Additional file 1 of Combined effect of dietary calcium consumption and physical activity on dental caries in children and adolescents: a study of the NHANES database

Supplementary Material

Additional file 1: of Development and application of a monoclonal antibody-based blocking ELISA for detection of antibodies to Tembusu virus in multiple poultry species

Recombinant plasmid construction and protein expression. (PDF 299 kb

Additional file 2: of Development and application of a monoclonal antibody-based blocking ELISA for detection of antibodies to Tembusu virus in multiple poultry species

Neutralizing activity of  MAbs 9E4 and ROC analysis of the blocking ELISA. (PDF 370 kb

Enhanced Photoelectrocatalytic Activity of a Novel Bi₂O₃–BiPO₄ Composite Electrode for the Degradation of Refractory Pollutants under Visible Light Irradiation

A novel Bi₂O₃–BiPO₄ composite electrode was successfully synthesized by the method of electrophoretic deposition, electrodeposition, and calcination in a proper sequence. The prepared electrodes were characterized by X-ray diffractometry (XRD) and scanning electronic microscopy (SEM). Linear sweep voltammetry (LSV) and photocurrent decay curves measurement indicated that the Bi₂O₃–BiPO₄ composite electrode exhibited better photoelectrochemical (PEC) activity than either pure Bi₂O₃ or BiPO₄ electrode. Incident photon to current conversion efficiency (IPCE) and electrochemical impedance spectra (EIS) measurements revealed that the composite electrode significantly improved the efficiency of charge transfer and decreased the recombination of photogenerated charges. Furthermore, the composite electrode also displayed higher efficiency and stability in the PEC degradation of organic pollutants. The <i>p</i>–<i>n</i> junction structure of the Bi₂O₃–BiPO₄ composite electrode was most likely responsible for the enhanced PEC activity

Sequences of primers used in this study.

<p>Sequences of primers used in this study.</p

Expression and purification of His-tagged nsp11_40-223aa protein.

<p>(A) After culture and IPTG induction, the plasmid pET28a-nsp11 transformed <i>E</i> coli cells were collected. The thallus, as well as supernatant and precipitation parts post lysing, were submitted to SDS-PAGE for detecting the nsp11 expression. (B) The purity and concentration of purified nsp11_40-223aa protein was analyzed in SDS-PAGE.</p

Serological test for PRRSV nsp11 and the identified ¹¹¹DCREY¹¹⁵ epitope.

<p>(A) The nsp11 specific antibody in anti-PRRSV sera were detected by reacting with nsp11_40-223aa protein in WB test. (B) The nsp11 specific antibody in anti-PRRSV sera were detected by nsp11_40-223aa coated indirect ELISA. (C)The ¹¹¹DCREY¹¹⁵ epitope specific antibody in anti-PRRSV sera were detected by peptide coated indirect ELISA. Asterisk indicates significant differences between PRRSV positive sera and negative sera, or between control and mAb 3F9 (* <i>P<</i>0.05; ** <i>P<</i>0.01; *** <i>P<</i>0.001).</p

Confirm the conservation of identified ¹¹¹DCREY¹¹⁵ epitope in both genotype PRRSV.

<p>(A) Multiple sequence alignment of nsp11 epitope region. The identified epitope was labeled with box. (B and C) The PRRSV JXwn06 (genotype 1) or GZ11-G1 (genotype 2) inoculated MARC-145 cells were detected in IFA (B) and WB (C), by using nsp11 specific mAb 3F9 and N protein specific mAb SDOW17(for IFA only) as primary antibody.</p

Identification of the anti-nsp11 monoclonal antibody (3F9).

<p>The PRRSV JXwn06 infected MARC-145 cells and mock cells were submitted for WB analysis (A) and IFA (B) by using mAb 3F9 as primary antibody.</p

Identifying B-cell epitope of 3F9.

<p>(A) Four overlapped fragments covered the nsp11_40-223aa were expressed by using vector PEGFP-N1, and then the mAb 3F9 reactivity of truncated nsp11 proteins were verified by WB. (B) The mAb 3F9 reactivity of nine overlapped fragment covered nsp11_84-133aa were further tested by WB. (C) Eight overlapped fragments covered the nsp11_109-118aa were further tested by WB. (D) The identified core unit was expressed in PEGFP-N1, for testing its mAb 3F9 reactivity by WB, with the nsp11_40-223aa as positive control.</p