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Antibodies to neutralising epitopes synergistically block the interaction of the receptor-binding domain of SARS-CoV-2 to ACE 2.

Clinical & translational immunology

Pandey M, Ozberk V, Eskandari S, Shalash AO, Joyce MA, Saffran HA, Day CJ, Lepletier A, Spillings BL, Mills JL, Calcutt A, Fan F, Williams JT, Stanisic DI, Hattingh L, Gerrard J, Skwarczynski M, Mak J, Jennings MP, Toth I, Tyrrell DL, Good MF.
PMID: 33732459
Clin Transl Immunology. 2021 Mar 07;10(3):e1260. doi: 10.1002/cti2.1260. eCollection 2021.

OBJECTIVES: A major COVID-19 vaccine strategy is to induce antibodies that prevent interaction between the Spike protein's receptor-binding domain (RBD) and angiotensin-converting enzyme 2 (ACE2). These vaccines will also induce T-cell responses. However, concerns were raised that aberrant vaccine-induced...

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Pandey M, Ozberk V, Eskandari S, et al. Antibodies to neutralising epitopes synergistically block the interaction of the receptor-binding domain of SARS-CoV-2 to ACE 2. Clin Transl Immunology. 2021;10(3):e1260doi: 10.1002/cti2.1260.
Pandey, M., Ozberk, V., Eskandari, S., Shalash, A. O., Joyce, M. A., Saffran, H. A., Day, C. J., Lepletier, A., Spillings, B. L., Mills, J. L., Calcutt, A., Fan, F., Williams, J. T., Stanisic, D. I., Hattingh, L., Gerrard, J., Skwarczynski, M., Mak, J., Jennings, M. P., Toth, I., Tyrrell, D. L., & Good, M. F. (2021). Antibodies to neutralising epitopes synergistically block the interaction of the receptor-binding domain of SARS-CoV-2 to ACE 2. Clinical & translational immunology, 10(3), e1260. https://doi.org/10.1002/cti2.1260
Pandey, Manisha, et al. "Antibodies to neutralising epitopes synergistically block the interaction of the receptor-binding domain of SARS-CoV-2 to ACE 2." Clinical & translational immunology vol. 10,3 (2021): e1260. doi: https://doi.org/10.1002/cti2.1260
Pandey M, Ozberk V, Eskandari S, Shalash AO, Joyce MA, Saffran HA, Day CJ, Lepletier A, Spillings BL, Mills JL, Calcutt A, Fan F, Williams JT, Stanisic DI, Hattingh L, Gerrard J, Skwarczynski M, Mak J, Jennings MP, Toth I, Tyrrell DL, Good MF. Antibodies to neutralising epitopes synergistically block the interaction of the receptor-binding domain of SARS-CoV-2 to ACE 2. Clin Transl Immunology. 2021 Mar 07;10(3):e1260. doi: 10.1002/cti2.1260. eCollection 2021. PMID: 33732459; PMCID: PMC7937407.
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Dengue Virus Serotype 1 Conformational Dynamics Confers Virus Strain-Dependent Patterns of Neutralization by Polyclonal Sera.

Journal of virology

VanBlargan LA, Milutinovic PS, Goo L, DeMaso CR, Durbin AP, Whitehead SS, Pierson TC, Dowd KA.
PMID: 34549976
J Virol. 2021 Nov 09;95(23):e0095621. doi: 10.1128/JVI.00956-21. Epub 2021 Sep 22.

Dengue virus cocirculates globally as four serotypes (DENV1 to -4) that vary up to 40% at the amino acid level. Viral strains within a serotype further cluster into multiple genotypes. Eliciting a protective tetravalent neutralizing antibody response is a...

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VanBlargan LA, Milutinovic PS, Goo L, et al. Dengue Virus Serotype 1 Conformational Dynamics Confers Virus Strain-Dependent Patterns of Neutralization by Polyclonal Sera. J Virol. 2021;95(23):e0095621doi: 10.1128/JVI.00956-21.
VanBlargan, L. A., Milutinovic, P. S., Goo, L., DeMaso, C. R., Durbin, A. P., Whitehead, S. S., Pierson, T. C., & Dowd, K. A. (2021). Dengue Virus Serotype 1 Conformational Dynamics Confers Virus Strain-Dependent Patterns of Neutralization by Polyclonal Sera. Journal of virology, 95(23), e0095621. https://doi.org/10.1128/JVI.00956-21
VanBlargan, Laura A, et al. "Dengue Virus Serotype 1 Conformational Dynamics Confers Virus Strain-Dependent Patterns of Neutralization by Polyclonal Sera." Journal of virology vol. 95,23 (2021): e0095621. doi: https://doi.org/10.1128/JVI.00956-21
VanBlargan LA, Milutinovic PS, Goo L, DeMaso CR, Durbin AP, Whitehead SS, Pierson TC, Dowd KA. Dengue Virus Serotype 1 Conformational Dynamics Confers Virus Strain-Dependent Patterns of Neutralization by Polyclonal Sera. J Virol. 2021 Nov 09;95(23):e0095621. doi: 10.1128/JVI.00956-21. Epub 2021 Sep 22. PMID: 34549976; PMCID: PMC8577358.
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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. 2021 Nov 24;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. (2021). 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 (2021): 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. 2021 Nov 24;300:114376. doi: 10.1016/j.jviromet.2021.114376. Epub 2021 Nov 24. PMID: 34826519.
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Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells.

Viruses

Oberhuber M, Schopf A, Hennrich AA, Santos-Mandujano R, Huhn AG, Seitz S, Riedel C, Conzelmann KK.
PMID: 34578307
Viruses. 2021 Aug 30;13(9). doi: 10.3390/v13091726.

Lyssaviruses are neurotropic rhabdoviruses thought to be restricted to mammalian hosts, and to originate from bats. The identification of lyssavirus sequences from amphibians and reptiles by metatranscriptomics thus comes as a surprise and challenges the mammalian origin of lyssaviruses....

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Oberhuber M, Schopf A, Hennrich AA, et al. Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells. Viruses. 2021;13(9)doi: 10.3390/v13091726.
Oberhuber, M., Schopf, A., Hennrich, A. A., Santos-Mandujano, R., Huhn, A. G., Seitz, S., Riedel, C., & Conzelmann, K. K. (2021). Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells. Viruses, 13(9), . https://doi.org/10.3390/v13091726
Oberhuber, Martina, et al. "Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells." Viruses vol. 13,9 (2021). doi: https://doi.org/10.3390/v13091726
Oberhuber M, Schopf A, Hennrich AA, Santos-Mandujano R, Huhn AG, Seitz S, Riedel C, Conzelmann KK. Glycoproteins of Predicted Amphibian and Reptile Lyssaviruses Can Mediate Infection of Mammalian and Reptile Cells. Viruses. 2021 Aug 30;13(9). doi: 10.3390/v13091726. PMID: 34578307; PMCID: PMC8473393.
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Immunogenicity of Cork and Loop Domains of Recombinant .

Avicenna journal of medical biotechnology

Esmaeilkhani H, Rasooli I, Hashemi M, Nazarian S, Sefid F.
PMID: 31057721
Avicenna J Med Biotechnol. 2019 Apr-Jun;11(2):180-186.

METHODS: The antigenic domains of RESULTS: The antibodies raised in mice could successfully recognize and bind antigenic domains. Passive immunization studies accomplished by immune rabbit serum inhibited the establishment of infection in mice.CONCLUSION: The results adapted from the present...

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Esmaeilkhani H, Rasooli I, Hashemi M, et al. Immunogenicity of Cork and Loop Domains of Recombinant . Avicenna J Med Biotechnol. 2019;11(2):180-186
Esmaeilkhani, H., Rasooli, I., Hashemi, M., Nazarian, S., & Sefid, F. (2019). Immunogenicity of Cork and Loop Domains of Recombinant . Avicenna journal of medical biotechnology, 11(2), 180-186.
Esmaeilkhani, Hamid, et al. "Immunogenicity of Cork and Loop Domains of Recombinant ." Avicenna journal of medical biotechnology vol. 11,2 (2019): 180-186.
Esmaeilkhani H, Rasooli I, Hashemi M, Nazarian S, Sefid F. Immunogenicity of Cork and Loop Domains of Recombinant . Avicenna J Med Biotechnol. 2019 Apr-Jun;11(2):180-186. PMID: 31057721; PMCID: PMC6490406.
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A Multi-Hemagglutinin-Based Enzyme-Linked Immunosorbent Assay to Serologically Detect Influenza A Virus Infection in Animals.

Veterinary sciences

Okumura M, Takenaka-Uema A, Murakami S, Horimoto T.
PMID: 31336638
Vet Sci. 2019 Jul 22;6(3). doi: 10.3390/vetsci6030064.

Mammals can play a role as an intermediate host in the emergence of mammalian-adapted reassortants or mutants of avian influenza A viruses, with pandemic potential. Therefore, detecting viral infection in animals followed by assessment of the hemagglutinin (HA) subtype...

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Okumura M, Takenaka-Uema A, Murakami S, et al. A Multi-Hemagglutinin-Based Enzyme-Linked Immunosorbent Assay to Serologically Detect Influenza A Virus Infection in Animals. Vet Sci. 2019;6(3)doi: 10.3390/vetsci6030064.
Okumura, M., Takenaka-Uema, A., Murakami, S., & Horimoto, T. (2019). A Multi-Hemagglutinin-Based Enzyme-Linked Immunosorbent Assay to Serologically Detect Influenza A Virus Infection in Animals. Veterinary sciences, 6(3), . https://doi.org/10.3390/vetsci6030064
Okumura, Miki, et al. "A Multi-Hemagglutinin-Based Enzyme-Linked Immunosorbent Assay to Serologically Detect Influenza A Virus Infection in Animals." Veterinary sciences vol. 6,3 (2019). doi: https://doi.org/10.3390/vetsci6030064
Okumura M, Takenaka-Uema A, Murakami S, Horimoto T. A Multi-Hemagglutinin-Based Enzyme-Linked Immunosorbent Assay to Serologically Detect Influenza A Virus Infection in Animals. Vet Sci. 2019 Jul 22;6(3). doi: 10.3390/vetsci6030064. PMID: 31336638; PMCID: PMC6789898.
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Incorporation of NS1 and prM/M are important to confer effective protection of adenovirus-vectored Zika virus vaccine carrying E protein.

NPJ vaccines

Liu X, Qu L, Ye X, Yi C, Zheng X, Hao M, Su W, Yao Z, Chen P, Zhang S, Feng Y, Wang Q, Yan Q, Li P, Li H, Li F, Pan W, Niu X, Xu R, Feng L, Chen L.
PMID: 30062066
NPJ Vaccines. 2018 Jul 24;3:29. doi: 10.1038/s41541-018-0072-6. eCollection 2018.

Current design of Zika virus (ZIKV) vaccine mainly considered envelope (E) as the major target antigen. Non-structural protein NS1 was seldom considered. Herein, we generated three adenovirus-vectored vaccines carrying E (Ad2-E), or premembrane/membrane (prM/M) with E (Ad2-prME), or NS1...

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Liu X, Qu L, Ye X, et al. Incorporation of NS1 and prM/M are important to confer effective protection of adenovirus-vectored Zika virus vaccine carrying E protein. NPJ Vaccines. 2018;3:29doi: 10.1038/s41541-018-0072-6.
Liu, X., Qu, L., Ye, X., Yi, C., Zheng, X., Hao, M., Su, W., Yao, Z., Chen, P., Zhang, S., Feng, Y., Wang, Q., Yan, Q., Li, P., Li, H., Li, F., Pan, W., Niu, X., Xu, R., Feng, L., & Chen, L. (2018). Incorporation of NS1 and prM/M are important to confer effective protection of adenovirus-vectored Zika virus vaccine carrying E protein. NPJ vaccines, 329. https://doi.org/10.1038/s41541-018-0072-6
Liu, Xinglong, et al. "Incorporation of NS1 and prM/M are important to confer effective protection of adenovirus-vectored Zika virus vaccine carrying E protein." NPJ vaccines vol. 3 (2018): 29. doi: https://doi.org/10.1038/s41541-018-0072-6
Liu X, Qu L, Ye X, Yi C, Zheng X, Hao M, Su W, Yao Z, Chen P, Zhang S, Feng Y, Wang Q, Yan Q, Li P, Li H, Li F, Pan W, Niu X, Xu R, Feng L, Chen L. Incorporation of NS1 and prM/M are important to confer effective protection of adenovirus-vectored Zika virus vaccine carrying E protein. NPJ Vaccines. 2018 Jul 24;3:29. doi: 10.1038/s41541-018-0072-6. eCollection 2018. PMID: 30062066; PMCID: PMC6057874.
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Production and characterization of polyclonal antibodies to human recombinant domain B-free antihemophilic factor VIII.

Turkish journal of biology = Turk biyoloji dergisi

Tykhomyrov A, Nedzvetsky V, Shemet S, Ağca CA.
PMID: 30814851
Turk J Biol. 2017 Dec 18;41(6):857-867. doi: 10.3906/biy-1704-10. eCollection 2017.

Moroctocog alpha is a human B-domain deleted recombinant factor VIII (BDDrFVIII), which represents a new generation of pure antihemophilic products. We describe here an optimized procedure for polyclonal anti-FVIII-antibody production with the use of BDDrFVIII as an immunogen. The...

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Tykhomyrov A, Nedzvetsky V, Shemet S, et al. Production and characterization of polyclonal antibodies to human recombinant domain B-free antihemophilic factor VIII. Turk J Biol. 2017;41(6):857-867doi: 10.3906/biy-1704-10.
Tykhomyrov, A., Nedzvetsky, V., Shemet, S., & Ağca, C. A. (2017). Production and characterization of polyclonal antibodies to human recombinant domain B-free antihemophilic factor VIII. Turkish journal of biology = Turk biyoloji dergisi, 41(6), 857-867. https://doi.org/10.3906/biy-1704-10
Tykhomyrov, Artem, et al. "Production and characterization of polyclonal antibodies to human recombinant domain B-free antihemophilic factor VIII." Turkish journal of biology = Turk biyoloji dergisi vol. 41,6 (2017): 857-867. doi: https://doi.org/10.3906/biy-1704-10
Tykhomyrov A, Nedzvetsky V, Shemet S, Ağca CA. Production and characterization of polyclonal antibodies to human recombinant domain B-free antihemophilic factor VIII. Turk J Biol. 2017 Dec 18;41(6):857-867. doi: 10.3906/biy-1704-10. eCollection 2017. PMID: 30814851; PMCID: PMC6353303.
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Identification of Tropomyosin and Its Immunological Properties from Larvae of Cattle Tick, Boophilus annulatus.

Iranian journal of parasitology

Nabian S, Taheri M, Fard RM, Aramoon M.
PMID: 23914237
Iran J Parasitol. 2013 Apr;8(2):242-8.

BACKGROUND: Boophilus annulatus is an obligate blood feeder tick that can cause great losses in animals due to anemia and its ability to injure its host skin directly. The aim of this study was identification of cattle humoral immune...

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Nabian S, Taheri M, Fard RM, et al. Identification of Tropomyosin and Its Immunological Properties from Larvae of Cattle Tick, Boophilus annulatus. Iran J Parasitol. 2013;8(2):242-8
Nabian, S., Taheri, M., Fard, R. M., & Aramoon, M. (2013). Identification of Tropomyosin and Its Immunological Properties from Larvae of Cattle Tick, Boophilus annulatus. Iranian journal of parasitology, 8(2), 242-8.
Nabian, S, et al. "Identification of Tropomyosin and Its Immunological Properties from Larvae of Cattle Tick, Boophilus annulatus." Iranian journal of parasitology vol. 8,2 (2013): 242-8.
Nabian S, Taheri M, Fard RM, Aramoon M. Identification of Tropomyosin and Its Immunological Properties from Larvae of Cattle Tick, Boophilus annulatus. Iran J Parasitol. 2013 Apr;8(2):242-8. PMID: 23914237; PMCID: PMC3724149.
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EXPERIMENTAL LIVER NECROSIS; IV. NUCLEIN METABOLISMS.

The Journal of experimental medicine

Jackson HC, Pearce RM.
PMID: 19867111
J Exp Med. 1907 Sep 21;9(5):569-77. doi: 10.1084/jem.9.5.569.

In necrosis of the liver of the dog produced by haemotoxic immune sera, the increased excretion of uric acid, purin bases and inorganic phosphorus pentoxide is the result of the hydrolysis of nuclear material occurring during the autolysis of...

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Jackson HC, Pearce RM. EXPERIMENTAL LIVER NECROSIS; IV. NUCLEIN METABOLISMS. J Exp Med. 1907;9(5):569-77doi: 10.1084/jem.9.5.569.
Jackson, H. C., & Pearce, R. M. (1907). EXPERIMENTAL LIVER NECROSIS; IV. NUCLEIN METABOLISMS. The Journal of experimental medicine, 9(5), 569-77. https://doi.org/10.1084/jem.9.5.569
Jackson, H C, and Pearce, R M. "EXPERIMENTAL LIVER NECROSIS; IV. NUCLEIN METABOLISMS." The Journal of experimental medicine vol. 9,5 (1907): 569-77. doi: https://doi.org/10.1084/jem.9.5.569
Jackson HC, Pearce RM. EXPERIMENTAL LIVER NECROSIS; IV. NUCLEIN METABOLISMS. J Exp Med. 1907 Sep 21;9(5):569-77. doi: 10.1084/jem.9.5.569. PMID: 19867111; PMCID: PMC2124686.
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STUDIES ON PNEUMOCOCCUS INFECTION IN ANIMALS : SECOND PAPER: ACTION OF IMMUNE SERA ON PNEUMOCOCCUS INFECTION.

The Journal of experimental medicine

Wadsworth AB.
PMID: 19867556
J Exp Med. 1912 Jul 01;16(1):78-102. doi: 10.1084/jem.16.1.78.

From the results of this study of the action of immune sera on pneumococcus infection it is evident that immune sera vary greatly in their curative value. Immune sera possess protective action, but protective action is not necessarily indicative...

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Wadsworth AB. STUDIES ON PNEUMOCOCCUS INFECTION IN ANIMALS : SECOND PAPER: ACTION OF IMMUNE SERA ON PNEUMOCOCCUS INFECTION. J Exp Med. 1912;16(1):78-102doi: 10.1084/jem.16.1.78.
Wadsworth, A. B. (1912). STUDIES ON PNEUMOCOCCUS INFECTION IN ANIMALS : SECOND PAPER: ACTION OF IMMUNE SERA ON PNEUMOCOCCUS INFECTION. The Journal of experimental medicine, 16(1), 78-102. https://doi.org/10.1084/jem.16.1.78
Wadsworth, A B. "STUDIES ON PNEUMOCOCCUS INFECTION IN ANIMALS : SECOND PAPER: ACTION OF IMMUNE SERA ON PNEUMOCOCCUS INFECTION." The Journal of experimental medicine vol. 16,1 (1912): 78-102. doi: https://doi.org/10.1084/jem.16.1.78
Wadsworth AB. STUDIES ON PNEUMOCOCCUS INFECTION IN ANIMALS : SECOND PAPER: ACTION OF IMMUNE SERA ON PNEUMOCOCCUS INFECTION. J Exp Med. 1912 Jul 01;16(1):78-102. doi: 10.1084/jem.16.1.78. PMID: 19867556; PMCID: PMC2124824.
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ETIOLOGY OF YELLOW FEVER : X. COMPARATIVE IMMUNOLOGICAL STUDIES ON LEPTOSPIRA ICTEROIDES AND LEPTOSPIRA ICTEROHAEMOORRHAGIAE.

The Journal of experimental medicine

Noguchi H.
PMID: 19868393
J Exp Med. 1920 Jan 31;31(2):135-58. doi: 10.1084/jem.31.2.135.

It has been previously reported that a filterable microorganism belonging to the genus Leptospira has been recovered from the blood or organs of human beings suffering from the disease known as yellow fever in Guayaquil, and that the organism,...

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Noguchi H. ETIOLOGY OF YELLOW FEVER : X. COMPARATIVE IMMUNOLOGICAL STUDIES ON LEPTOSPIRA ICTEROIDES AND LEPTOSPIRA ICTEROHAEMOORRHAGIAE. J Exp Med. 1920;31(2):135-58doi: 10.1084/jem.31.2.135.
Noguchi, H. (1920). ETIOLOGY OF YELLOW FEVER : X. COMPARATIVE IMMUNOLOGICAL STUDIES ON LEPTOSPIRA ICTEROIDES AND LEPTOSPIRA ICTEROHAEMOORRHAGIAE. The Journal of experimental medicine, 31(2), 135-58. https://doi.org/10.1084/jem.31.2.135
Noguchi, H. "ETIOLOGY OF YELLOW FEVER : X. COMPARATIVE IMMUNOLOGICAL STUDIES ON LEPTOSPIRA ICTEROIDES AND LEPTOSPIRA ICTEROHAEMOORRHAGIAE." The Journal of experimental medicine vol. 31,2 (1920): 135-58. doi: https://doi.org/10.1084/jem.31.2.135
Noguchi H. ETIOLOGY OF YELLOW FEVER : X. COMPARATIVE IMMUNOLOGICAL STUDIES ON LEPTOSPIRA ICTEROIDES AND LEPTOSPIRA ICTEROHAEMOORRHAGIAE. J Exp Med. 1920 Jan 31;31(2):135-58. doi: 10.1084/jem.31.2.135. PMID: 19868393; PMCID: PMC2128223.
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