scholarly journals Hierarchical phosphorylation of apical membrane antigen 1 is required for efficient red blood cell invasion by malaria parasites

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Boris Prinz ◽  
Katherine L. Harvey ◽  
Louisa Wilcke ◽  
Ulrike Ruch ◽  
Klemens Engelberg ◽  
...  
Keyword(s):  
Blood Cell ◽  
Cell Invasion ◽  
Red Blood Cell ◽  
Apical Membrane ◽  
Malaria Parasites ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen ◽  
Hierarchical Phosphorylation

scholarly journals Babesia divergens Apical Membrane Antigen 1 and Its Interaction with the Human Red Blood Cell

2009 ◽  
Vol 77 (11) ◽  
pp. 4783-4793 ◽  
Author(s):  
Estrella Montero ◽  
Marilis Rodriguez ◽  
Yelena Oksov ◽  
Cheryl A. Lobo
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Apical Membrane ◽  
Vital Role ◽  
Red Cell ◽  
Electron Microscopic ◽  
Red Cell Membrane ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen ◽  
Babesia Divergens

ABSTRACT Multiple parasite ligand-erythrocyte receptor interactions must occur for successful Babesia and Plasmodium invasion of the human red cell. One such parasite ligand is the apical membrane antigen 1 (AMA1) which is a conserved apicomplexan protein present in the micronemes and then secreted onto the surface of the merozoite. Much evidence exists for a vital role for AMA1 in host cell invasion; however, its interaction with the host erythrocyte has remained controversial. In this paper, we present a detailed characterization of a Babesia divergens homolog of AMA1 (BdAMA1), and taking advantage of the relatively high amounts of native BdAMA1 available from the parasite culture system, show that proteolytic products of native BdAMA1 bind to a trypsin- and chymotrypsin-sensitive receptor on the red blood cell. Moreover, immuno-electron microscopic images of the B. divergens merozoite captured during invasion offer additional evidence of the presence of BdAMA1 on the red cell membrane. Given the importance of AMA1 in invasion and the central role invasion plays in pathogenesis, these studies have implications both for novel drug design and for the development of new vaccine approaches aimed at interfering with AMA1 function.

scholarly journals Conditional Expression of Toxoplasma gondii Apical Membrane Antigen-1 (TgAMA1) Demonstrates That TgAMA1 Plays a Critical Role in Host Cell Invasion

2005 ◽  
Vol 16 (9) ◽  
pp. 4341-4349 ◽  
Author(s):  
Jeffrey Mital ◽  
Markus Meissner ◽  
Dominique Soldati ◽  
Gary E. Ward
Keyword(s):  
Toxoplasma Gondii ◽  
Host Cell ◽  
Cell Invasion ◽  
Apical Membrane ◽  
Conditional Knockout ◽  
Host Cell Invasion ◽  
Apical Membrane Antigen 1 ◽  
Apicomplexan Parasites ◽  
Apical Membrane Antigen ◽  
Conditional Expression

Toxoplasma gondii is an obligate intracellular parasite and an important human pathogen. Relatively little is known about the proteins that orchestrate host cell invasion by T. gondii or related apicomplexan parasites (including Plasmodium spp., which cause malaria), due to the difficulty of studying essential genes in these organisms. We have used a recently developed regulatable promoter to create a conditional knockout of T. gondii apical membrane antigen-1 (TgAMA1). TgAMA1 is a transmembrane protein that localizes to the parasite's micronemes, secretory organelles that discharge during invasion. AMA1 proteins are conserved among apicomplexan parasites and are of intense interest as malaria vaccine candidates. We show here that T. gondii tachyzoites depleted of TgAMA1 are severely compromised in their ability to invade host cells, providing direct genetic evidence that AMA1 functions during invasion. The TgAMA1 deficiency has no effect on microneme secretion or initial attachment of the parasite to the host cell, but it does inhibit secretion of the rhoptries, organelles whose discharge is coupled to active host cell penetration. The data suggest a model in which attachment of the parasite to the host cell occurs in two distinct stages, the second of which requires TgAMA1 and is involved in regulating rhoptry secretion.

scholarly journals Complement and Antibody-mediated Enhancement of Red Blood Cell Invasion and Growth of Malaria Parasites

EBioMedicine ◽  
2016 ◽  
Vol 9 ◽  
pp. 207-216 ◽  
Author(s):  
Sergei Biryukov ◽  
Evelina Angov ◽  
Mary E. Landmesser ◽  
Michele D. Spring ◽  
Christian F. Ockenhouse ◽  
...  
Keyword(s):  
Blood Cell ◽  
Cell Invasion ◽  
Red Blood Cell ◽  
Malaria Parasites

scholarly journals Independent Roles of Apical Membrane Antigen 1 and Rhoptry Neck Proteins during Host Cell Invasion by Apicomplexa

2011 ◽  
Vol 10 (6) ◽  
pp. 591-602 ◽  
Author(s):  
Donatella Giovannini ◽  
Stephan Späth ◽  
Céline Lacroix ◽  
Audrey Perazzi ◽  
Daniel Bargieri ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Apical Membrane ◽  
Host Cell Invasion ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen

scholarly journals Eimeria tenella Eimeria-specific protein that interacts with apical membrane antigen 1 (EtAMA1) is involved in host cell invasion

2019 ◽  
Author(s):  
Cong Li ◽  
Qiping Zhao ◽  
Shunhai Zhu ◽  
Qingjie Wang ◽  
Haixia Wang ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Apical Membrane ◽  
Specific Protein ◽  
Host Cells ◽  
Bimolecular Fluorescence Complementation ◽  
Host Cell Invasion ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen

Abstract Apical membrane antigen 1 (AMA1), which is released from micronemes and is conserved across all apicomplexans, plays a central role in the host cell invasion. In this study, we characterized one putative Et AMA1-interacting protein, E. tenella Eimeria -specific protein ( Et Esp). The interaction between Et AMA1 and Et Esp was confirmed with bimolecular fluorescence complementation (BiFC) in vivo and by glutathione S-transferase (GST) fusion protein pull-down (GST pull-down) in vitro . We showed that Et Esp is differentially expressed during distinct phases of the parasite life cycle by using qPCR and western blotting. Immunofluorescence analysis showed that the Et Esp protein is mainly distributed on the parasite surface, and that the expression of this protein increases during the development of the parasite in the host cells. Using staurosporine, we showed that Et Esp is a micronemal protein secreted by sporozoites. In inhibition tests, a polyclonal anti-r Et Esp antibody attenuated the capacity of E. tenella to invade host cells in vitro . These data have implications for the use of Et AMA1 or Et AMA1-interacting proteins as targets in intervention strategies against avian coccidiosis.

scholarly journals A Chimeric Peptide Inhibits Red Blood Cell Invasion by Plasmodium falciparum with Hundredfold Increased Efficacy

2021 ◽  
Author(s):  
Jamsad Mannuthodikayil ◽  
Suman Sinha ◽  
Sameer Singh ◽  
Anamika Biswas ◽  
Irshad Ali ◽  
...  
Keyword(s):  
Blood Cell ◽  
Cell Invasion ◽  
Red Blood Cell ◽  
Peptide Inhibitors ◽  
Apical Membrane Antigen 1 ◽  
Tight Junction Formation ◽  
Chimeric Peptide ◽  
Unique Approach ◽  
Structural Insights

Inhibition of tight junction formation between two malaria parasite proteins, apical membrane antigen 1 and rhoptry neck protein 2, crucial for red blood cell invasion, prevents the disease progression. In this work, we have utilized a unique approach to design a chimeric peptide, prepared by fusion of the best features of two peptide inhibitors, that has displayed parasite growth inhibition, in-vitro, with nanomolar IC50, which is hundredfold better than any of its parent peptides. Further, to gain structural insights, we computationally modeled the hybrid peptide on its receptor.

Sign in / Sign up

Export Citation Format

Share Document