scholarly journals Homology-Based Prediction of Potential Protein-Protein Interactions between Human Erythrocytes and Plasmodium falciparum

2015 ◽  
Vol 9 ◽  
pp. BBI.S31880 ◽  
Author(s):  
Gayatri Ramakrishnan ◽  
Narayanaswamy Srinivasan ◽  
Ponnan Padmapriya ◽  
Vasant Natarajan
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Interactions ◽  
Laboratory Experiments ◽  
Host Cells ◽  
Interacting Proteins ◽  
Protein Protein Interactions ◽  
Parasite Protein ◽  
Obligate Intracellular ◽  
Host Parasite Interactions ◽  
Host Parasite

Plasmodium falciparum, a causative agent of malaria, is a well-characterized obligate intracellular parasite known for its ability to remodel host cells, particularly erythrocytes, to successfully persist in the host environment. However, the current levels of understanding from the laboratory experiments on the host-parasite interactions and the strategies pursued by the parasite to remodel host erythrocytes are modest. Several computational means developed in the recent past to predict host-parasite/pathogen interactions have generated testable hypotheses on feasible protein-protein interactions. We demonstrate the utility of protein structure-based protocol in the recognition of potential interacting proteins across P. falciparum and host erythrocytes. In concert with the information on the expression and subcellular localization of host and parasite proteins, we have identified 208 biologically feasible interactions potentially brought about by 59 P. falciparum and 30 host erythrocyte proteins. For selected cases, we have evaluated the physicochemical viability of the predicted interactions in terms of surface complementarity, electrostatic complementarity, and interaction energies at protein interface regions. Such careful inspection of molecular and mechanistic details generates high confidence on the predicted host-parasite protein-protein interactions. The predicted host-parasite interactions generate many experimentally testable hypotheses that can contribute to the understanding of possible mechanisms undertaken by the parasite in host erythrocyte remodeling. Thus, the key protein players recognized in P. falciparum can be explored for their usefulness as targets for chemotherapeutic intervention.

scholarly journals The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking

2003 ◽  
Vol 162 (2) ◽  
pp. 317-327 ◽  
Author(s):  
Tim-Wolf Gilberger ◽  
Jennifer K. Thompson ◽  
Michael B. Reed ◽  
Robert T. Good ◽  
Alan F. Cowman
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Protein Interactions ◽  
Protein Trafficking ◽  
Cytoplasmic Domain ◽  
Specific Protein ◽  
Host Cells ◽  
Protein Protein Interactions ◽  
Parasite Plasmodium Falciparum ◽  
Erythrocyte Binding

The invasion of host cells by the malaria parasite Plasmodium falciparum requires specific protein–protein interactions between parasite and host receptors and an intracellular translocation machinery to power the process. The transmembrane erythrocyte binding protein-175 (EBA-175) and thrombospondin-related anonymous protein (TRAP) play central roles in this process. EBA-175 binds to glycophorin A on human erythrocytes during the invasion process, linking the parasite to the surface of the host cell. In this report, we show that the cytoplasmic domain of EBA-175 encodes crucial information for its role in merozoite invasion, and that trafficking of this protein is independent of this domain. Further, we show that the cytoplasmic domain of TRAP, a protein that is not expressed in merozoites but is essential for invasion of liver cells by the sporozoite stage, can substitute for the cytoplasmic domain of EBA-175. These results show that the parasite uses the same components of its cellular machinery for invasion regardless of the host cell type and invasive form.

Protein-Protein Interactions in the Tetraspanin Web

Physiology ◽  
2005 ◽  
Vol 20 (4) ◽  
pp. 218-224 ◽  
Author(s):  
Shoshana Levy ◽  
Tsipi Shoham
Keyword(s):  
Signal Transduction ◽  
Cell Proliferation ◽  
Protein Interactions ◽  
Membrane Microdomains ◽  
Protein Protein Interactions ◽  
Host Parasite Interactions ◽  
Evolutionarily Conserved ◽  
And Migration ◽  
Host Parasite ◽  
Partner Proteins

Tetraspanins are evolutionarily conserved membrane proteins that tend to associate laterally with one another and to cluster dynamically with numerous partner proteins in membrane microdomains. Consequently, members of this family are involved in the coordination of intracellular and intercellular processes, including signal transduction; cell proliferation, adhesion, and migration; cell fusion; and host-parasite interactions.

scholarly journals Cerebral malaria: insights from host-parasite protein-protein interactions

2010 ◽  
Vol 9 (1) ◽  
Author(s):  
Aditya Rao ◽  
Mayil K Kumar ◽  
Thomas Joseph ◽  
Gopalakrishnan Bulusu
Keyword(s):  
Cerebral Malaria ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Parasite Protein ◽  
Host Parasite

scholarly journals Sex-based differences in clearance of chronic Plasmodium falciparum infection

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Jessica Briggs ◽  
Noam Teyssier ◽  
Joaniter I Nankabirwa ◽  
John Rek ◽  
Prasanna Jagannathan ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Host Response ◽  
Behavioral Risk ◽  
Biological Sex ◽  
Force Of Infection ◽  
Host Parasite Interactions ◽  
Infection Event ◽  
Asymptomatic Infections ◽  
Host Parasite ◽  
Eastern Uganda

Multiple studies have reported a male bias in incidence and/or prevalence of malaria infection in males compared to females. To test the hypothesis that sex-based differences in host-parasite interactions affect the epidemiology of malaria, we intensively followed Plasmodium falciparum infections in a cohort in a malaria endemic area of eastern Uganda and estimated both force of infection (FOI) and rate of clearance using amplicon deep-sequencing. We found no evidence of differences in behavioral risk factors, incidence of malaria, or FOI by sex. In contrast, females cleared asymptomatic infections at a faster rate than males (hazard ratio [HR]=1.82, 95% CI 1.20 to 2.75 by clone and HR = 2.07, 95% CI 1.24 to 3.47 by infection event) in multivariate models adjusted for age, timing of infection onset, and parasite density. These findings implicate biological sex-based differences as an important factor in the host response to this globally important pathogen.

Receptor-ligand and parasite protein-protein interactions inPlasmodium vivax: Analysing rhoptry neck proteins 2 and 4

2018 ◽  
Vol 20 (7) ◽  
pp. e12835 ◽  
Author(s):  
Maritza Bermúdez ◽  
Gabriela Arévalo-Pinzón ◽  
Laura Rubio ◽  
Olivier Chaloin ◽  
Sylviane Muller ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Parasite Protein ◽  
Receptor Ligand

scholarly journals The Coupling Protein Cagβ and Its Interaction Partner CagZ Are Required for Type IV Secretion of the Helicobacter pylori CagA Protein

2010 ◽  
Vol 78 (12) ◽  
pp. 5244-5251 ◽  
Author(s):  
Angela Jurik ◽  
Elisabeth Haußer ◽  
Stefan Kutter ◽  
Isabelle Pattis ◽  
Sandra Praßl ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Host Cell ◽  
Protein Interactions ◽  
Translocation Factor ◽  
Type Iv Secretion ◽  
Host Cells ◽  
Protein Protein Interactions ◽  
Type Iv ◽  
Coupling Protein ◽  
Translocation Factors

ABSTRACT Bacterial type IV secretion systems are macromolecule transporters with essential functions for horizontal gene transfer and for symbiotic and pathogenic interactions with eukaryotic host cells. Helicobacter pylori, the causative agent of type B gastritis, peptic ulcers, gastric adenocarcinoma, and mucosa-associated lymphoid tissue (MALT) lymphoma, uses the Cag type IV secretion system to inject its effector protein CagA into gastric cells. This protein translocation results in altered host cell gene expression profiles and cytoskeletal rearrangements, and it has been linked to cancer development. Interactions of CagA with host cell proteins have been studied in great detail, but little is known about the molecular details of CagA recognition as a type IV secretion substrate or of the translocation process. Apart from components of the secretion apparatus, we previously identified several CagA translocation factors that are either required for or support CagA translocation. To identify protein-protein interactions between these translocation factors, we used a yeast two-hybrid approach comprising all cag pathogenicity island genes. Among several other interactions involving translocation factors, we found a strong interaction between the coupling protein homologue Cagβ (HP0524) and the Cag-specific translocation factor CagZ (HP0526). We show that CagZ has a stabilizing effect on Cagβ, and we demonstrate protein-protein interactions between the cytoplasmic part of Cagβ and CagA and between CagZ and Cagβ, using immunoprecipitation and pull-down assays. Together, our data suggest that these interactions represent a substrate-translocation factor complex at the bacterial cytoplasmic membrane.

scholarly journals Plasmodium falciparum STEVOR Proteins Are Highly Expressed in Patient Isolates and Located in the Surface Membranes of Infected Red Blood Cells and the Apical Tips of Merozoites

2008 ◽  
Vol 76 (7) ◽  
pp. 3329-3336 ◽  
Author(s):  
Jane E. Blythe ◽  
Xue Yan Yam ◽  
Claudia Kuss ◽  
Zbynek Bozdech ◽  
Anthony A. Holder ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Multigene Family ◽  
Blood Cells ◽  
Antigenic Variation ◽  
Human Parasite ◽  
Host Parasite Interactions ◽  
Maurer's Clefts ◽  
Host Parasite ◽  
Family Code

ABSTRACT The human parasite Plasmodium falciparum has the potential to express a vast repertoire of variant proteins on the surface of the infected red blood cell (iRBC). Variation in the expression pattern of these proteins is linked to antigenic variation and thereby evasion of host antibody-mediated immunity. The genes in the stevor multigene family code for small variant antigens that are expressed in blood-stage parasites where they can be detected in membranous structures called Maurer's clefts (MC). Some studies have indicated that STEVOR protein may also be trafficked to the iRBC membrane. To address the location of STEVOR protein in more detail, we have analyzed expression in several cultured parasite lines and in parasites obtained directly from patients. We detected STEVOR expression in a higher proportion of parasites recently isolated from patients than in cultured parasite lines and show that STEVOR is trafficked in schizont-stage parasites from the MC to the RBC cytosol and the iRBC membrane. Furthermore, STEVOR protein is also detected at the apical end of merozoites. Importantly, we show that culture-adapted parasites do not require STEVOR for survival. These findings provide new insights into the role of the stevor multigene family during both the schizont and merozoite stages of the parasite and highlight the importance of studying freshly isolated parasites, rather than parasite lines maintained in culture, when investigating potential mediators of host-parasite interactions.

scholarly journals The Role of Meningococcal Porin B in Protein-Protein Interactions with Host Cells

2018 ◽  
Vol 62 (1) ◽  
pp. 52-58
Author(s):  
E. Káňová ◽  
I. Jiménez-Munguía ◽  
Ľ. Čomor ◽  
Z. Tkáčová ◽  
I. Širochmanová ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Cell Signalling ◽  
Structure And Function ◽  
Host Cells ◽  
Protein Protein Interactions ◽  
Receptor Interactions ◽  
And Function ◽  
Fatal Sepsis ◽  
Porin B

Abstract Neisseria meningitidis is a Gram-negative diplococcus responsible for bacterial meningitis and fatal sepsis. Ligand-receptor interactions are one of the main steps in the development of neuroinvasion. Porin B (PorB), neisserial outer membrane protein (ligand), binds to host receptors and triggers many cell signalling cascades allowing the meningococcus to damage the host cells or induce immune cells responses via the TLR2-dependent mechanisms. In this paper, we present a brief review of the structure and function of PorB.

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