کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8648323 | 1570629 | 2018 | 34 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Functional characterisation of the actin-depolymerising factor from the apicomplexan Neospora caninum (NcADF)
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Functional characterisation of the actin-depolymerising factor from the apicomplexan Neospora caninum (NcADF) Functional characterisation of the actin-depolymerising factor from the apicomplexan Neospora caninum (NcADF)](/preview/png/8648323.png)
چکیده انگلیسی
Neospora caninum is an apicomplexan parasite that causes infectious abortion in cows. As an obligate intracellular parasite, N. caninum requires a host cell environment to survive and replicate. The locomotion and invasion mechanisms of apicomplexan parasites are centred on the actin-myosin system to propel the parasite forwards and into the host cell. The functions of actin, an intrinsically dynamic protein, are modulated by actin-binding proteins (ABPs). Actin-depolymerising factor (ADF) is a ubiquitous ABP responsible for accelerating actin turnover in eukaryotic cells and is one of the few known conserved ABPs from apicomplexan parasites. Apicomplexan ADFs have nonconventional properties compared with ADF/cofilins from higher eukaryotes. In the present paper, we characterised the ADF from N. caninum (NcADF) using computational and in vitro biochemical approaches to investigate its function in rabbit muscle actin dynamics. Our predicted computational tertiary structure of NcADF demonstrated a conserved structure and phylogeny with respect to other ADF/cofilins, although certain differences in filamentous actin (F-actin) binding sites were present. The activity of recombinant NcADF on heterologous actin was regulated in part by pH and the presence of inorganic phosphate. In addition, our data suggest a comparatively weak disassembly of F-actin by NcADF. Taken together, the data presented herein represent a contribution to the field towards the understanding of the role of ADF in N. caninum and a comparative analysis of ABPs in the phylum Apicomplexa.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular and Biochemical Parasitology - Volume 224, September 2018, Pages 26-36
Journal: Molecular and Biochemical Parasitology - Volume 224, September 2018, Pages 26-36
نویسندگان
Luciana Baroni, Luiz M. Pereira, Sutherland K. Maciver, Ana P. Yatsuda,