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BIODEV Formation et Consulting pcr product purification kit biodev-tech
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JEOL transmission electron microscope tem
Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. <t>TEM</t> images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at <t>100k×</t> magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).
Transmission Electron Microscope Tem, supplied by JEOL, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Milenia Biotech GmBH kinetic analyzer milenia
Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. <t>TEM</t> images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at <t>100k×</t> magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).
Kinetic Analyzer Milenia, supplied by Milenia Biotech GmBH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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brain products gmbh brain vision analyzer (bva) software
Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. <t>TEM</t> images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at <t>100k×</t> magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).
Brain Vision Analyzer (Bva) Software, supplied by brain products gmbh, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Integrated DNA Technologies ultramer format
Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. <t>TEM</t> images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at <t>100k×</t> magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).
Ultramer Format, supplied by Integrated DNA Technologies, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. <t>TEM</t> images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at <t>100k×</t> magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).
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ATCC anti west nile virus antibody responses 140
Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. <t>TEM</t> images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at <t>100k×</t> magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).
Anti West Nile Virus Antibody Responses 140, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Sequence homology analysis of immunodominant B cell <t>epitopes</t> among SARS-CoV-2 variants of concern: The figure represents the results of sequence homology analysis to assess the degree of conservancy of immunodominant B cell epitopes among SARS-CoV-2 variants of concern. Seventeen peptides, identified as potential B cell epitopes, were subjected to analysis, and categorized into conserved epitopes without mutation and conserved epitopes with mutation based on sequence similarity across different variants. Conserved epitopes exhibit a high degree of sequence conservation among variants, suggesting potential cross-reactivity and broad immune recognition. Conserved epitopes with mutation, on the other hand, show variability in sequence composition across variants, indicating potential immune evasion and reduced recognition by antibodies.
Mrna Vaccines, supplied by BioNTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. TEM images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at 100k× magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).

Journal: ACS applied materials & interfaces

Article Title: Cerium Oxide and Chondroitin Sulfate Doped Polyurethane Scaffold to Bridge Tendons.

doi: 10.1021/acsami.3c06144

Figure Lengend Snippet: Figure 1. SEM micrographs of (a) T6 (dimensional analysis: 351.57 ± 98.02 nm), (b) T9 (dimensional analysis: 349.80 ± 78.72 nm), and (c) T12 (dimensional analysis: 391.17 ± 50.34 nm) electrospun fibers at 10.0k× magnification. (d) SEM micrographs of random T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 430.17 ± 50.34, 402.07 ± 76.31, 566.60 ± 67.35, and 407.17 ± 36.62 nm, respectively) and after 6 days of hydration (dimensional analysis: 439.93 ± 47.13, 435.70 ± 92.08, 595.43 ± 92.08, and 439.77 ± 44.79 nm, respectively; % of fiber increase: 2.27 ± 0.50, 8.36 ± 1.10, 5.09 ± 0.90, and 8.01 ± 1.03%, respectively) at 5.0k× magnification. (e) SEM micrographs of aligned tubular T12, T12-CS, T12-CeO2, and T12-CS-CeO2 as electrospun (dimensional analysis: 505.81 ± 93.27, 433.27 ± 95.80, 518.07 ± 91.56, and 439.53 ± 67.92 nm) and after 6 days of hydration (dimensional analysis: 521.30 ± 96.11, 476.27 ± 114.67, 536.53 ± 107.66, and 468.80 ± 93.83 nm, respectively; % of fiber increase: 3.06 ± 0.70, 9.92 ± 1.40, 3.56 ± 0.60, and 6.66 ± 1.10%, respectively) at 5.0k× magnification. TEM images of (f) CeO2 powder, (g) T12-CeO2 scaffold, and (h) T12-CS-CeO2 scaffold at 100k× magnification. Scale bar: 200 nm (mean values ± s.d.; n = 90).

Article Snippet: The incorporation of the CeO2 nanoparticles into the fibrous matrix was assessed with a transmission electron microscope (TEM) (JEOL JEM-1200 EX II microscope; CCD camera Olympus Mega View G2 with 1376 × 1032 pixel format, Tokyo, Japan; operating HV at 100 kV; magnification 100k).

Techniques:

Sequence homology analysis of immunodominant B cell epitopes among SARS-CoV-2 variants of concern: The figure represents the results of sequence homology analysis to assess the degree of conservancy of immunodominant B cell epitopes among SARS-CoV-2 variants of concern. Seventeen peptides, identified as potential B cell epitopes, were subjected to analysis, and categorized into conserved epitopes without mutation and conserved epitopes with mutation based on sequence similarity across different variants. Conserved epitopes exhibit a high degree of sequence conservation among variants, suggesting potential cross-reactivity and broad immune recognition. Conserved epitopes with mutation, on the other hand, show variability in sequence composition across variants, indicating potential immune evasion and reduced recognition by antibodies.

Journal: Frontiers in Immunology

Article Title: Dynamics of spike-specific neutralizing antibodies across five-year emerging SARS-CoV-2 variants of concern reveal conserved epitopes that protect against severe COVID-19

doi: 10.3389/fimmu.2025.1503954

Figure Lengend Snippet: Sequence homology analysis of immunodominant B cell epitopes among SARS-CoV-2 variants of concern: The figure represents the results of sequence homology analysis to assess the degree of conservancy of immunodominant B cell epitopes among SARS-CoV-2 variants of concern. Seventeen peptides, identified as potential B cell epitopes, were subjected to analysis, and categorized into conserved epitopes without mutation and conserved epitopes with mutation based on sequence similarity across different variants. Conserved epitopes exhibit a high degree of sequence conservation among variants, suggesting potential cross-reactivity and broad immune recognition. Conserved epitopes with mutation, on the other hand, show variability in sequence composition across variants, indicating potential immune evasion and reduced recognition by antibodies.

Article Snippet: The design of COVID-19 vaccines has been heavily influenced by the need to elicit a strong antibody response against key B cell epitopes. mRNA vaccines, such as those developed by Pfizer-BioNTech and Moderna, encode the spike protein and stimulate an immune response targeting the RBD ( – ).

Techniques: Sequencing, Mutagenesis

The effect of immunization with Adeno-Associated Virus 9 based multiepitope-Coronavirus vaccine incorporating conserved human B cell epitopes on COVID-19-like symptoms detected from triple transgenic HLA-A*02:01/HLA-DRB1*01:01-hACE-2 mice and infected with highly pathogenic SARS-CoV-2 Delta variant of concern: (A) Experimental plan to study the effect of vaccination in triple transgenic HLA-A*02:01/HLA-DRB1*01:01-hACE-2 mice. On day 0 Triple transgenic HLA-A*02:01/HLA-DRB1*01:01-hACE-2 mice (7-8-week-old, n = 15) were vaccinated intranasally with two different AAV9 based multiepitope vaccines 2 x 10 10 Viral Particle per vaccine per mouse named as multiepitope vaccine containing 8 conserved B cell epitopes ( n = 5), control vaccine containing 6 B cell epitopes ( n = 5) and finally Mock vaccinated group that received 1XPBS ( n = 5) were used as control. At day 26 post immunization the blood was drown for ELISA and FFA and two days later mice intranasally challenged with 20ul of SARS-CoV-2 Delta (B.1.617.2) variant of concern at 1 x 10 4 pfu. Mice were followed for wight loss, survival, and viral titer for 14 days. (B) Data showing average percent weight change each day post immunization to the body weight on the day of infection. (C) shows the percentage survival detected in mice groups that received either multiepitope vaccine or control vaccine and finally the mock vaccinated group. (D) Viral titration data showing viral RNA copy number in the nasopharyngeal swabs of each group at days 2, 6, 10 and 14 post challenge Delta (B.1.617.2) variant. The IgG binding affinity specific for 6 “universal” B cell epitopes as well as the spike protein measured by ELISA are shown in panel (E) . The (F) panel represents neutralization percent by sera from mice that were given multiepitope vaccine, control vaccine or Mock vaccinated group against Alpha (B.1.1.7), Beta (B.1.351), Epsilon (B.1.427/B.1.429), Delta (B.1.617.2), and Omicron (XBB1.5). Bars represent means ± SEM. P values are calculated using unpaired t -test, comparing results obtained in vaccinated vs. mock-vaccinated mice.

Journal: Frontiers in Immunology

Article Title: Dynamics of spike-specific neutralizing antibodies across five-year emerging SARS-CoV-2 variants of concern reveal conserved epitopes that protect against severe COVID-19

doi: 10.3389/fimmu.2025.1503954

Figure Lengend Snippet: The effect of immunization with Adeno-Associated Virus 9 based multiepitope-Coronavirus vaccine incorporating conserved human B cell epitopes on COVID-19-like symptoms detected from triple transgenic HLA-A*02:01/HLA-DRB1*01:01-hACE-2 mice and infected with highly pathogenic SARS-CoV-2 Delta variant of concern: (A) Experimental plan to study the effect of vaccination in triple transgenic HLA-A*02:01/HLA-DRB1*01:01-hACE-2 mice. On day 0 Triple transgenic HLA-A*02:01/HLA-DRB1*01:01-hACE-2 mice (7-8-week-old, n = 15) were vaccinated intranasally with two different AAV9 based multiepitope vaccines 2 x 10 10 Viral Particle per vaccine per mouse named as multiepitope vaccine containing 8 conserved B cell epitopes ( n = 5), control vaccine containing 6 B cell epitopes ( n = 5) and finally Mock vaccinated group that received 1XPBS ( n = 5) were used as control. At day 26 post immunization the blood was drown for ELISA and FFA and two days later mice intranasally challenged with 20ul of SARS-CoV-2 Delta (B.1.617.2) variant of concern at 1 x 10 4 pfu. Mice were followed for wight loss, survival, and viral titer for 14 days. (B) Data showing average percent weight change each day post immunization to the body weight on the day of infection. (C) shows the percentage survival detected in mice groups that received either multiepitope vaccine or control vaccine and finally the mock vaccinated group. (D) Viral titration data showing viral RNA copy number in the nasopharyngeal swabs of each group at days 2, 6, 10 and 14 post challenge Delta (B.1.617.2) variant. The IgG binding affinity specific for 6 “universal” B cell epitopes as well as the spike protein measured by ELISA are shown in panel (E) . The (F) panel represents neutralization percent by sera from mice that were given multiepitope vaccine, control vaccine or Mock vaccinated group against Alpha (B.1.1.7), Beta (B.1.351), Epsilon (B.1.427/B.1.429), Delta (B.1.617.2), and Omicron (XBB1.5). Bars represent means ± SEM. P values are calculated using unpaired t -test, comparing results obtained in vaccinated vs. mock-vaccinated mice.

Article Snippet: The design of COVID-19 vaccines has been heavily influenced by the need to elicit a strong antibody response against key B cell epitopes. mRNA vaccines, such as those developed by Pfizer-BioNTech and Moderna, encode the spike protein and stimulate an immune response targeting the RBD ( – ).

Techniques: Virus, Transgenic Assay, Infection, Variant Assay, Vaccines, Control, Enzyme-linked Immunosorbent Assay, Titration, Binding Assay, Neutralization

IgG Response to conserved and non-conserved epitopes in COVID-19 patients infected with different SARS-CoV-2 variants: The figure displays six pie charts representing the IgG response to S 565-598 and S 13-37 epitopes (upper panel) and S 287-317 and S 601-628 (bottom panel) in COVID-19 patients infected with various SARS-CoV-2 variants of concern. Each pie chart corresponds to a specific variant, including Alpha, Beta, Gamma, Delta, Omicron BA.1, and Omicron BA.2, which appeared at different time points during the pandemic. In each pie chart, black segments represent the IgG response against conserved peptide sequences (S 565-598 and S 287-317 ), while white segments represent the IgG response against non-conserved peptide sequences (S 13-37 and S 601-628 ). The darker and lighter shades of the black and white segments indicate the relative magnitude of the IgG response to conserved and non-conserved epitopes, respectively.

Journal: Frontiers in Immunology

Article Title: Dynamics of spike-specific neutralizing antibodies across five-year emerging SARS-CoV-2 variants of concern reveal conserved epitopes that protect against severe COVID-19

doi: 10.3389/fimmu.2025.1503954

Figure Lengend Snippet: IgG Response to conserved and non-conserved epitopes in COVID-19 patients infected with different SARS-CoV-2 variants: The figure displays six pie charts representing the IgG response to S 565-598 and S 13-37 epitopes (upper panel) and S 287-317 and S 601-628 (bottom panel) in COVID-19 patients infected with various SARS-CoV-2 variants of concern. Each pie chart corresponds to a specific variant, including Alpha, Beta, Gamma, Delta, Omicron BA.1, and Omicron BA.2, which appeared at different time points during the pandemic. In each pie chart, black segments represent the IgG response against conserved peptide sequences (S 565-598 and S 287-317 ), while white segments represent the IgG response against non-conserved peptide sequences (S 13-37 and S 601-628 ). The darker and lighter shades of the black and white segments indicate the relative magnitude of the IgG response to conserved and non-conserved epitopes, respectively.

Article Snippet: The design of COVID-19 vaccines has been heavily influenced by the need to elicit a strong antibody response against key B cell epitopes. mRNA vaccines, such as those developed by Pfizer-BioNTech and Moderna, encode the spike protein and stimulate an immune response targeting the RBD ( – ).

Techniques: Infection, Variant Assay