissue invasion and other proteins to avoid the immune system. This review is a broad overview [...] Read more.
Virulence in pathogenic protozoa is often tied to secretory processes such as the expression of adhesins on parasite surfaces or the secretion of proteases to assisted in tissue invasion and other proteins to avoid the immune system. This review is a broad overview of the endomembrane systems of pathogenic protozoa with a focus on Giardia, Trichomonas, Entamoeba, kinetoplastids, and apicomplexans. The focus is on unique features of these protozoa and how these features relate to virulence. In general, the basic elements of the endocytic and exocytic pathways are present in all protozoa. Some of these elements, especially the endosomal compartments, have been repurposed by the various species and quite often the repurposing is associated with virulence. The Apicomplexa exhibit the most unique endomembrane systems. This includes unique secretory organelles that play a central role in interactions between parasite and host and are involved in the invasion of host cells. Furthermore, as intracellular parasites, the apicomplexans extensively modify their host cells through the secretion of proteins and other material into the host cell. This includes a unique targeting motif for proteins destined for the host cell. Most notable among the apicomplexans is the malaria parasite, which extensively modifies and exports numerous proteins into the host erythrocyte. These modifications of the host erythrocyte include the formation of unique membranes and structures in the host erythrocyte cytoplasm and on the erythrocyte membrane. The transport of parasite proteins to the host erythrocyte involves several unique mechanisms and components, as well as the generation of compartments within the erythrocyte that participate in extraparasite trafficking. Full article
(This article belongs to the Special Issue Cellular Interactions between Protozoan Pathogens and Hosts)
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23 pages, 7422 KiB  
Review
Mechanisms Associated with Trypanosoma cruzi Host Target Cell Adhesion, Recognition and Internalization
by Oscar Hernán Rodríguez-Bejarano, Catalina Avendaño and Manuel Alfonso Patarroyo
Life 2021, 11(6), 534; https://doi.org/10.3390/life11060534 - 09 Jun 2021
Cited by 7 | Viewed by 5250
Abstract
Chagas disease is caused by the kinetoplastid parasite Trypanosoma cruzi, which is mainly transmitted by hematophagous insect bites. The parasite’s lifecycle has an obligate intracellular phase (amastigotes), while metacyclic and bloodstream-trypomastigotes are its infective forms. Mammalian host cell recognition of the parasite [...] Read more.
Chagas disease is caused by the kinetoplastid parasite Trypanosoma cruzi, which is mainly transmitted by hematophagous insect bites. The parasite’s lifecycle has an obligate intracellular phase (amastigotes), while metacyclic and bloodstream-trypomastigotes are its infective forms. Mammalian host cell recognition of the parasite involves the interaction of numerous parasite and host cell plasma membrane molecules and domains (known as lipid rafts), thereby ensuring internalization by activating endocytosis mechanisms triggered by various signaling cascades in both host cells and the parasite. This increases cytoplasmatic Ca2+ and cAMP levels; cytoskeleton remodeling and endosome and lysosome intracellular system association are triggered, leading to parasitophorous vacuole formation. Its membrane becomes modified by containing the parasite’s infectious form within it. Once it has become internalized, the parasite seeks parasitophorous vacuole lysis for continuing its intracellular lifecycle, fragmenting such a vacuole’s membrane. This review covers the cellular and molecular mechanisms involved in T. cruzi adhesion to, recognition of and internalization in host target cells. Full article
(This article belongs to the Special Issue Cellular Interactions between Protozoan Pathogens and Hosts)
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