rbd fragment  (Native Antigen Inc)

Journal: International Journal of Molecular Sciences

Article Title: Microcystis viridis NIES-102 Cyanobacteria Lectin (MVL) Interacts with SARS-CoV-2 Spike Protein Receptor Binding Domains (RBDs) via Protein–Protein Interaction

doi: 10.3390/ijms25126696

Figure Lengend Snippet: Results of MVL (yellow) and spike protein RBD (brown) docking analysis using HDOCK. ( a ) Alpha RBD, ( b ) Delta RBD, ( c ) Omicron RBD, ( d ) original RBD. Residues showing polar interactions are listed to the right.

Article Snippet: For the Omicron variant, due to numerous mutation sites in its RBD, the In-fusion method was employed to ligate the synthetic Omicron spike protein RBD gene fragment (Integrated DNA Tachnology k.k., Tokyo, Japan) with the pcDNA3-sfGFP vector fragment, to construct the pcDNA3-Omicron-RBD-sfGFP plasmid.

Techniques:

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: Isolation and generation of MERS-CoV RBD-specific antibodies. (A) Schematic representation illustrating the selection strategy for single-chain variable fragment (scFv) antibodies targeting the receptor-binding domain (RBD) of the MERS-CoV. The process used phage display technology, involving six rounds of biopanning using magnetic beads immobilized with MERS-CoV RBD. (B) Phage ELISA was conducted on 96 randomly selected phage clones to identify those expressing MERS-CoV RBD-specific scFv clones.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Isolation, Selection, Binding Assay, Magnetic Beads, Enzyme-linked Immunosorbent Assay, Clone Assay, Expressing

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: Neutralizing properties of selected antibodies against MERS-CoV pseudotyped virus in vitro. (A) Schematic representation of the neutralizing activity analysis using a pseudotyped virus assay. (B) Verification of hDPP4 expression in 293T/hDPP4 cell lines using immunoblot analysis. (C) Multiplicity of infection (MOI)-dependent infection by the MERS-CoV pseudotyped virus in 293T/hDPP4 cells. (D–G) Concentration-dependent neutralization of MERS-CoV pseudotyped virus infection in 293T/hDPP4 cells by the control IgG and selected mAbs: (D) K111.1, (E) K111.2, (F) K111.3, and (G) K111.4.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Virus, In Vitro, Activity Assay, Expressing, Western Blot, Infection, Concentration Assay, Neutralization

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: IC 50 values for selected antibodies against MERS-CoV pseudovirus infection.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Infection

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: Generation and characterization of engineered bsAbs. (A–C) SPR sensorgrams showing response units for the competitive binding of mAbs to MERS-CoV RBD pre-saturated with K111.3. Each panel depicts the results for a different mAb tested: (A) K111.1, (B) K111.2, and (C) K111.4, illustrating their ability to bind to the RBD in the presence of K111.3. (D) Schematic diagrams depict the designed bsAbs in the IgG4-(scFv) 2 format, engineered to simultaneously engage multiple epitopes on the MERS-CoV RBD. (E–H) SPR sensorgrams show the binding kinetics of parental mAb and engineered bsAbs to MERS-CoV RBD: (E) K111.3, (F) K207.A, (G) K207.B, and (H) K207.C.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Binding Assay

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: Binding kinetics of the selected antibodies against MERS-CoV RBD.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Binding Assay

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: IC 50 values for the antibodies against MERS-CoV pseudovirus infection.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Infection

Journal: Virus Research

Article Title: A dual-targeting approach using a human bispecific antibody against the receptor-binding domain of the Middle East Respiratory Syndrome Coronavirus

doi: 10.1016/j.virusres.2024.199383

Figure Lengend Snippet: Biochemical characterization and neutralization efficacy analysis of bsAbs for MERS-CoV RBD. (A) SPR sensorgrams showing the binding of bsAb K207.C on an RBD-immobilized sensor chip that was pre-saturated with K111.3 (left) and the binding of K207.C to an RBD-immobilized sensor chip that was pre-saturated with K111.1 (right). (B) SPR sensorgrams demonstrating the competitive binding of K111.1 (left) and K111.3 (right) on an RBD-immobilized sensor chip pre-saturated with bsAb K207.C. (C) Results from the neutralization activity assay, showing the efficacy of parental mAb K111.3, bsAb K207.C, and control IgG against MERS-CoV pseudotyped virus infections in 293T/hDPP4 cells, displayed in a dose−response curve. (D) Bar graph representing the neutralization potency of parental mAb K111.3, bsAb K207.C, and control IgG in disrupting the interaction of MERS-CoV RBD with the hDPP4 protein.

Article Snippet: This process involved six rounds of selection using M-270 epoxy Dynabeads™ (Invitrogen, Waltham, MA, USA), which were covalently immobilized with 4 μg of recombinant His-tagged MERS-CoV RBD (RBD-His; Sino Biological, Beijing, China).

Techniques: Neutralization, Binding Assay, Activity Assay, Virus