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1.
Chinese Journal of School Health ; (12): 594-597, 2022.
Article in Chinese | WPRIM (Western Pacific) | ID: wpr-924111

ABSTRACT

Objective@#To investigate the age related changes in cervical range of motion (CROM) and its relationship with cervical spondylosis in school students aged 12-18 in Nanyang City, to provide reference for prevention, early diagnosis and treatment evaluation of cervical spondylosis.@*Methods@#Stratified sampling was adopted in 13 counties and districts of Nanyang City and 890 students aged 12-18 were assessed for CROM using the Coda Motion Analyzer. SPSS 19.0 was used to data analyze.@*Results@#A decreasing trend was observed in CROM among boys and girls aged 12-18 years in Nanyang. For boys aged 15 and 18 years old, higher anterior flexion ( t =2.02, 2.70), posterior extension ( t =2.01, 2.81), left flexion ( t =3.51, 2.99), right flexion ( t =5.07, 2.66), sinistral ( t =2.28, 2.92) and dextral ( t =2.91,3.60) were found compared with younger age groups ( P <0.05). Similar findings were found in girls aged 15 and 18-years old [anterior flexion ( t =2.38, 2.20), posterior extension ( t =2.09,2.02), left flexion ( t =2.33, 2.55), right flexion ( t =7.34, 4.60), sinistral ( t =3.73, 2.35) and dextral ( t =2.31, 3.99, P <0.05). Except for the right flexion, the CROM of boys in was higher than that of girls at the same age group. The prevalence of cervical spondylosis showed an increasing trend (boys: χ 2 trend =13.93, girls: χ 2 trend =12.87, P <0.05). Except for 14-year-old group, the prevalence of cervical spondylosis in girls was higher than that in boys, with significant differences observed in 15 and 17-year-old groups ( χ 2=10.35, 9.64, P <0.05).@*Conclusion@#With the increase of age, the CROM of male and female students shows a downward trend in general. The prevalence of cervical spondylosis increases with the decrease of CROM. CROM measurement is conducive to the prevention, early diagnosis and treatment of juvenile cervical spondylosis.

2.
Inorg Chem ; 60(24): 19278-19286, 2021 Dec 20.
Article in English | MEDLINE | ID: mdl-34860499

ABSTRACT

To acquire more new crystalline proton conductive materials, three ferrocene-based phenyl carboxylate frameworks (FCFs), [FcCO(o-C6H4COOH)] (FCF 1) (Fc = (η5-C5H5)Fe(η5-C5H4)), [m-FcC6H4COOH] (FCF 2), and [p-FcC6H4COOH] (FCF 3), supported by hydrogen bonds and π···π interactions were prepared. Their structures and phase purities are clarified by single-crystal X-ray diffraction or powder X-ray diffraction (PXRD). In addition, their high thermal and water stability were confirmed by thermogravimetric analyses, PXRD, and scanning electron microscopy determinations. Proton conductivity (σ) of 1-3 was studied under different relative humidities (RHs) and temperatures, and it was found that their σ boosted with the increase of humidity and temperature. Under 100 °C and 98% RH, their optimal σ values are 0.77 × 10-3, 1.94 × 10-4, and 3.46 × 10-3 S·cm-1, respectively. Consequently, their proton conductive mechanisms were proposed by means of activation energy calculation and structural analysis. Note that they are good proton conductive materials and are expected to be used in proton exchange membrane fuel cells.

3.
Clin Immunol ; 138(1): 77-84, 2011 Jan.
Article in English | MEDLINE | ID: mdl-21075691

ABSTRACT

Enterohemorrhagic E. coli (EHEC) causes severe diseases in humans and animals via the production of Shiga toxins, and injection of effectors into epithelia using type III secretion system (TTSS). E. coli secreted protein A (EspA) forms the filamentous conduits of TTSS, which extends into the translocation pore embedded in host cell membranes and aids in the transportation of bacterial effectors. In addition, EspA is closely associated with initial bacterial adhesion and the formation of biofilms. EspA in its various forms elicits protective immune responses, although the epitope responsible has not to be identified. Here we report the presence of a linear, immunogenic, conserved and partially protective epitope E07 (100Lys-120Val) on EspA, which is recognized by the novel monoclonal antibody 1H10. This antibody blocks EHEC-induced actin polymerization and confers protection in mice. These findings provide a better understanding of EspA-induced immune responses and could lead to epitope-based vaccines and antibody-based therapies.


Subject(s)
Antibodies, Monoclonal/immunology , Antibodies, Neutralizing/immunology , Enterohemorrhagic Escherichia coli/immunology , Epitopes/immunology , Escherichia coli Proteins/immunology , Actins/metabolism , Amino Acid Sequence/genetics , Animals , Antibodies, Monoclonal/pharmacology , Antibodies, Monoclonal/therapeutic use , Antibodies, Neutralizing/pharmacology , Antibodies, Neutralizing/therapeutic use , Antigen-Antibody Reactions/immunology , Conserved Sequence/genetics , Conserved Sequence/immunology , Enterohemorrhagic Escherichia coli/drug effects , Enterohemorrhagic Escherichia coli/genetics , Epitope Mapping , Escherichia coli/drug effects , Escherichia coli/genetics , Escherichia coli/immunology , Escherichia coli Infections/microbiology , Escherichia coli Infections/prevention & control , Escherichia coli O157/drug effects , Escherichia coli O157/genetics , Escherichia coli O157/immunology , Escherichia coli Proteins/genetics , Feces/microbiology , Female , HeLa Cells , Humans , Immunoglobulin G/blood , Immunoglobulin G/immunology , Mice , Mice, Inbred BALB C , Molecular Sequence Data , Peptide Fragments/genetics , Peptide Fragments/immunology , Polymerization/drug effects , Recombinant Proteins/genetics , Recombinant Proteins/immunology , Vaccination
4.
J Microbiol ; 47(4): 498-505, 2009 Aug.
Article in English | MEDLINE | ID: mdl-19763426

ABSTRACT

Shiga toxin 2 (Stx2) is a major virulence factor for enterohemorrhagic Escherichia coli (EHEC), which is encoded by lambda lysogenic phage integrated into EHEC chromosome. Stx2Al, Al subunit of Stx2 toxin has gathered extensive concerns due to its potential of being developed into a vaccine candidate. However, the substantial progress is hampered in part for the lack of a suitable in vitro expression system. Here we report use of the prokaryotic system pET-28a::espA-Stx2Al/BL21 to carry out the fusion expression of Stx2Al which is linked to E. coli secreted protein A (EspA) at its N-terminus. Under the IPTG induction, EspA-Stx2Al fusion protein in the form of inclusion body was obtained successfully, whose expression level can reach about 40% of total bacterial protein at 25 degrees C, much higher than that at 37 degrees C. Western blot test suggested the refolded fusion protein is of excellent immuno-reactivity with both monoclonal antibodies, which are specific to EspA and Stx2Al, respectively. Anti-sera from Balb/c mice immunized with the EspA-Stx2Al fusion protein were found to exhibit strong neutralization activity and protection capability in vitro and in vivo. These data have provided a novel feasible method to produce Stx2Al in large scale in vitro, which is implicated for the development of multivalent subunit vaccines candidate against EHEC 0157:H7 infections.


Subject(s)
Bacterial Vaccines/immunology , Enterohemorrhagic Escherichia coli/immunology , Escherichia coli Infections/immunology , Escherichia coli Proteins/immunology , Protein Engineering , Shiga Toxin 2/immunology , Animals , Antibodies, Bacterial/immunology , Bacterial Vaccines/administration & dosage , Bacterial Vaccines/genetics , Enterohemorrhagic Escherichia coli/genetics , Escherichia coli Infections/microbiology , Escherichia coli Proteins/administration & dosage , Escherichia coli Proteins/genetics , Gene Expression , HeLa Cells , Humans , Mice , Mice, Inbred BALB C , Recombinant Fusion Proteins/administration & dosage , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/immunology , Shiga Toxin 2/administration & dosage , Shiga Toxin 2/genetics
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