Fostering Critical Thinking, Reasoning, and Argumentation Skills through Bioethics Education

Developing a position on a socio-scientific issue and defending it using a well-reasoned justification involves complex cognitive skills that are challenging to both teach and assess. Our work centers on instructional strategies for fostering critical thinking skills in high school students using bioethical case studies, decision-making frameworks, and structured analysis tools to scaffold student argumentation. In this study, we examined the effects of our teacher professional development and curricular materials on the ability of high school students to analyze a bioethical case study and develop a strong position. We focused on student ability to identify an ethical question, consider stakeholders and their values, incorporate relevant scientific facts and content, address ethical principles, and consider the strengths and weaknesses of alternate solutions. 431 students and 12 teachers participated in a research study using teacher cohorts for comparison purposes. The first cohort received professional development and used the curriculum with their students; the second did not receive professional development until after their participation in the study and did not use the curriculum. In order to assess the acquisition of higher-order justification skills, students were asked to analyze a case study and develop a well-reasoned written position. We evaluated statements using a scoring rubric and found highly significant differences (p<0.001) between students exposed to the curriculum strategies and those who were not. Students also showed highly significant gains (p<0.001) in self-reported interest in science content, ability to analyze socio-scientific issues, awareness of ethical issues, ability to listen to and discuss viewpoints different from their own, and understanding of the relationship between science and society. Our results demonstrate that incorporating ethical dilemmas into the classroom is one strategy for increasing student motivation and engagement with science content, while promoting reasoning and justification skills that help prepare an informed citizenry

Cohort 1 (CURE) and Cohort 2 (Comparison) Pre- and Post-Test Scores (N = 431).

<p>Mean scores for individual items of the pre-test for each cohort revealed no differences between groups for any of the items (Cohort 1, CURE, N = 323; Cohort 2, Comparison, N = 108). Post-test gains of Cohort 1 (CURE) relative to Cohort 2 (Comparison) were statistically significant for all questions. (Question (Q) 1) What is your decision? (Q2) What facts support your decision? Is there missing information that could be used to make a better decision? (Q3) Who will be impacted by the decision and how will they be impacted? (Q4) What are the main ethical considerations? and (Q5)What are some strengths and weaknesses of alternate solutions? Specifically: (Q1), (Q3), (Q4) were significant at p<0.001 (***); (Q2) was significant at p<0.01 (**); and (Q5) was significant at p<0.05 (*). Lines represent standard deviations.</p

Cohort Group Comparison of Post-Test Composite Mean Scores.

a<p>Standard Deviation.</p

Participants in the CURE Research Study.

a<p>Advanced Placement Biology.</p>b<p>Environmental Sciences.</p

Demographic Characteristics of Cohort 1 (CURE Treatment) and Cohort 2 (Comparison) Students^a.

a<p>Percentages of individual items might not equal 100% because of missing responses.</p>b<p>American Indian/Alaska Native.</p>c<p>Native Hawaiian.</p

Student Perceptions about Participation in the CURE Ethics Unit.

<p>Mean scores for individual items of the retrospective items on the post-test for Cohort 1 students revealed significant gains (p<0.001) in all self-reported items: <b>Interest</b> in science (N = 308), ability to <b>Analyze</b> issues related to science and society and make well-justified decisions (N = 306), <b>Awareness</b> of ethics and ethical issues (N = 309), <b>Understanding</b> of the connection between science and society (N = 308), and the ability to <b>Listen</b> and discuss different viewpoints (N = 308). Lines represent standard deviations.</p

Multimeric Scaffolds Displaying the HIV-1 Envelope MPER Induce MPER-Specific Antibodies and Cross-Neutralizing Antibodies when Co-Immunized with gp160 DNA

<div><p>Developing a vaccine that overcomes the diversity of HIV-1 is likely to require a strategy that directs antibody (Ab) responses toward conserved regions of the viral Envelope (Env). However, the generation of neutralizing Abs (NAbs) targeting these regions through vaccination has proven to be difficult. One conserved region of particular interest is the membrane proximal external region (MPER) of Env located within the gp41 ectodomain. In order to direct the immune response to this region, the MPER and gp41 ectodomain were expressed separately as N-terminal fusions to the E2 protein of <i>Geobacillus stearothermophilus</i>. The E2 protein acts as a scaffold by self-assembling into 60-mer particles, displaying up to 60 copies of the fused target on the surface. Rabbits were immunized with E2 particles displaying MPER and/or the gp41 ectodomain in conjunction with DNA encoding full-length gp160. Only vaccines including E2 particles displaying MPER elicited MPER-specific Ab responses. NAbs were elicited after two immunizations that largely targeted the V3 loop. To overcome V3 immunodominance in the DNA component, E2 particles displaying MPER were used in conjunction with gp160 DNA lacking hypervariable regions V2, V3, or combined V1V2V3. All rabbits had HIV binding Ab responses and NAbs following the second vaccination. Using HIV-2/HIV-1 MPER chimeric viruses as targets, NAbs were detected in 12/16 rabbits after three immunizations. Low levels of NAbs specific for Tier 1 and 2 viruses were observed in all groups. This study provides evidence that co-immunizing E2 particles displaying MPER and gp160 DNA can focus Ab responses toward conserved regions of Env.</p></div

Neutralization Activity Against HIV-2/HIV-1 MPER Chimera Viruses elicited in rabbits co-immunized with Env(MPER)-E2 and either SF162 gp160full-length, ΔV3, ΔV2, or ΔV123 DNA.

<p>(A) Neutralization titers against the autologous SF162 pseudovirus, parental HIV-2 virus 7312A wt, and the HIV-2/HIV-1 MPER chimera viruses 7312A C1, C3, and C4 were determined using the TZM-bl assay. Values stated are the IC₅₀ values for individual rabbits in each of the four groups at week 14 following the third vaccination. Pre-bleed samples as well as sera from a Env(V3)-E2+SF162 gp160 DNA vaccinated rabbit were included as controls. Darker colors represent an increase in NAb titer.</p

Construction and antigenic characterization of the HIV-1 Env(MPER)-E2 and Env(gp41)-E2 particles.

<p>(A) Schematic illustration of an E2 monomer with the HIV-1 Env region fused to the N-terminus. Amino acid sequences of the Env(MPER)-E2 and Env(gp41)-E2 constructs are shown below and numerated in relationship to the reference strain HXB2. Within the amino acid sequences, the 2F5 mAb epitope is underlined and highlighted in green and the 4E10 mAb epitope is underlined and highlighted in blue. (B) Representative SuperdexX200 gel filtration chromatograph of purified Env(MPER)-E2 particles. (C) Representative transmission electron micrograph of HIV-1 Env(gp41)-E2 particles. Env(MPER)-E2 and E2wt particles were of similar size and shape. Scale bar is 75 nm. (D) SimplyBlue stain of Env(MPER)-E2 (lane 1) and Env(gp41)-E2 (lane 2) revealing the purity of these particles at 93% and 90%, respectively. Western blot analysis of Env(MPER)-E2 (lanes 3 and 5) and Env(gp41)-E2 (lanes 4 and 6) using the Li-COR Odyssey dual-detection system to demonstrate the identity of these particles. Red bands indicate proteins detected with anti-E2 Abs, and green bands indicate proteins detected by either 2F5 or 4E10 mAbs. Yellow bands indicate proteins that are detected by both anti-E2 and either 2F5 or 4E10 mAbs. (E) Surface Plasmon Resonance Spectroscopy of Env(MPER)-E2 particles binding to the 2F5 NmAb to demonstrate accessibility of the 2F5 epitope on the surface of the scaffold. Binding was detected by flowing 2F5 mAb concentrations of 18.75 nM, 75 nM and 300 nM over E2 particles immobilized on a CM3 chip. No binding of the E2wt scaffold (lacking HIV fusion proteins) or Env(V3)-E2 particles to the 2F5 mAb were detected.</p