Journal: mAbs

Article Title: Full-length recombinant antibodies from Escherichia coli : production, characterization, effector function (Fc) engineering, and clinical evaluation

doi: 10.1080/19420862.2022.2111748

Figure Lengend Snippet: Crystal structure (a) and a simplified diagram (b) of a full-length glycosylated monoclonal IgG1 antibody. a) Crystal structure (PDB:1HZH) showing two Fab domains and one Fc domain with glycans. b) Simplified architecture showing various domains. vH, variable heavy chain; vL, variable light chain; CL, constant light chain; CH1-CH3, constant heavy chain 1–3; Fab, fragment antigen binding; Fc, fragment crystallizable. N -linked glycans in the Fc CH2 domain are shown in stick (a) and red dots (b).

Article Snippet: Genentech and Sutro Biopharma have advanced multiple E. coli- produced, full-length IgG-based antibody therapeutics, including mAb, BsAb, ADC, and bispecific ADC drug modalities, into different stages of clinical trials in the areas of oncology, immuno-oncology, and allergy ( ).

Techniques: Binding Assay

Journal: mAbs

Article Title: Full-length recombinant antibodies from Escherichia coli : production, characterization, effector function (Fc) engineering, and clinical evaluation

doi: 10.1080/19420862.2022.2111748

Figure Lengend Snippet: Recent advances in the production of full-length antibodies in Escherichia coli.

Article Snippet: Genentech and Sutro Biopharma have advanced multiple E. coli- produced, full-length IgG-based antibody therapeutics, including mAb, BsAb, ADC, and bispecific ADC drug modalities, into different stages of clinical trials in the areas of oncology, immuno-oncology, and allergy ( ).

Techniques: Isolation, Mutagenesis, Purification, Expressing, Plasmid Preparation, Incubation

Journal: mAbs

Article Title: Full-length recombinant antibodies from Escherichia coli : production, characterization, effector function (Fc) engineering, and clinical evaluation

doi: 10.1080/19420862.2022.2111748

Figure Lengend Snippet: Crystal structure (a) and a simplified diagram (b) of a full-length glycosylated monoclonal IgG1 antibody. a) Crystal structure (PDB:1HZH) showing two Fab domains and one Fc domain with glycans. b) Simplified architecture showing various domains. vH, variable heavy chain; vL, variable light chain; CL, constant light chain; CH1-CH3, constant heavy chain 1–3; Fab, fragment antigen binding; Fc, fragment crystallizable. N -linked glycans in the Fc CH2 domain are shown in stick (a) and red dots (b).

Article Snippet: Genentech and Sutro Biopharma have advanced multiple E. coli- produced, full-length IgG-based antibody therapeutics, including mAb, BsAb, ADC, and bispecific ADC drug modalities, into different stages of clinical trials in the areas of oncology, immuno-oncology, and allergy ( ).

Techniques: Binding Assay

Journal: mAbs

Article Title: Full-length recombinant antibodies from Escherichia coli : production, characterization, effector function (Fc) engineering, and clinical evaluation

doi: 10.1080/19420862.2022.2111748

Figure Lengend Snippet: Recent advances in the production of full-length antibodies in Escherichia coli.

Article Snippet: Genentech and Sutro Biopharma have advanced multiple E. coli- produced, full-length IgG-based antibody therapeutics, including mAb, BsAb, ADC, and bispecific ADC drug modalities, into different stages of clinical trials in the areas of oncology, immuno-oncology, and allergy ( ).

Techniques: Isolation, Mutagenesis, Purification, Expressing, Plasmid Preparation, Incubation

Journal: Frontiers in Immunology

Article Title: Antibody Targets and Properties for Complement-Fixation Against the Circumsporozoite Protein in Malaria Immunity

doi: 10.3389/fimmu.2021.775659

Figure Lengend Snippet: Targets of naturally acquired antibodies associated with complement-fixation to CSP. Plasma collected from malaria-exposed adults (n=102) were tested for (A) C1q-fixation to CSP and stratified into positive and negative groups (C1q positive, n=52; C1q negative, n=50). The C1q positive and C1q negative groups were tested for (B) IgG1 and IgG3 subclasses to CSP, and (C) IgG and (D) IgM to full-length CSP and antigens representing the N-terminal (NT), central-repeat (NANP) and C-terminal (CT) regions of CSP. Samples were tested in duplicate, and the mean of duplicates is shown along with the group median and IQR. Dotted lines represent the positivity threshold relative to malaria-naïve negative controls. Reactivity between C1q positive and C1q negative groups were compared using the Mann-Whitney U test. In panels (C, D) , the odds ratio and 95% confidence interval are shown for IgG/IgM positivity to each region of CSP and C1q-fixation positivity using logistic regression; y-axis was presented on a log2 scale.

Article Snippet: We generated rabbit IgG raised against the Sanaria near full-length CSP (200 µg/dose), the truncated N+C construct (200 µg/dose), and the NT (100 µg/dose) and CT (150 µg/dose) regions of CSP.

Techniques: MANN-WHITNEY

Journal: Frontiers in Immunology

Article Title: Antibody Targets and Properties for Complement-Fixation Against the Circumsporozoite Protein in Malaria Immunity

doi: 10.3389/fimmu.2021.775659

Figure Lengend Snippet: Antibody breadth is associated with C1q-fixation. Plasma collected from malaria exposed adults (n=102) were tested for C1q-fixation to CSP and stratified into (A) C1q positive (n=52) and (B) C1q negative (n=50) groups. Heat-maps display IgG/IgM seropositivity to antigens representing the N-terminal (NT), central-repeat (NANP) and C-terminal (CT) regions of CSP. Each row represents an individual participant that was defined as seropositive (score = 1) or seronegative (score = 0) for IgG or IgM to each antigen. (C) The breadth scores for IgG and IgM were calculated by combining the seropositivity score for all three antigens (total breadth scores were between 0 and 3). The IgG and IgM breadth score for the C1q positive and C1q negative groups are shown as box plots (box represents the 25th and 75th percentile, whiskers represent the highest and lowest values within 1.5xIQR and values outside this range are shown as dots) and were compared using the Mann-Whitney U test.

Article Snippet: We generated rabbit IgG raised against the Sanaria near full-length CSP (200 µg/dose), the truncated N+C construct (200 µg/dose), and the NT (100 µg/dose) and CT (150 µg/dose) regions of CSP.

Techniques: MANN-WHITNEY

Journal: Frontiers in Immunology

Article Title: Antibody Targets and Properties for Complement-Fixation Against the Circumsporozoite Protein in Malaria Immunity

doi: 10.3389/fimmu.2021.775659

Figure Lengend Snippet: Complement-fixing activity of rabbit anti-CSP IgG to different regions of CSP. Rabbit anti-CSP IgG was tested for (A) IgG at 0.001-10 μg/ml and (B) C1q-fixation at 0.1-1000 μg/ml to CSP and antigens representing the N-terminal (NT), central-repeat (NANP) and C-terminal (CT) regions of CSP; x-axis was presented on a log10 scale. (C) The rabbit anti-CSP IgG was also tested at 100 μg/ml for C1q-fixation to CSP after pre-incubation with competing anitgen (including a no competition control); see Figure S1B for related data. Results were corrected for background reactivity using no-IgG control wells and the mean and range of two independent experiments is shown.

Article Snippet: We generated rabbit IgG raised against the Sanaria near full-length CSP (200 µg/dose), the truncated N+C construct (200 µg/dose), and the NT (100 µg/dose) and CT (150 µg/dose) regions of CSP.

Techniques: Activity Assay, Incubation

Journal: Frontiers in Immunology

Article Title: Antibody Targets and Properties for Complement-Fixation Against the Circumsporozoite Protein in Malaria Immunity

doi: 10.3389/fimmu.2021.775659

Figure Lengend Snippet: Rabbit IgG to the non-repeat regions of CSP can fix complement. Rabbit IgG were generated against (A) truncted CSP that lacked the central-repeat region (N+C) and the (B) C-terminal (CT) and (C) N-terminal (NT) regions of CSP. Rabbit IgG were tested for IgG at 0.001-10 μg/ml (left) and C1q-fixation at 0.1-1000 μg/ml (right) against full-length CSP, NT, NANP and CT anitgens [and N+C for panel (A) ]; x-axis was presented on a log10 scale. Results were corrected for background reactivity using no-IgG control wells and the mean and range of two independent experiments is shown.

Article Snippet: We generated rabbit IgG raised against the Sanaria near full-length CSP (200 µg/dose), the truncated N+C construct (200 µg/dose), and the NT (100 µg/dose) and CT (150 µg/dose) regions of CSP.

Techniques: Generated