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1.
Materials (Basel) ; 17(10)2024 May 17.
Article in English | MEDLINE | ID: mdl-38793483

ABSTRACT

As the Brønsted acid sites in the 8-membered ring (8-MR) of mordenite (MOR) are reported to be the active center for dimethyl ether (DME) carbonylation reaction, it is of great importance to selectively increase the Brønsted acid amount in the 8-MR. Herein, a series of Fe-HMOR was prepared through one-pot hydrothermal synthesis by adding the EDTA-Fe complex into the gel. By combining XRD, FTIR, UV-Vis, Raman and XPS, it was found that the Fe atoms selectively substituted for the Al atoms in the 12-MR channels because of the large size of the EDTA-Fe complex. The NH3-TPD and Py-IR results showed that with the increase in Fe addition from Fe/Si = 0 to 0.02, the Brønsted acid sites derived from Si-OH-Al in the 8-MR first increased and then decreased, with the maximum at Fe/Si = 0.01. The Fe-modified MOR with Fe/Si = 0.01 showed the highest activity in DME carbonylation, which was three times that of HMOR. The TG/DTG results indicated that the carbon deposition and heavy coke formation in the spent Fe-HMOR catalysts were inhibited due to Fe addition. This work provides a practical way to design a catalyst with enhanced catalytic performance.

2.
Fish Shellfish Immunol ; 52: 23-30, 2016 May.
Article in English | MEDLINE | ID: mdl-26975412

ABSTRACT

Fish-egg lectins (FELs) are identified in several species of fishes, but their activity and mode of action remain largely unknown in early life stages. Here we showed that zebrafish FEL (zFEL) was a maternal factor, which was capable of interacting with Gram-negative and Gram-positive bacteria and enhancing the phagocytosis of the bacteria by macrophages. Interestingly, microinjection of purified native zFEL into the embryos (resulting in the increase of zFEL in the embryos) markedly promoted the resistance of the embryos to the pathogenic Aeromonas hydrophila. Taken together, zFEL appears a maternal immune-relevant molecule capable of defending the developing embryos/larvae from pathogenic attacks.


Subject(s)
Fish Proteins/metabolism , Immunity, Innate/immunology , Lectins/metabolism , Zebrafish/genetics , Zebrafish/immunology , Aeromonas hydrophila/physiology , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA, Complementary/genetics , DNA, Complementary/metabolism , Embryo, Nonmammalian/immunology , Fish Proteins/genetics , Fish Proteins/isolation & purification , Fish Proteins/pharmacology , Gram-Negative Bacteria/physiology , Gram-Positive Bacteria/physiology , Immunity, Innate/drug effects , Lectins/genetics , Lectins/isolation & purification , Lectins/pharmacology , RNA, Messenger/genetics , RNA, Messenger/metabolism , Zebrafish/metabolism , Zebrafish/microbiology
3.
Dev Comp Immunol ; 46(2): 314-22, 2014 Oct.
Article in English | MEDLINE | ID: mdl-24858663

ABSTRACT

The lectin pathway involves recognition of pathogen-associated molecular patterns by mannose-binding lectin (MBL), and the subsequent activation of associated enzymes, termed MBL-associated serine proteases (MASPs). In this study, we demonstrate that the transcript of MBL gene is present in the early embryo of zebrafish, and MBL protein is also present in the embryo. In addition, we show that recombinant zebrafish MBL was able to bind the Gram-negative bacterium Escherichia coli and the Gram-positive bacterium Staphylococcus aureus, and rMBL was able to promote the phagocytosis of E. coli and S. aureus by macrophages, indicating that like mammalian MBL, zebrafish MBL performs a dual function in both pattern recognition and opsonization. Importantly, we show that microinjection of anti-MBL antibody into the early developing embryos resulted in a significantly increased mortality in the embryos challenged with Aeromonas hydrophila (pathogenic to zebrafish); and injection of rMBL into the embryos (resulting in increase in MBL in the embryo) markedly promoted their resistance to A. hydrophila; and this promoted bacterial resistance was significantly reduced by the co-injection of anti-MBL antibody with rMBL but not by the injection of anti-actin antibody with rMBL. These suggest that the lectin pathway may be already functional in the early embryos in zebrafish before their immune system is fully matured, protecting the developing embryos from microbial infection. This work provides a new angle to understand the immune role of the lectin pathway in early development of animals.


Subject(s)
Fish Diseases/immunology , Gram-Negative Bacterial Infections/veterinary , Mannose-Binding Lectin/genetics , Zebrafish/immunology , Adaptive Immunity , Aeromonas hydrophila/immunology , Amino Acid Sequence , Animals , Complement Activation , Complement System Proteins , Embryo, Nonmammalian/immunology , Embryo, Nonmammalian/metabolism , Embryo, Nonmammalian/microbiology , Female , Fish Diseases/metabolism , Fish Diseases/microbiology , Gram-Negative Bacterial Infections/immunology , Gram-Negative Bacterial Infections/metabolism , Immunity, Innate , Male , Mannose-Binding Lectin/biosynthesis , Molecular Sequence Data , Phagocytosis , Protein Binding , Zebrafish/genetics , Zebrafish/metabolism
4.
Peptides ; 37(2): 309-13, 2012 Oct.
Article in English | MEDLINE | ID: mdl-22841856

ABSTRACT

A phosvitin (Pv)-derived peptide, Pt5, which consists of the C-terminal 55 residues of Pv in zebrafish, has been shown to function as an antimicrobial agent capable of killing microbes in vitro. However, its in vivo role in zebrafish remains unknown. In this study, we clearly demonstrated that Pt5 protected adult zebrafish from pathogenic Aeromonas hydrophila attack, capable of significantly enhancing the survival rate of zebrafish after the pathogenic challenge. Pt5 also caused a marked decrease in the numbers of A. hydrophila in the blood, spleen, kidney, liver and muscle, suggesting that Pt5 was able to block multiplication/dissemination of A. hydrophila in zebrafish. Additionally, Pt5 markedly suppressed the expression of the proinflammatory cytokine genes IL-1ß, IL-6, TNF-α and IFN-γ in the spleen and head kidney of A. hydrophila-infected zebrafish, but it considerably enhanced the expressions of the antiinflammatory cytokine genes IL-10 and IL-4 in the same tissues. Taken together, these data indicate that Pt5 plays a dual role in zebrafish as an antimicrobial and immunomodulatory agent, capable of protecting zebrafish against pathogenic A. hydrophila through its antimicrobial activity as well as preventing zebrafish from the detrimental effects of an excessive inflammatory response via modulating immune functions.


Subject(s)
Aeromonas hydrophila/drug effects , Anti-Bacterial Agents/pharmacology , Immunomodulation , Peptide Fragments/immunology , Peptide Fragments/pharmacology , Phosvitin/chemistry , Zebrafish Proteins/immunology , Zebrafish Proteins/pharmacology , Zebrafish , Animals , Anti-Bacterial Agents/chemistry , Anti-Bacterial Agents/immunology , Immunomodulation/drug effects , Microbial Sensitivity Tests , Peptide Fragments/chemistry , Phosvitin/immunology , Phosvitin/pharmacology , Structure-Activity Relationship , Zebrafish Proteins/chemistry
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