Abstract
ADP-ribosylation factors (ARFs) are members of the Ras-related small GTPase family involved in the vesicular trafficking regulation. Immunomodulatory effects of these proteinson host cell arenot being addressed yet. H. contortus small GTPase ADP-ribosylation 1 gene (HcARF1) was cloned and recombinant protein of HcARF1 (rHcARF1) was successfully expressed in Escherichia coli. Binding activity of rHcARF1 to goat PBMCs was confirmed by immunofluorescence assay (IFA) and its immunomudulatory effects on cytokine secretion, cell proliferation, cell migration and nitric oxide production (NO) were observed by co-incubation of rHcARF1. IFA results revealed that rHcARF1 could bind to the PBMCs. The interaction of rHcARF1 modulated the cytokine production, the production of IL-4, IL-10 and IL-17 was increased in a dose dependent manner, however, the IFN-γ production was significantly decreased. Cell migration and NO production were significantly increased by rHcARF1, whereas, rHcARF1 treatment significantly suppressed the proliferation of the PBMC in a dose dependent manner. Our findings showed that the rHcARF1 play important roles on the goat PBMCs.
Highlights
ADP-ribosylation factors (ARFs) are member of the Ras-related small GTPases family known as low molecular weight guanine-nucleotide-binding (G) proteins [1] and their involvement in the vesicular trafficking regulation has been well characterized [2]
The results of the multiple alignments showed that HcARF1 is very close to the ADP-ribosylation factor family protein of Ancylostoma ceylanicum (98%), Dictyocaulus viviparous (98%), Necator americanus (98%), Loa loa (97%), Strongyloides ratti (97%), Wuchereria bancrofti (97%), Pristionchus pacificus (97%) Caenorhabditis elegans (96%), The typical characteristics of the HcARF1 were confirmed as ARF 1-5 by their GTP/Mg2 binding and putative GAP interaction sites (Figure 1B)
The phylogenic tree analysis indicated that HcARF1 was closely related to ARF of homologous protein sequence obtained from NCBI data base (Figure 1C)
Summary
ADP-ribosylation factors (ARFs) are member of the Ras-related small GTPases family known as low molecular weight guanine-nucleotide-binding (G) proteins [1] and their involvement in the vesicular trafficking regulation has been well characterized [2]. ARF1 is characteristically related with the golgi and in some cell types be found related with the plasma membrane and is an important regulator of the biological process induced by epidermal growth factor [3,4,5,6,7]. ARF1 is involved in membrane affinity and it actively involve in the formation of non-clatherin/clatherin coated vesicles which helps in the transportation of vesicles to carry important cellular components required for biological processes such as cell signaling [11]. Characterization of the ARF proteins has been performed in various parasites included Caenorhabditis elegans [13, 14], Entamoeba histolytica [15], Plasmodium falciparum [16, 17] and Leishmania [18]
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