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ON CROSS REACTIONS OF IMMUNE SERA TO AZOPROTEINS.

The Journal of experimental medicine

Landsteiner K, van der Scheer J.
PMID: 19870475
J Exp Med. 1936 Feb 29;63(3):325-39. doi: 10.1084/jem.63.3.325.

The phenomena observed on absorption of immune sera to azoproteins with heterologous azoantigens lead to the conclusion that in general the sera do not contain a single antibody but antibody fractions somewhat different in their reactivity for heterologous antigens....

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Landsteiner K, van der Scheer J. ON CROSS REACTIONS OF IMMUNE SERA TO AZOPROTEINS. J Exp Med. 1936;63(3):325-39doi: 10.1084/jem.63.3.325.
Landsteiner, K., & van der Scheer, J. (1936). ON CROSS REACTIONS OF IMMUNE SERA TO AZOPROTEINS. The Journal of experimental medicine, 63(3), 325-39. https://doi.org/10.1084/jem.63.3.325
Landsteiner, K, and van der Scheer, J. "ON CROSS REACTIONS OF IMMUNE SERA TO AZOPROTEINS." The Journal of experimental medicine vol. 63,3 (1936): 325-39. doi: https://doi.org/10.1084/jem.63.3.325
Landsteiner K, van der Scheer J. ON CROSS REACTIONS OF IMMUNE SERA TO AZOPROTEINS. J Exp Med. 1936 Feb 29;63(3):325-39. doi: 10.1084/jem.63.3.325. PMID: 19870475; PMCID: PMC2133341.
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A mosaic hemagglutinin-based influenza virus vaccine candidate protects mice from challenge with divergent H3N2 strains.

NPJ vaccines

Broecker F, Liu STH, Suntronwong N, Sun W, Bailey MJ, Nachbagauer R, Krammer F, Palese P.
PMID: 31341648
NPJ Vaccines. 2019 Jul 19;4:31. doi: 10.1038/s41541-019-0126-4. eCollection 2019.

Current seasonal influenza virus vaccines only provide limited, short-lived protection, and antigenic drift in the hemagglutinin surface glycoprotein necessitates their annual re-formulation and re-administration. To overcome these limitations, universal vaccine strategies that aim at eliciting broadly protective antibodies to...

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Broecker F, Liu STH, Suntronwong N, et al. A mosaic hemagglutinin-based influenza virus vaccine candidate protects mice from challenge with divergent H3N2 strains. NPJ Vaccines. 2019;4:31doi: 10.1038/s41541-019-0126-4.
Broecker, F., Liu, S. T. H., Suntronwong, N., Sun, W., Bailey, M. J., Nachbagauer, R., Krammer, F., & Palese, P. (2019). A mosaic hemagglutinin-based influenza virus vaccine candidate protects mice from challenge with divergent H3N2 strains. NPJ vaccines, 431. https://doi.org/10.1038/s41541-019-0126-4
Broecker, Felix, et al. "A mosaic hemagglutinin-based influenza virus vaccine candidate protects mice from challenge with divergent H3N2 strains." NPJ vaccines vol. 4 (2019): 31. doi: https://doi.org/10.1038/s41541-019-0126-4
Broecker F, Liu STH, Suntronwong N, Sun W, Bailey MJ, Nachbagauer R, Krammer F, Palese P. A mosaic hemagglutinin-based influenza virus vaccine candidate protects mice from challenge with divergent H3N2 strains. NPJ Vaccines. 2019 Jul 19;4:31. doi: 10.1038/s41541-019-0126-4. eCollection 2019. PMID: 31341648; PMCID: PMC6642189.
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Complement enhances in vitro neutralizing potency of antibodies to human cytomegalovirus glycoprotein B (gB) and immune sera induced by gB/MF59 vaccination.

NPJ vaccines

Li F, Freed DC, Tang A, Rustandi RR, Troutman MC, Espeseth AS, Zhang N, An Z, McVoy M, Zhu H, Ha S, Wang D, Adler SP, Fu TM.
PMID: 29263890
NPJ Vaccines. 2017 Dec 14;2:36. doi: 10.1038/s41541-017-0038-0. eCollection 2017.

Human cytomegalovirus (HCMV) is the leading cause of in utero viral infection in the United States. Since congenital HCMV infection can lead to birth defects in newborns, developing a prophylactic vaccine is a high priority. One of the early...

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Li F, Freed DC, Tang A, et al. Complement enhances in vitro neutralizing potency of antibodies to human cytomegalovirus glycoprotein B (gB) and immune sera induced by gB/MF59 vaccination. NPJ Vaccines. 2017;2:36doi: 10.1038/s41541-017-0038-0.
Li, F., Freed, D. C., Tang, A., Rustandi, R. R., Troutman, M. C., Espeseth, A. S., Zhang, N., An, Z., McVoy, M., Zhu, H., Ha, S., Wang, D., Adler, S. P., & Fu, T. M. (2017). Complement enhances in vitro neutralizing potency of antibodies to human cytomegalovirus glycoprotein B (gB) and immune sera induced by gB/MF59 vaccination. NPJ vaccines, 236. https://doi.org/10.1038/s41541-017-0038-0
Li, Fengsheng, et al. "Complement enhances in vitro neutralizing potency of antibodies to human cytomegalovirus glycoprotein B (gB) and immune sera induced by gB/MF59 vaccination." NPJ vaccines vol. 2 (2017): 36. doi: https://doi.org/10.1038/s41541-017-0038-0
Li F, Freed DC, Tang A, Rustandi RR, Troutman MC, Espeseth AS, Zhang N, An Z, McVoy M, Zhu H, Ha S, Wang D, Adler SP, Fu TM. Complement enhances in vitro neutralizing potency of antibodies to human cytomegalovirus glycoprotein B (gB) and immune sera induced by gB/MF59 vaccination. NPJ Vaccines. 2017 Dec 14;2:36. doi: 10.1038/s41541-017-0038-0. eCollection 2017. PMID: 29263890; PMCID: PMC5730571.
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Point Mutations in Retargeted gD Eliminate the Sensitivity of EGFR/EGFRvIII-Targeted HSV to Key Neutralizing Antibodies.

Molecular therapy. Methods & clinical development

Tuzmen C, Cairns TM, Atanasiu D, Lou H, Saw WT, Hall BL, Cohen JB, Cohen GH, Glorioso JC.
PMID: 32042851
Mol Ther Methods Clin Dev. 2020 Jan 13;16:145-154. doi: 10.1016/j.omtm.2019.12.013. eCollection 2020 Mar 13.

Effective oncolytic virotherapy may require systemic delivery, tumor targeting, and resistance to virus-neutralizing (VN) antibodies. Since herpes simplex virus (HSV) glycoprotein D (gD) is the viral attachment/entry protein and predominant VN target, we examined the impact of gD retargeting...

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Tuzmen C, Cairns TM, Atanasiu D, et al. Point Mutations in Retargeted gD Eliminate the Sensitivity of EGFR/EGFRvIII-Targeted HSV to Key Neutralizing Antibodies. Mol Ther Methods Clin Dev. 2020;16:145-154doi: 10.1016/j.omtm.2019.12.013.
Tuzmen, C., Cairns, T. M., Atanasiu, D., Lou, H., Saw, W. T., Hall, B. L., Cohen, J. B., Cohen, G. H., & Glorioso, J. C. (2020). Point Mutations in Retargeted gD Eliminate the Sensitivity of EGFR/EGFRvIII-Targeted HSV to Key Neutralizing Antibodies. Molecular therapy. Methods & clinical development, 16145-154. https://doi.org/10.1016/j.omtm.2019.12.013
Tuzmen, Ceren, et al. "Point Mutations in Retargeted gD Eliminate the Sensitivity of EGFR/EGFRvIII-Targeted HSV to Key Neutralizing Antibodies." Molecular therapy. Methods & clinical development vol. 16 (2020): 145-154. doi: https://doi.org/10.1016/j.omtm.2019.12.013
Tuzmen C, Cairns TM, Atanasiu D, Lou H, Saw WT, Hall BL, Cohen JB, Cohen GH, Glorioso JC. Point Mutations in Retargeted gD Eliminate the Sensitivity of EGFR/EGFRvIII-Targeted HSV to Key Neutralizing Antibodies. Mol Ther Methods Clin Dev. 2020 Jan 13;16:145-154. doi: 10.1016/j.omtm.2019.12.013. eCollection 2020 Mar 13. PMID: 32042851; PMCID: PMC7000558.
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Comparison of the neutralizing activities of antibodies in clinical sera against both Sabin and wild-type polio pseudoviruses.

Journal of virological methods

Liu S, Lu W, Ma S, Guo H, Zhang Z, Li X.
PMID: 34826519
J Virol Methods. 2022 Feb;300:114376. doi: 10.1016/j.jviromet.2021.114376. Epub 2021 Nov 24.

The cost-effectiveness of the Sabin inactivated poliovirus vaccine derived from the Sabin strains (S-IPV) and its reduced biosecurity risks during its manufacture make it the vaccine of choice over the IPVs derived from wild-type polioviruses. However, it is difficult...

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Liu S, Lu W, Ma S, et al. Comparison of the neutralizing activities of antibodies in clinical sera against both Sabin and wild-type polio pseudoviruses. J Virol Methods. 2021;300:114376doi: 10.1016/j.jviromet.2021.114376.
Liu, S., Lu, W., Ma, S., Guo, H., Zhang, Z., & Li, X. (2022). Comparison of the neutralizing activities of antibodies in clinical sera against both Sabin and wild-type polio pseudoviruses. Journal of virological methods, 300114376. https://doi.org/10.1016/j.jviromet.2021.114376
Liu, Shaohua, et al. "Comparison of the neutralizing activities of antibodies in clinical sera against both Sabin and wild-type polio pseudoviruses." Journal of virological methods vol. 300 (2022): 114376. doi: https://doi.org/10.1016/j.jviromet.2021.114376
Liu S, Lu W, Ma S, Guo H, Zhang Z, Li X. Comparison of the neutralizing activities of antibodies in clinical sera against both Sabin and wild-type polio pseudoviruses. J Virol Methods. 2022 Feb;300:114376. doi: 10.1016/j.jviromet.2021.114376. Epub 2021 Nov 24. PMID: 34826519.
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Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix.

Veterinary parasitology

Qu G, Xu Z, Tuo W, Li C, Lillehoj H, Wan G, Gong H, Huang J, Tian G, Li S, Liu Y, Liu L.
PMID: 34971828
Vet Parasitol. 2021 Dec 25;301:109642. doi: 10.1016/j.vetpar.2021.109642. Epub 2021 Dec 25.

Eimeria necatrix, an apicomplexan protozoa of the genus Eimeria, causes intestinal coccidiosis that can reduce growth performance of poultry and result in high mortality in older chickens. In this report, the whole sporozoite proteins of E.necatrix were studied by...

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Qu G, Xu Z, Tuo W, et al. Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix. Vet Parasitol. 2021;301:109642doi: 10.1016/j.vetpar.2021.109642.
Qu, G., Xu, Z., Tuo, W., Li, C., Lillehoj, H., Wan, G., Gong, H., Huang, J., Tian, G., Li, S., Liu, Y., & Liu, L. (2021). Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix. Veterinary parasitology, 301109642. https://doi.org/10.1016/j.vetpar.2021.109642
Qu, Guanggang, et al. "Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix." Veterinary parasitology vol. 301 (2021): 109642. doi: https://doi.org/10.1016/j.vetpar.2021.109642
Qu G, Xu Z, Tuo W, Li C, Lillehoj H, Wan G, Gong H, Huang J, Tian G, Li S, Liu Y, Liu L. Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix. Vet Parasitol. 2021 Dec 25;301:109642. doi: 10.1016/j.vetpar.2021.109642. Epub 2021 Dec 25. PMID: 34971828.
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Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix.

Veterinary parasitology

Qu G, Xu Z, Tuo W, Li C, Lillehoj H, Wan G, Gong H, Huang J, Tian G, Li S, Liu Y, Liu L.
PMID: 34971828
Vet Parasitol. 2022 Jan;301:109642. doi: 10.1016/j.vetpar.2021.109642. Epub 2021 Dec 25.

Eimeria necatrix, an apicomplexan protozoa of the genus Eimeria, causes intestinal coccidiosis that can reduce growth performance of poultry and result in high mortality in older chickens. In this report, the whole sporozoite proteins of E.necatrix were studied by...

Cite
Qu G, Xu Z, Tuo W, et al. Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix. Vet Parasitol. 2021;301:109642doi: 10.1016/j.vetpar.2021.109642.
Qu, G., Xu, Z., Tuo, W., Li, C., Lillehoj, H., Wan, G., Gong, H., Huang, J., Tian, G., Li, S., Liu, Y., & Liu, L. (2022). Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix. Veterinary parasitology, 301109642. https://doi.org/10.1016/j.vetpar.2021.109642
Qu, Guanggang, et al. "Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix." Veterinary parasitology vol. 301 (2022): 109642. doi: https://doi.org/10.1016/j.vetpar.2021.109642
Qu G, Xu Z, Tuo W, Li C, Lillehoj H, Wan G, Gong H, Huang J, Tian G, Li S, Liu Y, Liu L. Immunoproteomic analysis of the sporozoite antigens of Eimeria necatrix. Vet Parasitol. 2022 Jan;301:109642. doi: 10.1016/j.vetpar.2021.109642. Epub 2021 Dec 25. PMID: 34971828.
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Validation of a SARS-CoV-2 spike protein ELISA for use in contact investigations and serosurveillance.

bioRxiv : the preprint server for biology

Freeman B, Lester S, Mills L, Rasheed MAU, Moye S, Abiona O, Hutchinson GB, Morales-Betoulle M, Krapinunaya I, Gibbons A, Chiang CF, Cannon D, Klena J, Johnson JA, Owen SM, Graham BS, Corbett KS, Thornburg NJ.
PMID: 32511332
bioRxiv. 2020 Apr 25; doi: 10.1101/2020.04.24.057323.

Since emergence of SARS-CoV-2 in late 2019, there has been a critical need to understand prevalence, transmission patterns, to calculate the burden of disease and case fatality rates. Molecular diagnostics, the gold standard for identifying viremic cases, are not...

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Freeman B, Lester S, Mills L, et al. Validation of a SARS-CoV-2 spike protein ELISA for use in contact investigations and serosurveillance. bioRxiv. 2020;doi: 10.1101/2020.04.24.057323.
Freeman, B., Lester, S., Mills, L., Rasheed, M. A. U., Moye, S., Abiona, O., Hutchinson, G. B., Morales-Betoulle, M., Krapinunaya, I., Gibbons, A., Chiang, C. F., Cannon, D., Klena, J., Johnson, J. A., Owen, S. M., Graham, B. S., Corbett, K. S., & Thornburg, N. J. (2020). Validation of a SARS-CoV-2 spike protein ELISA for use in contact investigations and serosurveillance. bioRxiv : the preprint server for biology, . https://doi.org/10.1101/2020.04.24.057323
Freeman, Brandi, et al. "Validation of a SARS-CoV-2 spike protein ELISA for use in contact investigations and serosurveillance." bioRxiv : the preprint server for biology vol. (2020). doi: https://doi.org/10.1101/2020.04.24.057323
Freeman B, Lester S, Mills L, Rasheed MAU, Moye S, Abiona O, Hutchinson GB, Morales-Betoulle M, Krapinunaya I, Gibbons A, Chiang CF, Cannon D, Klena J, Johnson JA, Owen SM, Graham BS, Corbett KS, Thornburg NJ. Validation of a SARS-CoV-2 spike protein ELISA for use in contact investigations and serosurveillance. bioRxiv. 2020 Apr 25; doi: 10.1101/2020.04.24.057323. PMID: 32511332; PMCID: PMC7239067.
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SARS-CoV-2 recruits a haem metabolite to evade antibody immunity.

medRxiv : the preprint server for health sciences

Rosa A, Pye VE, Graham C, Muir L, Seow J, Ng KW, Cook NJ, Rees-Spear C, Parker E, Dos Santos MS, Rosadas C, Susana A, Rhys H, Nans A, Masino L, Roustan C, Christodoulou E, Ulferts R, Wrobel A, Short CE, Fertleman M, Sanders RW, Heaney J, Spyer M, Kjær S, Riddell A, Malim MH, Beale R, MacRae JI, Taylor GP, Nastouli E, van Gils MJ, Rosenthal PB, Pizzato M, McClure MO, Tedder RS, Kassiotis G, McCoy LE, Doores KJ, Cherepanov P.
PMID: 33532784
medRxiv. 2021 Jan 26; doi: 10.1101/2021.01.21.21249203.

The coronaviral spike is the dominant viral antigen and the target of neutralizing antibodies. We show that SARS-CoV-2 spike binds biliverdin and bilirubin, the tetrapyrrole products of haem metabolism, with nanomolar affinity. Using cryo-electron microscopy and X-ray crystallography we...

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Rosa A, Pye VE, Graham C, et al. SARS-CoV-2 recruits a haem metabolite to evade antibody immunity. medRxiv. 2021;doi: 10.1101/2021.01.21.21249203.
Rosa, A., Pye, V. E., Graham, C., Muir, L., Seow, J., Ng, K. W., Cook, N. J., Rees-Spear, C., Parker, E., Dos Santos, M. S., Rosadas, C., Susana, A., Rhys, H., Nans, A., Masino, L., Roustan, C., Christodoulou, E., Ulferts, R., Wrobel, A., Short, C. E., Fertleman, M., Sanders, R. W., Heaney, J., Spyer, M., Kjær, S., Riddell, A., Malim, M. H., Beale, R., MacRae, J. I., Taylor, G. P., Nastouli, E., van Gils, M. J., Rosenthal, P. B., Pizzato, M., McClure, M. O., Tedder, R. S., Kassiotis, G., McCoy, L. E., Doores, K. J., & Cherepanov, P. (2021). SARS-CoV-2 recruits a haem metabolite to evade antibody immunity. medRxiv : the preprint server for health sciences, . https://doi.org/10.1101/2021.01.21.21249203
Rosa, Annachiara, et al. "SARS-CoV-2 recruits a haem metabolite to evade antibody immunity." medRxiv : the preprint server for health sciences vol. (2021). doi: https://doi.org/10.1101/2021.01.21.21249203
Rosa A, Pye VE, Graham C, Muir L, Seow J, Ng KW, Cook NJ, Rees-Spear C, Parker E, Dos Santos MS, Rosadas C, Susana A, Rhys H, Nans A, Masino L, Roustan C, Christodoulou E, Ulferts R, Wrobel A, Short CE, Fertleman M, Sanders RW, Heaney J, Spyer M, Kjær S, Riddell A, Malim MH, Beale R, MacRae JI, Taylor GP, Nastouli E, van Gils MJ, Rosenthal PB, Pizzato M, McClure MO, Tedder RS, Kassiotis G, McCoy LE, Doores KJ, Cherepanov P. SARS-CoV-2 recruits a haem metabolite to evade antibody immunity. medRxiv. 2021 Jan 26; doi: 10.1101/2021.01.21.21249203. PMID: 33532784; PMCID: PMC7852234.
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Discovery of four new B-cell protective epitopes for malaria using Q beta virus-like particle as platform.

NPJ vaccines

Atcheson E, Cabral-Miranda G, Salman AM, Reyes-Sandoval A.
PMID: 34620882
NPJ Vaccines. 2020 Oct 08;5(1):92. doi: 10.1038/s41541-020-00242-y.

Malaria remains one of the world's most urgent global health problems, with almost half a million deaths and hundreds of millions of clinical cases each year. Existing interventions by themselves will not be enough to tackle infection in high-transmission...

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Atcheson E, Cabral-Miranda G, Salman AM, et al. Discovery of four new B-cell protective epitopes for malaria using Q beta virus-like particle as platform. NPJ Vaccines. 2020;5(1):92doi: 10.1038/s41541-020-00242-y.
Atcheson, E., Cabral-Miranda, G., Salman, A. M., & Reyes-Sandoval, A. (2020). Discovery of four new B-cell protective epitopes for malaria using Q beta virus-like particle as platform. NPJ vaccines, 5(1), 92. https://doi.org/10.1038/s41541-020-00242-y
Atcheson, Erwan, et al. "Discovery of four new B-cell protective epitopes for malaria using Q beta virus-like particle as platform." NPJ vaccines vol. 5,1 (2020): 92. doi: https://doi.org/10.1038/s41541-020-00242-y
Atcheson E, Cabral-Miranda G, Salman AM, Reyes-Sandoval A. Discovery of four new B-cell protective epitopes for malaria using Q beta virus-like particle as platform. NPJ Vaccines. 2020 Oct 08;5(1):92. doi: 10.1038/s41541-020-00242-y. PMID: 34620882.
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Omicron variant showed lower neutralizing sensitivity than other SARS-CoV-2 variants to immune sera elicited by vaccines after boost.

Emerging microbes & infections

Ai J, Zhang H, Zhang Y, Lin K, Zhang Y, Wu J, Wan Y, Huang Y, Song J, Fu Z, Wang H, Guo J, Jiang N, Fan M, Zhou Y, Zhao Y, Zhang Q, Liu Q, Lv J, Li P, Qiu C, Zhang W.
PMID: 34935594
Emerg Microbes Infect. 2021 Dec 22;1-24. doi: 10.1080/22221751.2021.2022440. Epub 2021 Dec 22.

No abstract available.

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Ai J, Zhang H, Zhang Y, et al. Omicron variant showed lower neutralizing sensitivity than other SARS-CoV-2 variants to immune sera elicited by vaccines after boost. Emerg Microbes Infect. 2021;1-24doi: 10.1080/22221751.2021.2022440.
Ai, J., Zhang, H., Zhang, Y., Lin, K., Zhang, Y., Wu, J., Wan, Y., Huang, Y., Song, J., Fu, Z., Wang, H., Guo, J., Jiang, N., Fan, M., Zhou, Y., Zhao, Y., Zhang, Q., Liu, Q., Lv, J., Li, P., Qiu, C., & Zhang, W. (2021). Omicron variant showed lower neutralizing sensitivity than other SARS-CoV-2 variants to immune sera elicited by vaccines after boost. Emerging microbes & infections, 1-24. https://doi.org/10.1080/22221751.2021.2022440
Ai, Jingwen, et al. "Omicron variant showed lower neutralizing sensitivity than other SARS-CoV-2 variants to immune sera elicited by vaccines after boost." Emerging microbes & infections vol. (2021): 1-24. doi: https://doi.org/10.1080/22221751.2021.2022440
Ai J, Zhang H, Zhang Y, Lin K, Zhang Y, Wu J, Wan Y, Huang Y, Song J, Fu Z, Wang H, Guo J, Jiang N, Fan M, Zhou Y, Zhao Y, Zhang Q, Liu Q, Lv J, Li P, Qiu C, Zhang W. Omicron variant showed lower neutralizing sensitivity than other SARS-CoV-2 variants to immune sera elicited by vaccines after boost. Emerg Microbes Infect. 2021 Dec 22;1-24. doi: 10.1080/22221751.2021.2022440. Epub 2021 Dec 22. PMID: 34935594.
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Potency of BNT162b2 and mRNA-1273 vaccine-induced neutralizing antibodies against severe acute respiratory syndrome-CoV-2 variants of concern: A systematic review of in vitro studies.

Reviews in medical virology

Noori M, Nejadghaderi SA, Arshi S, Carson-Chahhoud K, Ansarin K, Kolahi AA, Safiri S.
PMID: 34286893
Rev Med Virol. 2021 Jul 19;e2277. doi: 10.1002/rmv.2277. Epub 2021 Jul 19.

BNT162b2 and mRNA-1273 are two types of mRNA-based vaccine platforms that have received emergency use authorization. The emergence of novel severe acute respiratory syndrome (SARS-CoV-2) variants has raised concerns of reduced sensitivity to neutralization by their elicited antibodies. We...

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Noori M, Nejadghaderi SA, Arshi S, et al. Potency of BNT162b2 and mRNA-1273 vaccine-induced neutralizing antibodies against severe acute respiratory syndrome-CoV-2 variants of concern: A systematic review of in vitro studies. Rev Med Virol. 2021;e2277doi: 10.1002/rmv.2277.
Noori, M., Nejadghaderi, S. A., Arshi, S., Carson-Chahhoud, K., Ansarin, K., Kolahi, A. A., & Safiri, S. (2021). Potency of BNT162b2 and mRNA-1273 vaccine-induced neutralizing antibodies against severe acute respiratory syndrome-CoV-2 variants of concern: A systematic review of in vitro studies. Reviews in medical virology, e2277. https://doi.org/10.1002/rmv.2277
Noori, Maryam, et al. "Potency of BNT162b2 and mRNA-1273 vaccine-induced neutralizing antibodies against severe acute respiratory syndrome-CoV-2 variants of concern: A systematic review of in vitro studies." Reviews in medical virology vol. (2021): e2277. doi: https://doi.org/10.1002/rmv.2277
Noori M, Nejadghaderi SA, Arshi S, Carson-Chahhoud K, Ansarin K, Kolahi AA, Safiri S. Potency of BNT162b2 and mRNA-1273 vaccine-induced neutralizing antibodies against severe acute respiratory syndrome-CoV-2 variants of concern: A systematic review of in vitro studies. Rev Med Virol. 2021 Jul 19;e2277. doi: 10.1002/rmv.2277. Epub 2021 Jul 19. PMID: 34286893; PMCID: PMC8420542.
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