Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials

2016 ◽  
Vol 29 (6) ◽  
pp. 281-291 ◽  
Author(s):  
Bankala Krishnarjuna ◽  
San Sui Lim ◽  
Shane M. Devine ◽  
Cael O. Debono ◽  
Raymond Lam ◽  
...  
Keyword(s):  
Small Molecule ◽  
Apical Membrane ◽  
Solution Nmr ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen ◽  
Nmr Characterization ◽  
Molecule Interactions

scholarly journals NMR characterization of RNA small molecule interactions

Methods ◽  
2019 ◽  
Vol 167 ◽  
pp. 66-77 ◽  
Author(s):  
Rhese D. Thompson ◽  
Jared T. Baisden ◽  
Qi Zhang
Keyword(s):  
Small Molecule ◽  
Nmr Characterization ◽  
Molecule Interactions

scholarly journals Characterization of a novel inhibitory human monoclonal antibody directed against Plasmodium falciparum Apical Membrane Antigen 1

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Dominika J. Maskus ◽  
Michał Królik ◽  
Susanne Bethke ◽  
Holger Spiegel ◽  
Stephanie Kapelski ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Plasmodium Falciparum ◽  
Apical Membrane ◽  
Human Monoclonal Antibody ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen

scholarly journals Identification and Characterization of Eimeria tenella Apical Membrane Antigen-1 (AMA1)

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e41115 ◽  
Author(s):  
Lianlian Jiang ◽  
Jiaojiao Lin ◽  
Hongyu Han ◽  
Hui Dong ◽  
Qiping Zhao ◽  
...  
Keyword(s):  
Apical Membrane ◽  
Eimeria Tenella ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen ◽  
Identification And Characterization

Screening and characterization of apical membrane antigen 1 interacting proteins in Eimeria tenella

2016 ◽  
Vol 170 ◽  
pp. 116-124 ◽  
Author(s):  
Hongyu Han ◽  
Pu Xue ◽  
Hui Dong ◽  
Shunhai Zhu ◽  
Qiping Zhao ◽  
...  
Keyword(s):  
Apical Membrane ◽  
Eimeria Tenella ◽  
Interacting Proteins ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen

Characterization of the Apical Membrane Antigen-1 in Italian Strains of Babesia bigemina

2010 ◽  
Vol 57 (1-2) ◽  
pp. 52-56 ◽  
Author(s):  
A. Torina ◽  
A. Agnone ◽  
G. Sireci ◽  
J. J. Mosqueda ◽  
V. Blanda ◽  
...  
Keyword(s):  
Apical Membrane ◽  
Babesia Bigemina ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen

scholarly journals Structural Characterization of Apical Membrane Antigen 1 (AMA1) from Toxoplasma gondii

2010 ◽  
Vol 285 (20) ◽  
pp. 15644-15652 ◽  
Author(s):  
Joanna Crawford ◽  
Michelle L. Tonkin ◽  
Ognjen Grujic ◽  
Martin J. Boulanger
Keyword(s):  
Toxoplasma Gondii ◽  
Structural Characterization ◽  
Apical Membrane ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen

scholarly journals Expression, Purification, and Biological Characterization of Babesia microti Apical Membrane Antigen 1

2015 ◽  
Vol 83 (10) ◽  
pp. 3890-3901 ◽  
Author(s):  
Prasun Moitra ◽  
Hong Zheng ◽  
Vivek Anantharaman ◽  
Rajdeep Banerjee ◽  
Kazuyo Takeda ◽  
...  
Keyword(s):  
Apical Membrane ◽  
The United States ◽  
Host Cells ◽  
Health Concern ◽  
Babesia Microti ◽  
Type I ◽  
Content Type ◽  
Apical Membrane Antigen 1 ◽  
Apical Membrane Antigen ◽  
Extracellular Region

The intraerythrocytic apicomplexanBabesia microti, the primary causative agent of human babesiosis, is a major public health concern in the United States and elsewhere. Apicomplexans utilize a multiprotein complex that includes a type I membrane protein called apical membrane antigen 1 (AMA1) to invade host cells. We have isolated the full-lengthB. microtiAMA1 (BmAMA1) gene and determined its nucleotide sequence, as well as the amino acid sequence of the AMA1 protein. This protein contains an N-terminal signal sequence, an extracellular region, a transmembrane region, and a short conserved cytoplasmic tail. It shows the same domain organization as the AMA1 orthologs from piroplasm, coccidian, and haemosporidian apicomplexans but differs from all other currently known piroplasmida, including otherBabesiaandTheileriaspecies, in lacking two conserved cysteines in highly variable domain III of the extracellular region. Minimal polymorphism was detected in BmAMA1 gene sequences of parasite isolates from six babesiosis patients from Nantucket. Immunofluorescence microscopy studies showed that BmAMA1 is localized on the cell surface and cytoplasm near the apical end of the parasite. Native BmAMA1 from parasite lysate and refolded recombinant BmAMA1 (rBmAMA1) expressed inEscherichia colireacted with a mouse anti-BmAMA1 antibody using Western blotting.In vitrobinding studies showed that both native BmAMA1 and rBmAMA1 bind to human red blood cells (RBCs). This binding is trypsin and chymotrypsin treatment sensitive but neuraminidase independent. Incubation ofB. microtiparasites in human RBCs with a mouse anti-BmAMA1 antibody inhibited parasite growth by 80% in a 24-h assay. Based on its antigenically conserved nature and potential role in RBC invasion, BmAMA1 should be evaluated as a vaccine candidate.

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