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Article ; Online: Monoclonal antibodies for prophylactic and therapeutic use against viral infections.

Both, Leonard / Banyard, Ashley C / van Dolleweerd, Craig / Wright, Edward / Ma, Julian K-C / Fooks, Anthony R

2013 Volume 31, Issue 12, Page(s) 1553–1559

Abstract: ... by highly potent monoclonal antibodies (mAbs). Cocktails of mAbs and bispecific constructs can be used ... Neutralizing antibodies play an essential part in antiviral immunity and are instrumental ... to simultaneously target multiple viral epitopes and to overcome issues of neutralization escape. Advances ...

Abstract	Neutralizing antibodies play an essential part in antiviral immunity and are instrumental in preventing or modulating viral diseases. Polyclonal antibody preparations are increasingly being replaced by highly potent monoclonal antibodies (mAbs). Cocktails of mAbs and bispecific constructs can be used to simultaneously target multiple viral epitopes and to overcome issues of neutralization escape. Advances in antibody engineering have led to a large array of novel mAb formats, while deeper insight into the biology of several viruses and increasing knowledge of their neutralizing epitopes has extended the list of potential targets. In addition, progress in developing inexpensive production platforms will make antiviral mAbs more widely available and affordable.
MeSH term(s)	Antibodies, Monoclonal/therapeutic use ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; Antibody Specificity ; Antiviral Agents/therapeutic use ; Humans ; Immunization, Passive ; Protein Engineering ; Virus Diseases/prevention & control ; Virus Diseases/therapy
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Antiviral Agents
Keywords	covid19
Language	English
Publishing date	2013-01-29
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2013.01.025
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Article: Monoclonal antibodies for prophylactic and therapeutic use against viral infections.

Both, Leonard / Banyard, Ashley C / van Dolleweerd, Craig / Wright, Edward / Ma, Julian K-C / Fooks, Anthony R

Pediatria polska

2013 Volume 88, Issue 5, Page(s) T15–T23

Abstract	Neutralizing antibodies play an essential part in antiviral immunity and are instrumental in preventing or modulating viral diseases. Polyclonal antibody preparations are increasingly being replaced by highly potent monoclonal antibodies (mAbs). Cocktails of mAbs and bispecific constructs can be used to simultaneously target multiple viral epitopes and to overcome issues of neutralization escape. Advances in antibody engineering have led to a large array of novel mAb formats, while deeper insight into the biology of several viruses and increasing knowledge of their neutralizing epitopes has extended the list of potential targets. In addition, progress in developing inexpensive production platforms will make antiviral mAbs more widely available and affordable.
Keywords	covid19
Language	English
Publishing date	2013-08-23
Publishing country	Poland
Document type	Journal Article ; Review
ZDB-ID	414020-5
ISSN	0031-3939
ISSN	0031-3939
DOI	10.1016/j.pepo.2013.08.006
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Article ; Online: Monoclonal antibodies for prophylactic and therapeutic use against viral infections

Both, Leonard / Banyard, Ashley C. / van Dolleweerd, Craig / Wright, Edward / Ma, Julian K.-C. / Fooks, Anthony R.

Pediatria Polska

Abstract: ... by highly potent monoclonal antibodies (mAbs). Cocktails of mAbs and bispecific constructs can be used ... Abstract Neutralizing antibodies play an essential part in antiviral immunity and are instrumental ... to simultaneously target multiple viral epitopes and to overcome issues of neutralization escape. Advances ...

Abstract	Abstract Neutralizing antibodies play an essential part in antiviral immunity and are instrumental in preventing or modulating viral diseases. Polyclonal antibody preparations are increasingly being replaced by highly potent monoclonal antibodies (mAbs). Cocktails of mAbs and bispecific constructs can be used to simultaneously target multiple viral epitopes and to overcome issues of neutralization escape. Advances in antibody engineering have led to a large array of novel mAb formats, while deeper insight into the biology of several viruses and increasing knowledge of their neutralizing epitopes has extended the list of potential targets. In addition, progress in developing inexpensive production platforms will make antiviral mAbs more widely available and affordable.
Keywords	covid19
Publisher	Elsevier
Document type	Article ; Online
DOI	10.1016/j.pepo.2013.08.006
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Article: Monoclonal antibodies for prophylactic and therapeutic use against viral infections

Both, Leonard / Banyard, Ashley C / van Dolleweerd, Craig / Wright, Edward / Ma, Julian K.-C / Fooks, Anthony R

Vaccine. 2013 Mar. 15, v. 31, no. 12

2013

Abstract	Neutralizing antibodies play an essential part in antiviral immunity and are instrumental in preventing or modulating viral diseases. Polyclonal antibody preparations are increasingly being replaced by highly potent monoclonal antibodies (mAbs). Cocktails of mAbs and bispecific constructs can be used to simultaneously target multiple viral epitopes and to overcome issues of neutralization escape. Advances in antibody engineering have led to a large array of novel mAb formats, while deeper insight into the biology of several viruses and increasing knowledge of their neutralizing epitopes has extended the list of potential targets. In addition, progress in developing inexpensive production platforms will make antiviral mAbs more widely available and affordable.
Keywords	engineering ; epitopes ; immunity ; monoclonal antibodies ; neutralization ; neutralizing antibodies ; polyclonal antibodies ; vaccines ; viruses ; covid19
Language	English
Dates of publication	2013-0315
Size	p. 1553-1559.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2013.01.025
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Article ; Online: Therapeutic monoclonal antibodies for COVID-19 management: an update.

Chavda, Vivek P / Prajapati, Riddhi / Lathigara, Disha / Nagar, Bhumi / Kukadiya, Jay / Redwan, Elrashdy M / Uversky, Vladimir N / Kher, Mukesh N / Patel, Rajvi

Expert opinion on biological therapy

2022 Volume 22, Issue 6, Page(s) 763–780

Abstract: ... against COVID-19, and have shown a reduction of the viral load, as well as lowering hospitalizations and ... Expert opinion: Monoclonal antibodies represents the most effective and viable therapy and/or prophylaxis option ... such as prophylactic treatments, repurposed drug treatments, convalescent plasma, and polyclonal antibody therapy have ...

Abstract	Background: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has affected more than 529 million people, and today the world is facing different mutant strains of the virus, leading to increased morbidity rates, fatality rates, and surfacing re-infections. Various therapies, such as prophylactic treatments, repurposed drug treatments, convalescent plasma, and polyclonal antibody therapy have been developed to help combat the coronavirus disease 2019 (COVID-19). Area covered: This review article provides insights into the basic aspects of monoclonal antibodies (mAbs) for the therapy of COVID-19, as well as its advancement in terms of clinical trial and current approval status. Expert opinion: Monoclonal antibodies represents the most effective and viable therapy and/or prophylaxis option against COVID-19, and have shown a reduction of the viral load, as well as lowering hospitalizations and death rates. In different countries, various mAbs are undergoing different phases of clinical trials, with a few of them having entered phases III and IV. Due to the soaring number of cases worldwide, the FDA has given emergency approval for the mAb combinations bamlanivimab with etesevimab and casirivimab with imdevimab.
MeSH term(s)	Antibodies, Monoclonal/therapeutic use ; Antibodies, Monoclonal, Humanized ; Antibodies, Neutralizing/therapeutic use ; COVID-19/therapy ; Humans ; Immunization, Passive ; SARS-CoV-2
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Monoclonal, Humanized ; Antibodies, Neutralizing ; imdevimab (2Z3DQD2JHM) ; bamlanivimab (45I6OFJ8QH) ; casirivimab (J0FI6WE1QN) ; etesevimab (N7Q9NLF11I)
Language	English
Publishing date	2022-05-29
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2052501-1
ISSN	1744-7682 ; 1471-2598
ISSN (online)	1744-7682
ISSN	1471-2598
DOI	10.1080/14712598.2022.2078160
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Article ; Online: Specific Monoclonal Antibodies Targeting Unique HA Epitopes Block H7N9 Influenza A Viral Replication.

Shen, Wentao / Wang, Qian / Wang, Zhengxiang / Liu, Minxuan / Du, Yingying / Yuan, Lvfeng / Han, Lu / Smietanka, Krzysztof / Chen, Hualan / Xu, Shuai / Zhu, Qiyun

Journal of virology

2022 Volume 96, Issue 18, Page(s) e0123822

Abstract: ... prophylactic and therapeutic effects against lethal challenge with H7N9 virus. Moreover, 4H1E8- and 7H9A6 ... influenza virus and display highly neutralizing activity against H7N9 virus. The epitopes recognized by two MAbs ... antibody-dependent cellular cytotoxicity. Mechanistically, the 4H1E8 and 7H9A6 antibodies inhibit the pH-dependent conformational change ...

Abstract	The H7N9 subtype influenza A viruses pose a serious threat to public health, and there is still a lack of vaccines or drugs for humans against H7N9 influenza viruses. In this study, we screened two monoclonal antibodies (MAbs), 4H1E8 and 7H9A6, that specifically recognize the hemagglutinin (HA) protein of H7N9 influenza virus and display highly neutralizing activity against H7N9 virus. The epitopes recognized by two MAbs are nearly all conserved within all known H7 subtypes. Characteristic identification showed that two MAbs have high avidity for the HA protein but no hemagglutinin inhibition activity or antibody-dependent cellular cytotoxicity. Mechanistically, the 4H1E8 and 7H9A6 antibodies inhibit the pH-dependent conformational change of HA and block the HA-mediated membrane fusion. More importantly, 4H1E8 and 7H9A6 exhibit promising prophylactic and therapeutic effects against lethal challenge with H7N9 virus. Moreover, 4H1E8- and 7H9A6-treated mice displayed inhibition of pulmonary viral replication and reduced lung lesions after viral challenge. Together, these findings indicate that antibodies 4H1E8 and 7H9A6 recognize unique epitopes in the HA protein and possess the neutralizing activity and protective efficacy against the H7N9 influenza A viruses.
MeSH term(s)	Animals ; Antibodies, Monoclonal/pharmacology ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Viral ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Epitopes/metabolism ; Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Humans ; Influenza A Virus, H7N9 Subtype ; Influenza, Human/drug therapy ; Mice ; Mice, Inbred BALB C ; Orthomyxoviridae Infections/drug therapy ; Virus Replication/drug effects
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Viral ; Antiviral Agents ; Epitopes ; Hemagglutinin Glycoproteins, Influenza Virus
Language	English
Publishing date	2022-08-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01238-22
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Article ; Online: Resilience of S309 and AZD7442 monoclonal antibody treatments against infection by SARS-CoV-2 Omicron lineage strains.

Case, James Brett / Mackin, Samantha / Errico, John M / Chong, Zhenlu / Madden, Emily A / Whitener, Bradley / Guarino, Barbara / Schmid, Michael A / Rosenthal, Kim / Ren, Kuishu / Dang, Ha V / Snell, Gyorgy / Jung, Ana / Droit, Lindsay / Handley, Scott A / Halfmann, Peter J / Kawaoka, Yoshihiro / Crowe, James E / Fremont, Daved H /

Virgin, Herbert W / Loo, Yueh-Ming / Esser, Mark T / Purcell, Lisa A / Corti, Davide / Diamond, Michael S

Nature communications

2022 Volume 13, Issue 1, Page(s) 3824

Abstract: ... in prophylactic and therapeutic settings. Correlation analyses between in vitro neutralizing activity and ... the resilience of S309 and AZD7442 mAbs against emerging SARS-CoV-2 variant strains and provide insight ... reductions in viral burden in K18-hACE2 or human FcγR transgenic mice suggest that S309 and AZD7442 have ...

Abstract	Omicron variant strains encode large numbers of changes in the spike protein compared to historical SARS-CoV-2 isolates. Although in vitro studies have suggested that several monoclonal antibody therapies lose neutralizing activity against Omicron variants, the effects in vivo remain largely unknown. Here, we report on the protective efficacy against three SARS-CoV-2 Omicron lineage strains (BA.1, BA.1.1, and BA.2) of two monoclonal antibody therapeutics (S309 [Vir Biotechnology] monotherapy and AZD7442 [AstraZeneca] combination), which correspond to ones used to treat or prevent SARS-CoV-2 infections in humans. Despite losses in neutralization potency in cell culture, S309 or AZD7442 treatments reduced BA.1, BA.1.1, and BA.2 lung infection in susceptible mice that express human ACE2 (K18-hACE2) in prophylactic and therapeutic settings. Correlation analyses between in vitro neutralizing activity and reductions in viral burden in K18-hACE2 or human FcγR transgenic mice suggest that S309 and AZD7442 have different mechanisms of protection against Omicron variants, with S309 utilizing Fc effector function interactions and AZD7442 acting principally by direct neutralization. Our data in mice demonstrate the resilience of S309 and AZD7442 mAbs against emerging SARS-CoV-2 variant strains and provide insight into the relationship between loss of antibody neutralization potency and retained protection in vivo.
MeSH term(s)	Animals ; Antibodies, Monoclonal/pharmacology ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Neutralizing ; Antibodies, Viral/therapeutic use ; Drug Combinations ; Humans ; Membrane Glycoproteins ; Mice ; Neutralization Tests ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; COVID-19 Drug Treatment
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Drug Combinations ; Membrane Glycoproteins ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; cilgavimab and tixagevimab drug combination ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-07-02
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-31615-7
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Article ; Online: Generation, characterization, and protective ability of mouse monoclonal antibodies against the HA of A (H1N1) influenza virus.

Wang, Liyan / Yang, Fan / Xiao, Yixin / Chen, Bin / Liu, Fumin / Cheng, Linfang / Yao, Hangping / Wu, Nanping / Wu, Haibo

Journal of medical virology

2022 Volume 94, Issue 6, Page(s) 2558–2567

Abstract: ... of epidemic strains. Monoclonal antibodies (mAbs) have attracted wide attention as a promising therapeutic ... as a preventive and protective tool, they may not be effective due to antigen drift or an inaccurate prediction ... 2H4, and 2G2, respectively, were derived from mice immunized with the HA protein from A/Michigan/45 ...

Abstract	Influenza virus infections pose a continuous threat to human health. Although vaccines function as a preventive and protective tool, they may not be effective due to antigen drift or an inaccurate prediction of epidemic strains. Monoclonal antibodies (mAbs) have attracted wide attention as a promising therapeutic method for influenza virus infections. In this study, three hemagglutinin (HA)-specific mAbs, named 2A1, 2H4, and 2G2, respectively, were derived from mice immunized with the HA protein from A/Michigan/45/2015(H1N1). The isolated mAbs all displayed hemagglutination inhibition activity and the 2G2 mAb exhibited the strongest neutralization effect. Two amino acid mutations (A198E and G173E), recognized in the process of selection of mAb-resistant mutants, were located in antigenic site Sb and Ca1, respectively. In prophylactic experiments, all three mAbs could achieve 100% protection in mice infected with a lethal dose of A/Michigan/45/2015(H1N1). A dose of 1 mg/kg for 2H4 and 2G2 was sufficient to achieve a full protective effect. Therapeutic experiments showed that all three mAbs could protect mice from death if they received the mAb administration at 6 h postinfection, and 2G2 was still protective after 24 h. Our findings indicate that these three mAbs may have potential prevention and treatment value in an H1N1 epidemic, as well as in the study of antigen epitope recognition.
MeSH term(s)	Animals ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Viral/therapeutic use ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinins ; Humans ; Influenza A Virus, H1N1 Subtype ; Influenza A virus ; Influenza, Human ; Mice ; Mice, Inbred BALB C ; Orthomyxoviridae Infections/drug therapy
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Viral ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins
Language	English
Publishing date	2022-01-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	752392-0
ISSN	1096-9071 ; 0146-6615
ISSN (online)	1096-9071
ISSN	0146-6615
DOI	10.1002/jmv.27584
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Article ; Online: Quantification of clesrovimab, an investigational, half-life extended, anti-respiratory syncytial virus protein F human monoclonal antibody in the nasal epithelial lining fluid of healthy adults.

Phuah, Jia Yao / Maas, Brian M / Tang, Aimin / Zhang, Ying / Caro, Luzelena / Railkar, Radha A / Swanson, Michael D / Cao, Yu / Li, Hankun / Roadcap, Brad / Catchpole, Andrew P / Aliprantis, Antonios O / Vora, Kalpit A

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie

2023 Volume 169, Page(s) 115851

Abstract: ... monoclonal antibody (mAb) against RSV F glycoprotein in clinical trials as a prophylactic agent against RSV infection ... reported in literature to partition ∼1-2 % of serum antibodies into nasal mucosa. Nasal: serum ratios of 1 ... concentrations in the nasal ELF were normalized for sampling dilution using urea concentrations from ELF and ...

Abstract	Background: Clesrovimab (MK-1654) is an investigational, half-life extended human monoclonal antibody (mAb) against RSV F glycoprotein in clinical trials as a prophylactic agent against RSV infection for infants. Methods: This adult study measured clesrovimab concentrations in the serum and nasal epithelial lining fluid (ELF) to establish the partitioning of the antibody after dosing. Clesrovimab concentrations in the nasal ELF were normalized for sampling dilution using urea concentrations from ELF and serum. Furthermore, in vitro RSV neutralization of human nasal ELF following dosing was also measured to examine the activity of clesrovimab in the nasal compartment. Findings: mAbs with YTE mutations are reported in literature to partition ∼1-2 % of serum antibodies into nasal mucosa. Nasal: serum ratios of 1:69-1:30 were observed for clesrovimab in two separate adult human trials after urea normalization, translating to 1.4-3.3 % of serum concentrations. The nasal PK and estimates of peripheral volume of distribution correlated with higher extravascular distribution of clesrovimab. These higher concentration of the antibody in the nasal ELF corroborated with the nasal sample's ability to neutralize RSV ex vivo. An overall trend of decreased viral plaque AUC was also noted with increasing availability of clesrovimab in the nasal ELF from a human RSV challenge study. Interpretation: Along with its extended half-life, the higher penetration of clesrovimab into the nasal epithelial lining fluid and the associated local increase in RSV neutralization activity could offer infants better protection against RSV infection.
MeSH term(s)	Humans ; Adult ; Antibodies, Monoclonal/therapeutic use ; Half-Life ; Antibodies, Viral ; Respiratory Syncytial Virus, Human ; Respiratory Syncytial Virus Infections/drug therapy ; Urea
Chemical Substances	Antibodies, Monoclonal ; MK-1654 ; Antibodies, Viral ; Urea (8W8T17847W)
Language	English
Publishing date	2023-11-14
Publishing country	France
Document type	Journal Article
ZDB-ID	392415-4
ISSN	1950-6007 ; 0753-3322 ; 0300-0893
ISSN (online)	1950-6007
ISSN	0753-3322 ; 0300-0893
DOI	10.1016/j.biopha.2023.115851
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Article ; Online: A conserved immunogenic and vulnerable site on the coronavirus spike protein delineated by cross-reactive monoclonal antibodies.

Wang, Chunyan / van Haperen, Rien / Gutiérrez-Álvarez, Javier / Li, Wentao / Okba, Nisreen M A / Albulescu, Irina / Widjaja, Ivy / van Dieren, Brenda / Fernandez-Delgado, Raul / Sola, Isabel / Hurdiss, Daniel L / Daramola, Olalekan / Grosveld, Frank / van Kuppeveld, Frank J M / Haagmans, Bart L / Enjuanes, Luis / Drabek, Dubravka / Bosch, Berend-Jan

Nature communications

2021 Volume 12, Issue 1, Page(s) 1715

Abstract: ... entry and the focus for development of protective antibodies and vaccines. Structural studies show ... 2, MERS-CoV and the endemic human coronavirus HCoV-OC43. Both cross-reactive antibodies target ... provide protection to mice from lethal MERS-CoV challenge in prophylactic and/or therapeutic models ...

Abstract	The coronavirus spike glycoprotein, located on the virion surface, is the key mediator of cell entry and the focus for development of protective antibodies and vaccines. Structural studies show exposed sites on the spike trimer that might be targeted by antibodies with cross-species specificity. Here we isolated two human monoclonal antibodies from immunized humanized mice that display a remarkable cross-reactivity against distinct spike proteins of betacoronaviruses including SARS-CoV, SARS-CoV-2, MERS-CoV and the endemic human coronavirus HCoV-OC43. Both cross-reactive antibodies target the stem helix in the spike S2 fusion subunit which, in the prefusion conformation of trimeric spike, forms a surface exposed membrane-proximal helical bundle. Both antibodies block MERS-CoV infection in cells and provide protection to mice from lethal MERS-CoV challenge in prophylactic and/or therapeutic models. Our work highlights an immunogenic and vulnerable site on the betacoronavirus spike protein enabling elicitation of antibodies with unusual binding breadth.
MeSH term(s)	Animals ; Antibodies, Monoclonal, Humanized/immunology ; Antibodies, Monoclonal, Humanized/therapeutic use ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/therapeutic use ; Antibodies, Viral/immunology ; Betacoronavirus/classification ; Betacoronavirus/immunology ; Camelus ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Cross Reactions ; Epitopes/chemistry ; Epitopes/genetics ; Epitopes/immunology ; Humans ; Mice ; Protein Conformation ; Protein Subunits ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology
Chemical Substances	Antibodies, Monoclonal, Humanized ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Protein Subunits ; Spike Glycoprotein, Coronavirus
Language	English
Publishing date	2021-03-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-21968-w
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