Journal: bioRxiv

Article Title: Preliminary stability studies of a ß-SARS-CoV-2 virus-like particle vaccine

doi: 10.64898/2026.03.11.711036

Figure Lengend Snippet: ELISA analysis of ß-SARS-CoV-2 VLPs in PBS or mixed with excipients PS80, sorbitol or L-histidine and incubated at 4 °C for 14 days. Plates were coated with ß-SARS-CoV-2 VLPs followed by probing with anti-Spike antibody in 2-fold dilutions from 1:400 to 1:51200 (mean ± SD). ELISAs were performed three times and each dilution tested in triplicate. Samples were collected on days 1, 5, 7 and 14 for ELISA analysis, probing with polyclonal anti-S antibody. Experiments were performed in triplicate.

Article Snippet: Following separation by SDS-PAGE and transfer to polyvinylidene fluoride (PVDF) membrane, blots were probed with anti-S (40591-T62, Sino Biologicals), anti-M (MBS434281, MyBioSource) and anti-E (MBS8309656, MyBioSource) antibodies for SARS-CoV-2 VLPs as described previously ( , ).

Techniques: Enzyme-linked Immunosorbent Assay, Incubation

Journal: RSC Chemical Biology

Article Title: Chemical modulation of the unfolded protein response reveals an antiviral role for the PERK pathway in human coronavirus 229E infection

doi: 10.1039/d5cb00242g

Figure Lengend Snippet: The antiviral effect of Tg against HCoV-229E infection does not require IRE1, ATF6, or PERK expression. (A) Stable UPR knockdown A549 cell lines were generated via lentiviral transduction. Silencing of protein expression was confirmed via western blot. (B–F) A549 shCTRL, shIRE1, shATF6, and shPERK cells were primed with DMSO or Tg (0.05 µM) for 30 minutes, then washed prior to infection with HCoV-229E (MOI 0.05). Cell lysates (B–E) or supernatants (F) were collected at 24 hpi. (B–D) Protein expression of IRE1, ATF6, PERK and HCoV-229E N were assessed by western blot. (E) Changes in gene expression were quantified by RT-qPCR. Data are normalized to actin and set relative to shCTRL DMSO. (F) Supernatants were used to determine viral titers by plaque assay on Huh7 cells. Due to variability between replicates, titration data is expressed as a percentage relative to the shCTRL DMSO in each experiment. Graphs show means ± SD from 3 independent experiments, with qPCR performed in technical triplicate. Statistical significance was assessed by two-way ANOVA (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001).

Article Snippet: Primary antibodies against IRE1α (Cell Signaling Technology (CST) 3294, dilution 1 : 1000), ATF6 (CST 8089, dilution 1 : 1000), PERK (CST 5683, dilution 1 : 1000), XBP1s (CST 12782T, dilution 1 : 1000), HERPUD1 (Abcam ab150424, dilution 1 : 1000), HCoV-229E N (SinoBiological 40640-T62, dilution 1 : 10 000), beta-actin (Abcam ab8226, dilution 1 : 5000), alpha-tubulin (Thermo Scientific MA5-31466, dilution 1 : 5000), and GAPDH (Thermo Scientific MA5-15738, dilution 1 : 1000) were used for western blotting.

Techniques: Infection, Expressing, Knockdown, Generated, Transduction, Western Blot, Gene Expression, Quantitative RT-PCR, Plaque Assay, Titration

Journal: RSC Chemical Biology

Article Title: Chemical modulation of the unfolded protein response reveals an antiviral role for the PERK pathway in human coronavirus 229E infection

doi: 10.1039/d5cb00242g

Figure Lengend Snippet: Pharmacological inhibition of IRE1 or ATF6 does not affect the antiviral activity of Tg against HCoV-229E infection. (A and B) A549 cells were primed with DMSO or Tg (0.05 µM) in the absence or presence of KIRA6 (10 µM) or Ceapin-A7 (6 µM). Cell lysates were collected at 24 hours post-treatment. Xbp1s (A) or HERPUD1 (B) protein expression was assessed by western blot. (C) A549 cells were treated with DMSO, KIRA6 (10 µM), or Ceapin-A7 (6 µM) for 24 hours. Alamar blue assay was used to assess cell viability, which is expressed as a percentage relative to DMSO. (D and F) A549 cells were primed with DMSO or Tg (0.05 µM) in the presence or absence of KIRA6 (10 µM), then washed prior to infection with HCoV-229E (MOI 0.05). Viral inoculum was removed 2 hours later and replaced with media containing DMSO or KIRA6 (10 µM). Cell lysates were collected at 24 hpi to assess XBP1s and N gene expression by RT-qPCR (D and F), or Xbp1s and HCoV-229E N protein expression by western blot (E). (G and I) A549 cells were primed with DMSO or Tg (0.05 µM) in the presence or absence of Ceapin-A7 (6 µM), then washed prior to infection with HCoV-229E (MOI 0.05). Viral inoculum was removed 2 hours later and replaced with media containing DMSO or Ceapin-A7 (6 µM). Cell lysates were collected at 24 hpi to assess HERPUD1 and N expression by RT-qPCR (G and I), or HERPUD1 and HCoV-229E N protein expression by western blot (H). RT-qPCR data are normalized to actin and set relative to DMSO. (J) A549 cells were primed with DMSO or Tg (0.05 µM) in the presence or absence of KIRA6 (10 µM) or Ceapin-A7 (6 µM), alone or in combination, prior to infection with HCoV-229E (MOI 0.05). Inoculum was removed 2 hours later and replaced with media containing the respective inhibitor(s). Viral supernatants were collected 24 hpi and titrated by plaque assay on Huh7 cells. Graphs show mean ± SD from 2–3 independent experiments performed in triplicate, with qPCR performed in technical triplicate (* p < 0.05, *** p < 0.001; **** p < 0.0001). Representative western blots are shown.

Article Snippet: Primary antibodies against IRE1α (Cell Signaling Technology (CST) 3294, dilution 1 : 1000), ATF6 (CST 8089, dilution 1 : 1000), PERK (CST 5683, dilution 1 : 1000), XBP1s (CST 12782T, dilution 1 : 1000), HERPUD1 (Abcam ab150424, dilution 1 : 1000), HCoV-229E N (SinoBiological 40640-T62, dilution 1 : 10 000), beta-actin (Abcam ab8226, dilution 1 : 5000), alpha-tubulin (Thermo Scientific MA5-31466, dilution 1 : 5000), and GAPDH (Thermo Scientific MA5-15738, dilution 1 : 1000) were used for western blotting.

Techniques: Inhibition, Activity Assay, Infection, Expressing, Western Blot, Alamar Blue Assay, Gene Expression, Quantitative RT-PCR, Plaque Assay

Journal: RSC Chemical Biology

Article Title: Chemical modulation of the unfolded protein response reveals an antiviral role for the PERK pathway in human coronavirus 229E infection

doi: 10.1039/d5cb00242g

Figure Lengend Snippet: Pharmacological activation of PERK inhibits HCoV-229E replication. (A–C) A549 cells were treated with DMSO or one of the selective UPR activators for 24 hours. IXA4 (10 µM) activates IRE1, AA147 (10 µM) activates ATF6, and CCT020312 (5 µM) activates PERK. RNA lysates were collected 24 hours post-treatment and the expression of genes downstream of each UPR pathway was assessed by RT-qPCR. Data are normalized to actin and set relative to DMSO. (D) A549 cells were primed with Tg (0.5 µM) for 30 minutes, then washed and infected with HCoV-229E (MOI 0.5). Alternatively, cells were treated with AA147 (10 µM) or CCT020312 (5 µM) for 24 hpi. Cell lysates were collected to assess the expression of HERPUD1, PERK and 229E N protein by western blot. (F and G) A549 cells were primed with DMSO or Tg (0.05 µM) for 30 minutes prior to infection with HCoV-229E (MOI 0.05). Alternatively, cells were infected and then treated with media containing DMSO or the selective UPR activators alone or in combination. Cell lysates and supernatants were collected at 24 hpi. (F) Changes in HCoV-229E N gene expression were assessed by RT-qPCR. Data are normalized to actin and set relative to DMSO. (F) Viral titer was assessed by plaque assay on Huh7 cells. (H–J) A549 cells were infected with HCoV-229E (MOI 0.05), then incubated with increasing concentrations of CCT020312 for 24 h. Cell lysates were collected to assess changes in HCoV-229E N gene (H) and CHOP (I) expression by RT-qPCR. (J) Cell viability was assessed by Alamar blue assay. Graphs show means ± SD from 2–3 independent experiments performed in triplicate, with qPCR performed in technical triplicate. Statistical significance was assessed by one-way ANOVA or t -test (* p < 0.05, ** p < 0.01, *** p < 0.001; **** p < 0.0001).

Article Snippet: Primary antibodies against IRE1α (Cell Signaling Technology (CST) 3294, dilution 1 : 1000), ATF6 (CST 8089, dilution 1 : 1000), PERK (CST 5683, dilution 1 : 1000), XBP1s (CST 12782T, dilution 1 : 1000), HERPUD1 (Abcam ab150424, dilution 1 : 1000), HCoV-229E N (SinoBiological 40640-T62, dilution 1 : 10 000), beta-actin (Abcam ab8226, dilution 1 : 5000), alpha-tubulin (Thermo Scientific MA5-31466, dilution 1 : 5000), and GAPDH (Thermo Scientific MA5-15738, dilution 1 : 1000) were used for western blotting.

Techniques: Activation Assay, Expressing, Quantitative RT-PCR, Infection, Western Blot, Gene Expression, Plaque Assay, Incubation, Alamar Blue Assay

Journal: RSC Chemical Biology

Article Title: Chemical modulation of the unfolded protein response reveals an antiviral role for the PERK pathway in human coronavirus 229E infection

doi: 10.1039/d5cb00242g

Figure Lengend Snippet: UPR activation by tunicamycin does not recapitulate the antiviral effect of Tg. (A–C) A549 cells were primed with Tg (0.5 µM) for 30 minutes or with Tm (1 µg mL −1 ) for 4 hours. Cells were then washed and either mock-infected or infected with HCoV-229E (MOI 0.05). At 24 hpi, cell lysates were collected to evaluate expression of UPR target genes ( CHOP , HERPUD1 and Xbp1s ) or HCoV-229E N gene by qPCR. Graphs show means ± SD from 2 independent experiments, with qPCR performed in technical triplicate. Statistical significance was assessed by one-way or two-way ANOVA (* p < 0.05, ** p < 0.01, *** p < 0.001; **** p < 0.0001).

Article Snippet: Primary antibodies against IRE1α (Cell Signaling Technology (CST) 3294, dilution 1 : 1000), ATF6 (CST 8089, dilution 1 : 1000), PERK (CST 5683, dilution 1 : 1000), XBP1s (CST 12782T, dilution 1 : 1000), HERPUD1 (Abcam ab150424, dilution 1 : 1000), HCoV-229E N (SinoBiological 40640-T62, dilution 1 : 10 000), beta-actin (Abcam ab8226, dilution 1 : 5000), alpha-tubulin (Thermo Scientific MA5-31466, dilution 1 : 5000), and GAPDH (Thermo Scientific MA5-15738, dilution 1 : 1000) were used for western blotting.

Techniques: Activation Assay, Infection, Expressing

Journal: Viruses

Article Title: Characterization of Immune Response Diversity in Rodents Vaccinated with a Vesicular Stomatitis Virus Vectored COVID-19 Vaccine

doi: 10.3390/v14061127

Figure Lengend Snippet: Characterization of the recombinant VSV viruses. ( a ) Schematic diagrams showing genome organization of the rVSV. VSV g was replaced by SARS-CoV-2 S to generate rVSV-ΔG-S and rVSV-ΔG-S-eGFP. ( b ) Indirect immunofluorescence identification results of rVSV-ΔG-S and rVSV-ΔG-S-eGFP. Vero E6 cells were infected with rVSV-ΔG-S or rVSV-ΔG-S-eGFP and recognized by SARS-CoV-2-specific antibody and Alexa Fluor 568-conjugated secondary antibody, presented red fluorescence, rVSV-ΔG-S-eGFP presented green fluorescence. No fluorescence signal was observed in the VSV control. ( c ) Lysates of rVSV-ΔG-S/rVSV-ΔG-S-eGFP-infected Vero E6 cells, and VSV-infected Vero cells were blotted with an antibody recognizing SARS-CoV-2 S protein, a band representing S at 190 kDa was detected in rVSV-ΔG-S and rVSV-ΔG-S-eGFP group, no band was observed in the VSV control. ( d ) Growth kinetics of rVSV-ΔG-S, rVSV-ΔG-S-eGFP and VSV. Vero E6 cells were infected with the recombinant VSV viruses (MOI = 0.01) and virus titers in the supernatant were measured at the indicated time points post-infection.

Article Snippet: Rabbit polyclonal antibody against SARS-CoV-2 S protein (Cat. 40589-T62) was purchased from Sino Biological Inc (Beijing, China).

Techniques: Recombinant, Immunofluorescence, Infection, Fluorescence

Journal: Viruses

Article Title: Characterization of Immune Response Diversity in Rodents Vaccinated with a Vesicular Stomatitis Virus Vectored COVID-19 Vaccine

doi: 10.3390/v14061127

Figure Lengend Snippet: Virus-specific antibody and neutralizing antibody induced by rVSVΔG-S. ( a ) Weight change monitoring of BALB/c mice following vaccination for 7 days. i.m., i.n. and control refer to i.m. ( n = 10), i.n. inoculation group ( n = 10) and PBS inoculation control group ( n = 10), respectively same in ( b – f ). ( b ) RBD-specific IgG in mouse serum samples at 14, 28 and 42 dpv. ( c ) nAbs in the serum of mice at 14, 28, 42 and 56 dpv. ( d ) Weight changes in golden hamsters 7 days after vaccination. ( e ) RBD-specific IgG in the serum of golden hamsters at 14 and 28 dpv. ( f ) nAb titers in hamster serum samples at 14, 28 dpv and post-SARS-CoV-2 challenge. Data are presented as mean ± SEM. (* p < 0.05, ** p < 0.01,*** p < 0.001, **** p < 0.0001).

Article Snippet: Rabbit polyclonal antibody against SARS-CoV-2 S protein (Cat. 40589-T62) was purchased from Sino Biological Inc (Beijing, China).

Techniques:

Journal: Viruses

Article Title: Characterization of Immune Response Diversity in Rodents Vaccinated with a Vesicular Stomatitis Virus Vectored COVID-19 Vaccine

doi: 10.3390/v14061127

Figure Lengend Snippet: Antibody subtype and cytokines induced by rVSVΔG-S in BALB/c mice. I.m., i.n. and control refer to i.m. ( n = 4), i.n. inoculation group ( n = 4) and PBS inoculation control group ( n = 2), respectively (same in b–f). ( a ) RBD-specific IgG1 and IgG2a induced by the rVSV vaccine in mice. ( b , c ) Splenocyte IFN-γ and IL-4 induced by the rVSV vaccine in mice. ( d ) Ratio of IgG2a/IgG1 in i.m. and i.n. group. ( e , f ) CD3+CD4+ and CD3+CD8+ positive T cell proportions in splenocyte before and post-stimulation with 20 μg/mL RBD protein of SARS-CoV-2 for 36 h at 37 °C, 5% CO 2 . Data are presented as mean ± SEM. (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: Rabbit polyclonal antibody against SARS-CoV-2 S protein (Cat. 40589-T62) was purchased from Sino Biological Inc (Beijing, China).

Techniques:

Journal: Viruses

Article Title: Characterization of Immune Response Diversity in Rodents Vaccinated with a Vesicular Stomatitis Virus Vectored COVID-19 Vaccine

doi: 10.3390/v14061127

Figure Lengend Snippet: Protective efficacy of rVSV-ΔG-S in golden hamsters following SARS-CoV-2 challenge. i.m., i.n. and control refer to i.m. ( n = 5), i.n. inoculation group ( n = 5) and PBS inoculation group ( n = 2) who were challenged with SARS-CoV-2, respectively (same in b–f). Unchallenged control refers to hamsters inoculated with PBS and free from SARS-CoV-2 challenge ( n = 6). ( a ) Survival rate following SARS-CoV-2 challenge. ( b ) Body weight change in golden hamsters following SARS-CoV-2 challenge. ( c , d ) SARS-CoV-2 viral RNA copies in the lungs and nasal turbinates following SARS-CoV-2 challenge. ( e , f ) SARS-CoV-2 viral titers in the lungs and nasal turbinates following SARS-CoV-2 challenge. Data are presented as mean ± SEM. (* p < 0.05, *** p < 0.001, **** p < 0.0001).

Article Snippet: Rabbit polyclonal antibody against SARS-CoV-2 S protein (Cat. 40589-T62) was purchased from Sino Biological Inc (Beijing, China).

Techniques:

Journal: Viruses

Article Title: Characterization of Immune Response Diversity in Rodents Vaccinated with a Vesicular Stomatitis Virus Vectored COVID-19 Vaccine

doi: 10.3390/v14061127

Figure Lengend Snippet: Representative H&E staining and IHC of lung sections from SARS-CoV-2-infected golden hamsters at 3 days post-infection. Mock refers to hamsters inoculated with PBS and free from SARS-CoV-2 challenged. i.m., i.n. and control refer to i.m. inoculation group, i.n. inoculation group and PBS inoculation group who were challenged with SARS-CoV-2, respectively. In H&E staining sections, the thickened alveolar wall and proliferated epithelial cells are marked with yellow arrows, broken alveolar diaphragms and atrophic alveoli are marked with red arrows. In IHC sections, SARS-CoV-2 antigens that were recognized by SARS-CoV-2-N-specific antibodies were marked with red arrows.

Article Snippet: Rabbit polyclonal antibody against SARS-CoV-2 S protein (Cat. 40589-T62) was purchased from Sino Biological Inc (Beijing, China).

Techniques: Staining, Infection

Journal: The Journal of Clinical Investigation

Article Title: SARS-CoV-2 Delta and Omicron variants resist spike cleavage by human airway trypsin-like protease

doi: 10.1172/JCI174304

Figure Lengend Snippet: ( A – C ) Infectivity of WT ( A ), Delta ( B ), and Omicron BA.1 ( C ) pseudoviruses pretreated with nasal wash samples (NW) from young (20–30 years) and old (55–70 years) participants ( n = 10). ( D ) Infectivity of WT pseudovirus with respiratory tract proteases or proteins ( n = 3). ( E ) WT pseudovirus treated with NW, with or without HAT inhibitors aprotinin and soybean trypsin inhibitor (STI) ( n = 10). ( F ) HAT (2 μg/mL) pretreated with spike proteins, incubated with WT pseudovirus, determined infectivity ( n = 3). ( G and H ) Representative images ( G ) and quantification ( H ) of CPE in Vero E6 cells infected with live ancestral viruses, with or without HAT (0.5–5 μg/mL) ( n = 3). ( I and J ) Cell lysates collected 48 hours after infection with live viruses for gRNA ( I ) and sgRNA ( J ) assays ( n = 3). ( K ) The mRNA levels of tmprss11d in trachea (left) and lung (right) tissues in mice infected with SARS-CoV-2 on day 3 after infection ( n = 3 mice each group). ( L and M ) The representative images displayed conjugates (arrow) formed with SARS-CoV-2 spike protein (green) and released trypsin-like protease (red) in bronchial tissues of infected mice ( L ) and primates ( M ). ( N ) The images indicated SARS-CoV-2 particles (green) trapped by filamentous HAT (red) in the sputum of patients with COVID-19. The inset shows magnified conjugates in merged images. Data are representative ( D , F , G – J , and K ) of 2 independent experiments with 3 replicates each. Unpaired, 2-tailed Student’s t test was performed in D and K , and 1-way ANOVA analysis followed by Tukey’s multiple comparison post hoc test was conducted in A – C , E , F , and H – J . Scale bars: 200 μm in G ; 4 μm in L and M ; and 10 μm in N . Data are presented as mean values ± SEM in A – K . * P <0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

Article Snippet: For protein detection, the following antibodies were used: rabbit anti-SARS-CoV-2 S1 polyclonal antibodies (Sino Biological, 40591-T62), rabbit anti-SARS-CoV-2 S2 polyclonal antibodies (Sino Biological, 40590-T62), rabbit anti-SARS-CoV-2 N polyclonal antibodies (Sino Biological, 40143-R001), and horseradish peroxidase–conjugated (HRP-conjugated) anti-rabbit polyclonal antibodies (Thermo Fisher Scientific, 31460).

Techniques: Infection, Incubation, Comparison

Journal: The Journal of Clinical Investigation

Article Title: SARS-CoV-2 Delta and Omicron variants resist spike cleavage by human airway trypsin-like protease

doi: 10.1172/JCI174304

Figure Lengend Snippet: ( A ) 5 × 10 4 PFU of ancestral SARS-CoV-2, Delta, and Omicron (BA.1) variants were preincubated with PBS or 80 ng HAT in a total volume of 40 μL. After incubation at 37°C for 2 hours, 6–8 week-old female transgenic hACE2 (hACE2-KI/NIFDC) mice were intranasally instilled with the mixtures. The lung tissues were collected on day 3 after infection to determine the histopathological changes and the viral loads ( n = 5 mice each group). ( B and C ) Representative images of histopathological changes ( B ) and pathological score ( C ) in the lung tissues in each group. Scale bars represent 100 μm in B . ( D ) The levels of gRNA in mouse lung tissues on day 3 after infection in each group were detected by RT-qPCR. 1-way ANOVA followed by Tukey’s multiple comparison post hoc test was conducted in C and D . Data are presented as mean values ± SEM in C and D . **** P < 0.0001.

Article Snippet: For protein detection, the following antibodies were used: rabbit anti-SARS-CoV-2 S1 polyclonal antibodies (Sino Biological, 40591-T62), rabbit anti-SARS-CoV-2 S2 polyclonal antibodies (Sino Biological, 40590-T62), rabbit anti-SARS-CoV-2 N polyclonal antibodies (Sino Biological, 40143-R001), and horseradish peroxidase–conjugated (HRP-conjugated) anti-rabbit polyclonal antibodies (Thermo Fisher Scientific, 31460).

Techniques: Incubation, Transgenic Assay, Infection, Quantitative RT-PCR, Comparison

Journal: The Journal of Clinical Investigation

Article Title: SARS-CoV-2 Delta and Omicron variants resist spike cleavage by human airway trypsin-like protease

doi: 10.1172/JCI174304

Figure Lengend Snippet: ( A ) Coomassie staining analysis of spike protein cleavage by HAT. Spike protein alone was used as control. Numbers represent normalized band intensities. ( B and C ) Western blot assessed spike protein cleavage by HAT using anti-S1( B ) and anti-S2 ( C ) antibodies. ( D ) Live viruses produced in Vero E6 cells, preincubated with HAT (2 μg/mL) with or without aprotinin, then assayed by Western blot using S1 (top) and nucleocapsid (bottom) antibodies. ( E ) The calculated spike cleavage rate in D . ( F ) A molecular model of HAT interacting with SARS-CoV-2 S proteins S1/S2 cleavage site. Proteins are shown in ribbon format, with HAT in cyan and the cleavage site in yellow. Important residues, including the catalytic triad H227, D272, and S368 and salt bridge R682–D362, are shown in stick form. ( G ) RMSD time evolution of SARS-CoV-2 S proteins S1/S2 cleavage site. ( H ) Time evolution of HAT-S1/S2 cleavage site contact area for SARS-CoV-2 S proteins. ( I and J ) Cleavage products of spike protein for mass spectrometry: in-gel collection, enzymatic digestion, and analysis. HAT cleaves spike protein at R682 site. ( K ) Diagram of cleavage and surrounding mutation sites in SARS-CoV-2 variants. ( L ) Infectivity of Mut-1 (R681P in Delta), Mut-2 (K679N in BA.1), and Mut-3 (H681P in BA.1) pseudoviruses preincubated with HAT (2 μg/mL) ( n = 3). ( M ) Infectivity of WT pseudovirus carrying P681R mutation pretreated with or without HAT (0.5–2 μg/mL) ( n = 3). ( N ) Time evolution of the RMSD of the S1/S2 cleavage site for BA.1 (N679K) or (P681H) mutation. ( O ) Time evolution of contact interface area between HAT and S1/S2 site for BA.1 (N679K) or (P681H) mutation. 2-way ANOVA followed by Šidák’s multiple comparisons test was conducted in L and M . Data are presented as mean values ± SEM. ** P < 0.01; **** P < 0.0001.

Article Snippet: For protein detection, the following antibodies were used: rabbit anti-SARS-CoV-2 S1 polyclonal antibodies (Sino Biological, 40591-T62), rabbit anti-SARS-CoV-2 S2 polyclonal antibodies (Sino Biological, 40590-T62), rabbit anti-SARS-CoV-2 N polyclonal antibodies (Sino Biological, 40143-R001), and horseradish peroxidase–conjugated (HRP-conjugated) anti-rabbit polyclonal antibodies (Thermo Fisher Scientific, 31460).

Techniques: Staining, Control, Western Blot, Produced, Mass Spectrometry, Mutagenesis, Infection