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Tytuł pozycji:

Interaction of a Trichinella spiralis cathepsin B with enterocytes promotes the larval intrusion into the cells.

Tytuł:
Interaction of a Trichinella spiralis cathepsin B with enterocytes promotes the larval intrusion into the cells.
Autorzy:
Han Y; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
Yue X; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
Hu CX; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
Liu F; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
Liu RD; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
He MM; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
Long SR; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China.
Cui J; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China. Electronic address: .
Wang ZQ; Department of Parasitology, Medical College, Zhengzhou University, Zhengzhou 450052, PR China. Electronic address: .
Źródło:
Research in veterinary science [Res Vet Sci] 2020 Jun; Vol. 130, pp. 110-117. Date of Electronic Publication: 2020 Mar 07.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Publication: London : British Veterinary Association
Original Publication: Oxford.
MeSH Terms:
Cathepsin B/*genetics
Enterocytes/*parasitology
Epithelial Cells/*parasitology
Helminth Proteins/*genetics
Intestinal Mucosa/*parasitology
Trichinella spiralis/*physiology
Animals ; Cathepsin B/metabolism ; Female ; Helminth Proteins/metabolism ; Larva/genetics ; Larva/growth & development ; Larva/physiology ; Mice ; Mice, Inbred BALB C ; Sequence Analysis, DNA/veterinary ; Trichinella spiralis/genetics ; Trichinella spiralis/growth & development ; Trichinellosis/parasitology
Contributed Indexing:
Keywords: Cathepsin B; Interaction; Intestinal epithelium; Invasion; Trichinella spiralis
Substance Nomenclature:
0 (Helminth Proteins)
EC 3.4.22.1 (Cathepsin B)
Entry Date(s):
Date Created: 20200316 Date Completed: 20200827 Latest Revision: 20200827
Update Code:
20240105
DOI:
10.1016/j.rvsc.2020.03.012
PMID:
32171999
Czasopismo naukowe
Cathepsin B is one member of cysteine protease family and widely distributed in organisms, it plays an important function in parasite penetrating, migrating, molting and immune escaping. The aim of this work was to investigate whether exist interaction between a Trichinella spiralis cathepsin B (TsCB) and mouse intestinal epithelium cells (IECs), and its influence in the process of larva cell invasion. The results of ELISA, indirect immunofluorescence assay (IIFA), confocal microscopy and Far western blotting showed that there was a strong specific binding of rTsCB and IEC proteins, and the binding positions were located in cytoplasm and nuclei of IECs. The results of the in vitro larva penetration test revealed that rTsCB facilitated the larva invasion of IECs, whereas anti-rTsCB antibodies impeded partially the larva intrusion of enterocytes, this promotive or inhibitory roles were dose-dependent of rTsCB or anti-rTsCB antibodies. Silencing TsCB by siRNA mediated RNA interference reduced the TsCB expression in T. spiralis larvae, and markedly inhibited the larva penetration of enterocytes. The results indicated that TsCB binding to IECs promoted larva penetration of host's enteral epithelia, and it is a promising molecular target against intestinal invasive stages of T. spiralis.
Competing Interests: Declaration of Competing Interest The authors declare that there is no conflict of interest. Statement: (i) All the authors have agreed to its submission and are responsible for its contents; (ii) All the authors have agreed that Jing Cui and Zhong Quan Wang may act on their behalf regarding any subsequent processing of the paper; (iii) The authors have declared that no competing interests exist.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)

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