Immune response in goats vaccinated with thiol-binding proteins fromHaemonchus contortus

2018 ◽  
Vol 40 (9) ◽  
pp. e12569 ◽  
Author(s):  
José Manuel Molina ◽  
Yeray Isidoro Hernández ◽  
Sergio Martín ◽  
Otilia Ferrer ◽  
Francisco Rodríguez ◽  
...  
2019 ◽  
Author(s):  
Xuelian Ma ◽  
Xiaomin Zhao ◽  
Kaili Wang ◽  
Xiaoyi Tang ◽  
Jianxiong Guo ◽  
...  

Abstract Abstract Background: Transmissible gastroenteritis virus (TGEV) infection can activate the immune response and cause inflammation. Long noncoding RNAs (lncRNAs) play important roles in antiviral innate immune response. However, whether lncRNAs participate in TGEV-induced inflammation in porcine intestinal epithelial cells (IPECs) is largely unknown. Results: In this study, the next-generation sequencing (NGS) technology was used to analyze the profiles of lncRNAs in Mock and TGEV-infected porcine intestinal epithelial cell-jejunum 2 (IPEC-J2) cell line. A total of 106 lncRNAs were differentially expressed. Many differentially expressed lncRNAs act as elements to competitively attach miRNAs with mRNAs to mediate expression of genes that related to Toll-like receptor, NOD-like receptor, TNF, and RIG-I-like receptor pathways. Functional analysis of the binding proteins and the up/down-stream genes of the differentially expressed lncRNAs revealed that lncRNAs were principally related to immune response. Meanwhile, we found that the differentially expressed lncRNA TCONS_00058367 might lead to a reduction of p-p65 in TGEV-infected IPEC-J2 cells by negatively regulating its antisense gene PML. Conclusions: The data showed that differentially expressed lncRNAs might be involved in immune response induced by TGEV through acting as miRNA sponges, regulating their up/down-stream genes, or directly binding proteins.


2000 ◽  
Vol 203 (12) ◽  
pp. 1777-1782 ◽  
Author(s):  
H. Decker ◽  
N. Terwilliger

Two closely related copper proteins, phenoloxidase and haemocyanin, are known to be involved in different physiological functions such as the primary immune response and oxygen transport. Although the proteins differ structurally, they have the same active site by which dioxygen is bound. Recent results reveal that haemocyanin also exhibits phenoloxidase activity. A scenario is proposed for the evolutionary relationships among copper oxygen-binding proteins (COPs).


2021 ◽  
Author(s):  
Sophia C. Parks ◽  
Chau Nguyen ◽  
Shyon Nasrolahi ◽  
Damian Juncaj ◽  
Dihong Lu ◽  
...  

AbstractParasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during infection, yet little is known about their interactions with host tissues. Leveraging the insect parasitic nematode, Steinernema carpocapsae, we provide the first in vivo study that shows FARs modulate animal immunity, causing an increase in susceptibility to bacterial infection. Next we determined that FARs dampen various aspects of the fly immune response including the phenoloxidase cascade and antimicrobial peptide (AMP) production. Finally, we found that FARs deplete lipid signaling precursors in vivo as well as bind to these fatty acids in vitro, suggesting that FARs elicit their immunomodulatory effects by altering the availability of lipid signaling molecules necessary for a functional immune response. Collectively, these data reveal a complex role for FARs in immunosuppression and provide detailed mechanistic insight into parasitism in phylum Nematoda.SignificanceA central aspect of parasitic nematode success is their ability to modify host biology, including evasion and/or subversion of host immunity. Modulation of host biology and the pathology caused by parasitic nematodes is largely effected through the release of proteins and small molecules. There are hundreds of proteins released by nematodes during an infection and few have been studied in detail. Fatty acid- and retinol-binding proteins (FARs) are a unique protein family released during infection. We report that nematode FARs from S. carpocapsae, C. elegans and A. ceylanicum dampen fly immunity decreasing resistance to infection. Mechanistically, this is achieved through modulation of the phenoloxidase cascade and antimicrobial peptide production. Furthermore, FARs alter the availability of lipid immune signaling precursors in vivo and show binding specificity in vitro.Graphical Abstract


2021 ◽  
Vol 17 (10) ◽  
pp. e1010027
Author(s):  
Sophia C. Parks ◽  
Susan Nguyen ◽  
Shyon Nasrolahi ◽  
Chaitra Bhat ◽  
Damian Juncaj ◽  
...  

Parasitic nematodes cause significant morbidity and mortality globally. Excretory/secretory products (ESPs) such as fatty acid- and retinol- binding proteins (FARs) are hypothesized to suppress host immunity during nematode infection, yet little is known about their interactions with host tissues. Leveraging the insect parasitic nematode, Steinernema carpocapsae, we describe here the first in vivo study demonstrating that FARs modulate animal immunity, causing an increase in susceptibility to bacterial co-infection. Moreover, we show that FARs dampen key components of the fly immune response including the phenoloxidase cascade and antimicrobial peptide (AMP) production. Our data also reveal that FARs deplete lipid signaling precursors in vivo as well as bind to these fatty acids in vitro, suggesting that FARs elicit their immunomodulatory effects by altering the availability of lipid signaling molecules necessary for an efficient immune response. Collectively, these data support a complex role for FARs in immunosuppression in animals and provide detailed mechanistic insight into parasitism in phylum Nematoda.


Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.


1999 ◽  
Vol 37 (2) ◽  
pp. 123-129 ◽  
Author(s):  
B. R. Mignon ◽  
T. Leclipteux ◽  
CH. Focant ◽  
A. J. Nikkels ◽  
G. E. PIErard ◽  
...  

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