Cell membrane labeling of Eimeria tenella sporozoites with the fluorescent dye PKH-67 GL for tracking parasite-host interactions

2001 ◽  
Vol 87 (7) ◽  
pp. 521-525 ◽  
Author(s):  
Not Available Not Available ◽  
Not Available Not Available
Cytometry ◽  
1995 ◽  
Vol 21 (2) ◽  
pp. 160-169 ◽  
Author(s):  
Ludwig Spötl ◽  
Alessandra Sarti ◽  
Manfred P. Dierich ◽  
Johannes Möst

Molecules ◽  
2012 ◽  
Vol 17 (1) ◽  
pp. 1055-1073 ◽  
Author(s):  
Christian Kleusch ◽  
Nils Hersch ◽  
Bernd Hoffmann ◽  
Rudolf Merkel ◽  
Agnes Csiszár

2020 ◽  
Vol 78 (6) ◽  
Author(s):  
Bruno Mendes ◽  
Carolina Proaño-Bolaños ◽  
Fernanda R Gadelha ◽  
José R Almeida ◽  
Danilo C Miguel

ABSTRACT Screenings of natural products have significantly contributed to the discovery of novel leishmanicidal agents. In this study, three known cruzioseptins—antibacterial peptides from Cruziohyla calcarifer skin—were synthesized and evaluated against promastigotes and amastigotes stages of Leishmania (L.) amazonensis and L. (V.) braziliensis. EC50 ranged from 9.17 to 74.82 μM, being cruzioseptin-1 the most active and selective compound, with selectivity index > 10 for both promastigotes and amastigotes of L. (V.) braziliensis. In vitro infections incubated with cruzioseptins at 50 μM showed up to ∼86% reduction in the amastigote number. Cruzioseptins were able to destabilize the parasite's cell membrane, allowing the incorporation of a DNA-fluorescent dye. Our data also demonstrated that hydrophobicity and charge appear to be advantageous features for enhancing parasiticidal activity. Antimicrobial cruzioseptins are suitable candidates and alternative molecules that deserve further in vivo investigation focusing on the development of novel antileishmanial therapies.


2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Nur Zazarina Ramly ◽  
Samuel R. Dix ◽  
Sergey N. Ruzheinikov ◽  
Svetlana E. Sedelnikova ◽  
Patrick J. Baker ◽  
...  

AbstractIn infections by apicomplexan parasites including Plasmodium, Toxoplasma gondii, and Eimeria, host interactions are mediated by proteins including families of membrane-anchored cysteine-rich surface antigens (SAGs) and SAG-related sequences (SRS). Eimeria tenella causes caecal coccidiosis in chickens and has a SAG family with over 80 members making up 1% of the proteome. We have solved the structure of a representative E. tenella SAG, EtSAG19, revealing that, despite a low level of sequence similarity, the entire Eimeria SAG family is unified by its three-layer αβα fold which is related to that of the CAP superfamily. Furthermore, sequence comparisons show that the Eimeria SAG fold is conserved in surface antigens of the human coccidial parasite Cyclospora cayetanensis but this fold is unrelated to that of the SAGs/SRS proteins expressed in other apicomplexans including Plasmodium species and the cyst-forming coccidia Toxoplasma gondii, Neospora caninum and Besnoitia besnoiti. However, despite having very different structures, Consurf analysis showed that Eimeria SAG and Toxoplasma SRS families each exhibit marked hotspots of sequence hypervariability that map to their surfaces distal to the membrane anchor. This suggests that the primary and convergent purpose of the different structures is to provide a platform onto which sequence variability can be imposed.


2007 ◽  
Vol 90 (2) ◽  
pp. 021110 ◽  
Author(s):  
Kazuya Yamamoto ◽  
Ichirou Ishimaru ◽  
Yoshiki Fujii ◽  
Toshiki Yasokawa ◽  
Shigeki Kuriyama ◽  
...  

1998 ◽  
Vol 37 (2) ◽  
pp. 110-115
Author(s):  
Sachio Takeno ◽  
Takaharu Tatsukawa ◽  
Hiroko Kawamoto ◽  
Noriyuki Fukushima ◽  
Koji Yazin

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e109162 ◽  
Author(s):  
Fatma M. Youniss ◽  
Gobalakrishnan Sundaresan ◽  
Laura J. Graham ◽  
Li Wang ◽  
Collin R. Berry ◽  
...  

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