Conjugation and Characterization of Latex Particles with Toxoplasma gondii–specific Immunoglobulin Y Antibodies for Diagnostic Aim and Evaluation Efficiency in In Vitro Culture

2020 ◽  
Vol 92 ◽  
pp. 103145
Author(s):  
Rabia Cakir-Koc ◽  
Yasemin Budama-Kilinc ◽  
Eslin Ustun ◽  
Cahit Babur
2001 ◽  
Vol 173 (1) ◽  
pp. 151-157 ◽  
Author(s):  
C. G. Kevil ◽  
D. C. Bullard
Keyword(s):  

1987 ◽  
Vol 17 (3) ◽  
pp. 829-834 ◽  
Author(s):  
Bernabe Chumpitazi ◽  
Pierre Ambroise-Thomas ◽  
Maryvonne Cagnard ◽  
Jean M. Autheman

1991 ◽  
Vol 21 (1) ◽  
pp. 129-132 ◽  
Author(s):  
A. Couatarmanach ◽  
P. Andre ◽  
D. Le Minous ◽  
L. Martin ◽  
R. Robert ◽  
...  

2005 ◽  
Vol 4 (12) ◽  
pp. 2057-2065 ◽  
Author(s):  
Aaron T. Smith ◽  
Samantha D. Tucker-Samaras ◽  
Alan H. Fairlamb ◽  
William J. Sullivan

ABSTRACT The restructuring of chromatin precedes tightly regulated events such as DNA transcription, replication, and repair. One type of chromatin remodeling involves the covalent modification of nucleosomes by histone acetyltransferase (HAT) complexes. The observation that apicidin exerts antiprotozoal activity by targeting a histone deacetyltransferase has prompted our search for more components of the histone modifying machinery in parasitic protozoa. We have previously identified GNAT family HATs in the opportunistic pathogen Toxoplasma gondii and now describe the first MYST (named for members MOZ, Ybf2/Sas3, Sas2, and Tip60) family HATs in apicomplexa (TgMYST-A and -B). The TgMYST-A genomic locus is singular and generates a ∼3.5-kb transcript that can encode two proteins of 411 or 471 amino acids. TgMYST-B mRNA is ∼7.0 kb and encodes a second MYST homologue. In addition to the canonical MYST HAT catalytic domain, both TgMYST-A and -B possess an atypical C2HC zinc finger and a chromodomain. Recombinant TgMYST-A exhibits a predilection to acetylate histone H4 in vitro at lysines 5, 8, 12, and 16. Antibody generated to TgMYST-A reveals that both the long and short (predominant) versions are present in the nucleus and are also plentiful in the cytoplasm. Moreover, both TgMYST-A forms are far more abundant in rapidly replicating parasites (tachyzoites) than encysted parasites (bradyzoites). A bioinformatics survey of the Toxoplasma genome reveals numerous homologues known to operate in native MYST complexes. The characterization of TgMYST HATs represents another important step toward understanding the regulation of gene expression in pathogenic protozoa and provides evolutionary insight into how these processes operate in eukaryotic cells in general.


2016 ◽  
Vol 18 (1) ◽  
pp. 49-58
Author(s):  
Ricardo Enrique Toso ◽  
◽  
Barbara Daniela Neher ◽  
Nicolás José María Alvarez Rubianes ◽  
Mirta Susana Toribio ◽  
...  

mBio ◽  
2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Vincent Tu ◽  
Tadakimi Tomita ◽  
Tatsuki Sugi ◽  
Joshua Mayoral ◽  
Bing Han ◽  
...  

ABSTRACT A characteristic of the latent cyst stage of Toxoplasma gondii is a thick cyst wall that forms underneath the membrane of the bradyzoite vacuole. Previously, our laboratory group published a proteomic analysis of purified in vitro cyst wall fragments that identified an inventory of cyst wall components. To further refine our understanding of the composition of the cyst wall, several cyst wall proteins were tagged with a promiscuous biotin ligase (BirA*), and their interacting partners were screened by streptavidin affinity purification. Within the cyst wall pulldowns, previously described cyst wall proteins, dense granule proteins, and uncharacterized hypothetical proteins were identified. Several of the newly identified hypothetical proteins were validated to be novel components of the cyst wall and tagged with BirA* to expand the model of the cyst wall interactome. Community detection of the cyst wall interactome model revealed three distinct clusters: a dense granule, a cyst matrix, and a cyst wall cluster. Characterization of several of the identified cyst wall proteins using genetic strategies revealed that MCP3 affects in vivo cyst sizes. This study provides a model of the potential protein interactions within the cyst wall and the groundwork to understand cyst wall formation. IMPORTANCE A model of the cyst wall interactome was constructed using proteins identified through BioID. The proteins within this cyst wall interactome model encompass several proteins identified in a prior characterization of the cyst wall proteome. This model provides a more comprehensive understanding of the composition of the cyst wall and may lead to insights on how the cyst wall is formed.


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