Recombinant interferon-gamma promotes immunoglobulin G and cytokine memory responses to cathepsin L-like cysteine proteinase of Hyalomma asiaticum and the efficacy of anti-tick

2021 ◽  
Vol 235 ◽  
pp. 110201
Author(s):  
Ruiqi Song ◽  
Xuejie Zhai ◽  
Xinli Fan ◽  
Ting Ge ◽  
Min Li ◽  
...  
FEBS Letters ◽  
1995 ◽  
Vol 359 (1) ◽  
pp. 78-80 ◽  
Author(s):  
Atsushi Takeda ◽  
Takako Yamamoto ◽  
Yoshiko Nakamura ◽  
Tadahito Takahashi ◽  
Toshihiko Hibino

Parasitology ◽  
1994 ◽  
Vol 109 (5) ◽  
pp. 611-621 ◽  
Author(s):  
Y. Kong ◽  
Y.-B. Chung ◽  
S.-Y. Cho ◽  
S.-Y. Kang

When immunoglobulin G (IgG) was incubated with Spirometra mansoni plerocercoid (sparganum), it was cleaved into Fab and Fc fragments. Fab/c fragments were also hydrolysed. The digestion was accelerated by dithiothreitol (DTT), indicating that cleavage of IgG heavy chain was due to a cysteine protease secreted into the medium. The responsible enzyme, of Mr 27 (± 0·8) kDa, was purified by a series of thiopropyl affinity, Sephacryl S-300 HR and DEAE-anion exchange chromatographies, either from worm extracts or from excretory–secretory products (ESP). The purified, thiol-dependent protease showed an optimal activity at pH 5·7 with 0·1 M sodium acetate but was active over the pH range 4·5–8·0. Its activity was inhibited completely by 10−5 M L-trans-epoxysuccinylleucylamido(4-guanidino) butane (E-64) and 1 mM iodoacetamide (IAA), but by only 53% using the specific cathepsin L inhibitor, Z-Phe-Phe-CHN2 (5 × 10−5 M). Partial NH2-terminal amino acid sequence was Leu-Pro-Asp-Ser-Val-Asn-Trp-Arg-Glu-Gly-Ala-Val-Thr-Ala-Val which showed 80% homology to human cathepsin S. Immunoblot analysis showed that sera from infected patients exhibited IgE antibody reaction. It is proposed that cleavage of immunoglobulin by an excreted–secreted, cathepsin S-like, allergenic protease is a mechanism of immune evasion used by the sparganum.


Author(s):  
Jordan L. Mitchell ◽  
Anna Raper ◽  
Danièlle A. Gunn-Moore ◽  
Jayne C. Hope

2007 ◽  
Vol 24 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Rathnayaka M. C. Deshapriya ◽  
Akiyo Takeuchi ◽  
Khoji Shirao ◽  
Kenji Isa ◽  
Shoji Watabe ◽  
...  

1991 ◽  
Vol 173 (3) ◽  
pp. 767-770 ◽  
Author(s):  
H R Hill ◽  
N H Augustine ◽  
H S Jaffe

In previous studies, we have reported that after chemotactic factor stimulation, PMNs from neonates fail to undergo certain critical activation steps. Furthermore, the concentration of free intracellular calcium reached is significantly below that of PMNs from adults. Interferon-gamma (IFN-gamma) is a lymphokine that has been shown to activate phagocytic cells, and IFN-gamma messenger RNA production by neonatal mononuclear leukocytes has been reported to be depressed. In the present studies, we found that recombinant human IFN-gamma markedly enhanced the chemotactic responses of PMNs from neonates to levels that were not different from that of PMNs from adults. Furthermore, preincubation of the neonatal cells with this recombinant human lymphokine also corrected the abnormality in intracellular calcium metabolism. These results suggest that this developmental defect in phagocytic cell movement may be the result of an intrinsic defect in IFN-gamma production resulting in deficiency of this critical phagocyte-activating lymphokine.


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