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Article ; Online: Better influenza vaccines: an industry perspective.

Chen, Juine-Ruey / Liu, Yo-Min / Tseng, Yung-Chieh / Ma, Che

2020 Volume 27, Issue 1, Page(s) 33

Abstract: Vaccination is the most effective measure at preventing influenza virus infections. However, current seasonal influenza vaccines are only protective against closely matched circulating strains. Even with extensive monitoring and annual reformulation our ... ...

Abstract	Vaccination is the most effective measure at preventing influenza virus infections. However, current seasonal influenza vaccines are only protective against closely matched circulating strains. Even with extensive monitoring and annual reformulation our efforts remain one step behind the rapidly evolving virus, often resulting in mismatches and low vaccine effectiveness. Fortunately, many next-generation influenza vaccines are currently in development, utilizing an array of innovative techniques to shorten production time and increase the breadth of protection. This review summarizes the production methods of current vaccines, recent advances that have been made in influenza vaccine research, and highlights potential challenges that are yet to be overcome. Special emphasis is put on the potential role of glycoengineering in influenza vaccine development, and the advantages of removing the glycan shield on influenza surface antigens to increase vaccine immunogenicity. The potential for future development of these novel influenza vaccine candidates is discussed from an industry perspective.
MeSH term(s)	Glycoproteins/chemistry ; Glycoproteins/immunology ; Glycoproteins/pharmacology ; Glycosylation ; Humans ; Immunogenicity, Vaccine ; Influenza Vaccines/analysis ; Influenza Vaccines/chemistry ; Influenza Vaccines/immunology ; Influenza Vaccines/pharmacology ; Protein Engineering ; Viral Proteins/chemistry ; Viral Proteins/immunology ; Viral Proteins/pharmacology
Chemical Substances	Glycoproteins ; Influenza Vaccines ; Viral Proteins
Keywords	covid19
Language	English
Publishing date	2020-02-14
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1193378-1
ISSN	1423-0127 ; 1021-7770
ISSN (online)	1423-0127
ISSN	1021-7770
DOI	10.1186/s12929-020-0626-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Better influenza vaccines

Juine-Ruey Chen / Yo-Min Liu / Yung-Chieh Tseng / Che Ma

Journal of Biomedical Science, Vol 27, Iss 1, Pp 1-

an industry perspective

2020 Volume 11

Abstract: Abstract Vaccination is the most effective measure at preventing influenza virus infections. However, current seasonal influenza vaccines are only protective against closely matched circulating strains. Even with extensive monitoring and annual ... ...

Abstract	Abstract Vaccination is the most effective measure at preventing influenza virus infections. However, current seasonal influenza vaccines are only protective against closely matched circulating strains. Even with extensive monitoring and annual reformulation our efforts remain one step behind the rapidly evolving virus, often resulting in mismatches and low vaccine effectiveness. Fortunately, many next-generation influenza vaccines are currently in development, utilizing an array of innovative techniques to shorten production time and increase the breadth of protection. This review summarizes the production methods of current vaccines, recent advances that have been made in influenza vaccine research, and highlights potential challenges that are yet to be overcome. Special emphasis is put on the potential role of glycoengineering in influenza vaccine development, and the advantages of removing the glycan shield on influenza surface antigens to increase vaccine immunogenicity. The potential for future development of these novel influenza vaccine candidates is discussed from an industry perspective.
Keywords	Influenza virus ; Universal vaccine ; Monoglycosylated HA ; Monoglycosylated split vaccine ; Medicine ; R
Subject code	670
Language	English
Publishing date	2020-02-01T00:00:00Z
Publisher	BMC
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2.

Liu, Yo-Min / Shahed-Al-Mahmud, Md / Chen, Xiaorui / Chen, Ting-Hua / Liao, Kuo-Shiang / Lo, Jennifer M / Wu, Yi-Min / Ho, Meng-Chiao / Wu, Chung-Yi / Wong, Chi-Huey / Jan, Jia-Tsrong / Ma, Che

Cell reports

2020 Volume 32, Issue 6, Page(s) 108016

Abstract: The influenza virus hemagglutinin (HA) and coronavirus spike (S) protein mediate virus entry. HA and S proteins are heavily glycosylated, making them potential targets for carbohydrate binding agents such as lectins. Here, we show that the lectin FRIL, ... ...

Abstract	The influenza virus hemagglutinin (HA) and coronavirus spike (S) protein mediate virus entry. HA and S proteins are heavily glycosylated, making them potential targets for carbohydrate binding agents such as lectins. Here, we show that the lectin FRIL, isolated from hyacinth beans (Lablab purpureus), has anti-influenza and anti-SARS-CoV-2 activity. FRIL can neutralize 11 representative human and avian influenza strains at low nanomolar concentrations, and intranasal administration of FRIL is protective against lethal H1N1 infection in mice. FRIL binds preferentially to complex-type N-glycans and neutralizes viruses that possess complex-type N-glycans on their envelopes. As a homotetramer, FRIL is capable of aggregating influenza particles through multivalent binding and trapping influenza virions in cytoplasmic late endosomes, preventing their nuclear entry. Remarkably, FRIL also effectively neutralizes SARS-CoV-2, preventing viral protein production and cytopathic effect in host cells. These findings suggest a potential application of FRIL for the prevention and/or treatment of influenza and COVID-19.
MeSH term(s)	A549 Cells ; Administration, Intranasal ; Animals ; Antiviral Agents/administration & dosage ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Betacoronavirus/drug effects ; COVID-19 ; Chick Embryo ; Chlorocebus aethiops ; Coronavirus Infections/drug therapy ; Dogs ; Fabaceae/chemistry ; Female ; Humans ; Influenza A Virus, H1N1 Subtype/drug effects ; Madin Darby Canine Kidney Cells ; Mice ; Mice, Inbred BALB C ; Orthomyxoviridae Infections/drug therapy ; Pandemics ; Plant Lectins/administration & dosage ; Plant Lectins/pharmacology ; Plant Lectins/therapeutic use ; Pneumonia, Viral/drug therapy ; Protein Binding ; SARS-CoV-2 ; Vero Cells ; Viral Envelope Proteins/metabolism
Chemical Substances	Antiviral Agents ; Plant Lectins ; Viral Envelope Proteins
Keywords	covid19
Language	English
Publishing date	2020-07-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.108016
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Article ; Online: A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2

Yo-Min Liu / Md. Shahed-Al-Mahmud / Xiaorui Chen / Ting-Hua Chen / Kuo-Shiang Liao / Jennifer M. Lo / Yi-Min Wu / Meng-Chiao Ho / Chung-Yi Wu / Chi-Huey Wong / Jia-Tsrong Jan / Che Ma

Cell Reports, Vol 32, Iss 6, Pp 108016- (2020)

2020

Abstract: Summary: The influenza virus hemagglutinin (HA) and coronavirus spike (S) protein mediate virus entry. HA and S proteins are heavily glycosylated, making them potential targets for carbohydrate binding agents such as lectins. Here, we show that the ... ...

Abstract	Summary: The influenza virus hemagglutinin (HA) and coronavirus spike (S) protein mediate virus entry. HA and S proteins are heavily glycosylated, making them potential targets for carbohydrate binding agents such as lectins. Here, we show that the lectin FRIL, isolated from hyacinth beans (Lablab purpureus), has anti-influenza and anti-SARS-CoV-2 activity. FRIL can neutralize 11 representative human and avian influenza strains at low nanomolar concentrations, and intranasal administration of FRIL is protective against lethal H1N1 infection in mice. FRIL binds preferentially to complex-type N-glycans and neutralizes viruses that possess complex-type N-glycans on their envelopes. As a homotetramer, FRIL is capable of aggregating influenza particles through multivalent binding and trapping influenza virions in cytoplasmic late endosomes, preventing their nuclear entry. Remarkably, FRIL also effectively neutralizes SARS-CoV-2, preventing viral protein production and cytopathic effect in host cells. These findings suggest a potential application of FRIL for the prevention and/or treatment of influenza and COVID-19.
Keywords	lectin ; influenza ; coronavirus ; SARS-CoV-2 ; antiviral ; N-glycosylation ; Biology (General) ; QH301-705.5 ; covid19
Subject code	570
Language	English
Publishing date	2020-08-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Vaccination with SARS-CoV-2 spike protein lacking glycan shields elicits enhanced protective responses in animal models.

Huang, Han-Yi / Liao, Hsin-Yu / Chen, Xiaorui / Wang, Szu-Wen / Cheng, Cheng-Wei / Shahed-Al-Mahmud, Md / Liu, Yo-Min / Mohapatra, Arpita / Chen, Ting-Hua / Lo, Jennifer M / Wu, Yi-Min / Ma, Hsiu-Hua / Chang, Yi-Hsuan / Tsai, Ho-Yang / Chou, Yu-Chi / Hsueh, Yi-Ping / Tsai, Ching-Yen / Huang, Pau-Yi / Chang, Sui-Yuan /

Chao, Tai-Ling / Kao, Han-Chieh / Tsai, Ya-Min / Chen, Yen-Hui / Wu, Chung-Yi / Jan, Jia-Tsrong / Cheng, Ting-Jen Rachel / Lin, Kuo-I / Ma, Che / Wong, Chi-Huey

Science translational medicine

2022 Volume 14, Issue 639, Page(s) eabm0899

Abstract: A major challenge to end the pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is to develop a broadly protective vaccine that elicits long-term immunity. As the key immunogen, the viral surface spike (S) protein is ... ...

Abstract	A major challenge to end the pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is to develop a broadly protective vaccine that elicits long-term immunity. As the key immunogen, the viral surface spike (S) protein is frequently mutated, and conserved epitopes are shielded by glycans. Here, we revealed that S protein glycosylation has site-differential effects on viral infectivity. We found that S protein generated by lung epithelial cells has glycoforms associated with increased infectivity. Compared to the fully glycosylated S protein, immunization of S protein with N-glycans trimmed to the mono-GlcNAc-decorated state (S
MeSH term(s)	Animals ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19/prevention & control ; COVID-19 Vaccines/immunology ; COVID-19 Vaccines/metabolism ; Humans ; Mice ; Models, Animal ; Polysaccharides ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Vaccination
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Polysaccharides ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-04-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2518854-9
ISSN	1946-6242 ; 1946-6234
ISSN (online)	1946-6242
ISSN	1946-6234
DOI	10.1126/scitranslmed.abm0899
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 6941: Show issues

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Article ; Online: A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2

Liu, Yo-Min / Shahed-Al-Mahmud, Md. / Chen, Xiaorui / Chen, Ting-Hua / Liao, Kuo-Shiang / Lo, Jennifer M. / Wu, Yi-Min / Ho, Meng-Chiao / Wu, Chung-Yi / Wong, Chi-Huey / Jan, Jia-Tsrong / Ma, Che

Cell Reports

2020 Volume 32, Issue 6, Page(s) 108016

Keywords	General Biochemistry, Genetics and Molecular Biology ; covid19
Language	English
Publisher	Elsevier BV
Publishing country	us
Document type	Article ; Online
ZDB-ID	2649101-1
ISSN	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.108016
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Debulking different Corona (SARS-COV-2 delta, omicron, OC43) and influenza (H1N1, H3N2) virus strains by plant viral trap proteins in chewing gums to decrease infection and transmission

Daniell, Henry / Nair, Smruti K. / Guan, Hancheng / Guo, Yuwei / Kulchar, Rachel J. / Torres, Marcelo D.T. / Shahed-Al-Mahmud, Md / Wakade, Geetanjali / Liu, Yo-Min / Marques, Andrew / Graham-Wooten, Jevon / Zhou, Wan / Wang, Ping / Molugu, Sudheer K. / de Araujo, William R. / de la Fuente-Nunez, Cesar / Ma, Che / Short, William R. / Tebas, Pablo /

Margulies, Kenneth B. / Bushman, Fredrick D. / Mante, Francis K. / Ricciardi, Robert / Collman, Ronald G. / Wolff, Mark S.

Biomaterials. 2022 July 06,

2022

Abstract: ... studies revealed that CTB-ACE2 release was time/dose-dependent and release was linear up to 20 min chewing ...

Abstract	Because oral transmission of SARS-CoV-2 is 3–5 orders of magnitude higher than nasal transmission, we investigated debulking of oral viruses using viral trap proteins (CTB-ACE2, FRIL) expressed in plant cells, delivered through the chewing gum. In omicron nasopharyngeal (NP) samples, the microbubble count (based on N-antigen) was significantly reduced by 20 μg of FRIL (p < 0.0001) and 0.925 μg of CTB-ACE2 (p = 0.0001). Among 20 delta or omicron NP samples, 17 had virus load reduced below the detection level of spike protein in the RAPID assay, after incubation with the CTB-ACE2 gum powder. A dose-dependent 50% plaque reduction with 50–100 ng FRIL or 600–800 μg FRIL gum against Influenza strains H1N1, H₃N₂, and Coronavirus HCoV-OC43 was observed with both purified FRIL, lablab bean powder or gum. In electron micrographs, large/densely packed clumps of overlapping influenza particles and FRIL protein were observed. Chewing simulator studies revealed that CTB-ACE2 release was time/dose-dependent and release was linear up to 20 min chewing. Phase I/II placebo-controlled, double-blinded clinical trial (IND 154897) is in progress to evaluate viral load in saliva before or after chewing CTB-ACE2/placebo gum. Collectively, this study advances the concept of chewing gum to deliver proteins to debulk oral viruses and decrease infection/transmission.
Keywords	Betacoronavirus 1 ; Lablab purpureus ; Severe acute respiratory syndrome coronavirus 2 ; biocompatible materials ; clinical trials ; dose response ; influenza ; microbubbles ; nose ; saliva ; viral load ; viruses
Language	English
Dates of publication	2022-0706
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	603079-8
ISSN	0142-9612
ISSN	0142-9612
DOI	10.1016/j.biomaterials.2022.121671
Database	NAL-Catalogue (AGRICOLA)

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Zs.B 2371: Show issues

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Article ; Online: Debulking different Corona (SARS-CoV-2 delta, omicron, OC43) and Influenza (H1N1, H3N2) virus strains by plant viral trap proteins in chewing gums to decrease infection and transmission.

Daniell, Henry / Nair, Smruti K / Guan, Hancheng / Guo, Yuwei / Kulchar, Rachel J / Torres, Marcelo D T / Shahed-Al-Mahmud, Md / Wakade, Geetanjali / Liu, Yo-Min / Marques, Andrew D / Graham-Wooten, Jevon / Zhou, Wan / Wang, Ping / Molugu, Sudheer K / de Araujo, William R / de la Fuente-Nunez, Cesar / Ma, Che / Short, William R / Tebas, Pablo /

Margulies, Kenneth B / Bushman, Frederic D / Mante, Francis K / Ricciardi, Robert P / Collman, Ronald G / Wolff, Mark S

Biomaterials

2022 Volume 288, Page(s) 121671

Abstract: ... studies revealed that CTB-ACE2 release was time/dose-dependent and release was linear up to 20 min chewing ...

Abstract	Because oral transmission of SARS-CoV-2 is 3-5 orders of magnitude higher than nasal transmission, we investigated debulking of oral viruses using viral trap proteins (CTB-ACE2, FRIL) expressed in plant cells, delivered through the chewing gum. In omicron nasopharyngeal (NP) samples, the microbubble count (based on N-antigen) was significantly reduced by 20 μg of FRIL (p < 0.0001) and 0.925 μg of CTB-ACE2 (p = 0.0001). Among 20 delta or omicron NP samples, 17 had virus load reduced below the detection level of spike protein in the RAPID assay, after incubation with the CTB-ACE2 gum powder. A dose-dependent 50% plaque reduction with 50-100 ng FRIL or 600-800 μg FRIL gum against Influenza strains H1N1, H3N2, and Coronavirus HCoV-OC43 was observed with both purified FRIL, lablab bean powder or gum. In electron micrographs, large/densely packed clumps of overlapping influenza particles and FRIL protein were observed. Chewing simulator studies revealed that CTB-ACE2 release was time/dose-dependent and release was linear up to 20 min chewing. Phase I/II placebo-controlled, double-blinded clinical trial (IND 154897) is in progress to evaluate viral load in saliva before or after chewing CTB-ACE2/placebo gum. Collectively, this study advances the concept of chewing gum to deliver proteins to debulk oral viruses and decrease infection/transmission.
MeSH term(s)	Angiotensin-Converting Enzyme 2 ; COVID-19 ; Chewing Gum ; Cytoreduction Surgical Procedures ; Humans ; Influenza A Virus, H1N1 Subtype ; Influenza A Virus, H3N2 Subtype ; Influenza, Human ; Plant Proteins ; Powders ; SARS-CoV-2 ; Viral Proteins
Chemical Substances	Chewing Gum ; Plant Proteins ; Powders ; Viral Proteins ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2022-07-18
Publishing country	Netherlands
Document type	Clinical Trial ; 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	603079-8
ISSN	1878-5905 ; 0142-9612
ISSN (online)	1878-5905
ISSN	0142-9612
DOI	10.1016/j.biomaterials.2022.121671
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Article: A Carbohydrate-Binding Protein from the Edible Lablab Beans Effectively Blocks the Infections of Influenza Viruses and SARS-CoV-2

Liu, Yo-Min / Shahed-Al-Mahmud, Md / Chen, Xiaorui / Chen, Ting-Hua / Liao, Kuo-Shiang / Lo, Jennifer M / Wu, Yi-Min / Ho, Meng-Chiao / Wu, Chung-Yi / Wong, Chi-Huey / Jan, Jia-Tsrong / Ma, Che

Cell Rep

Abstract	The influenza virus hemagglutinin (HA) and coronavirus spike (S) protein mediate virus entry. HA and S proteins are heavily glycosylated, making them potential targets for carbohydrate binding agents such as lectins. Here, we show that the lectin FRIL, isolated from hyacinth beans (Lablab purpureus), has anti-influenza and anti-SARS-CoV-2 activity. FRIL can neutralize 11 representative human and avian influenza strains at low nanomolar concentrations, and intranasal administration of FRIL is protective against lethal H1N1 infection in mice. FRIL binds preferentially to complex-type N-glycans and neutralizes viruses that possess complex-type N-glycans on their envelopes. As a homotetramer, FRIL is capable of aggregating influenza particles through multivalent binding and trapping influenza virions in cytoplasmic late endosomes, preventing their nuclear entry. Remarkably, FRIL also effectively neutralizes SARS-CoV-2, preventing viral protein production and cytopathic effect in host cells. These findings suggest a potential application of FRIL for the prevention and/or treatment of influenza and COVID-19.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #670926
Database	COVID19

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Article ; Online: Structure-function analysis of neutralizing antibodies to H7N9 influenza from naturally infected humans.

Nature microbiology

2018 Volume 4, Issue 2, Page(s) 306–315

Abstract: Little is known about the specificities and neutralization breadth of the H7-reactive antibody repertoire induced by natural H7N9 infection in humans. We have isolated and characterized 73 H7-reactive monoclonal antibodies from peripheral B cells from ... ...

Abstract	Little is known about the specificities and neutralization breadth of the H7-reactive antibody repertoire induced by natural H7N9 infection in humans. We have isolated and characterized 73 H7-reactive monoclonal antibodies from peripheral B cells from four donors infected in 2013 and 2014. Of these, 45 antibodies were H7-specific, and 17 of these neutralized the virus, albeit with few somatic mutations in their variable domain sequences. An additional set of 28 antibodies, isolated from younger donors born after 1968, cross-reacted between H7 and H3 haemagglutinins in binding assays, and had accumulated significantly more somatic mutations, but were predominantly non-neutralizing in vitro. Crystal structures of three neutralizing and protective antibodies in complex with the H7 haemagglutinin revealed that they recognize overlapping residues surrounding the receptor-binding site of haemagglutinin. One of the antibodies, L4A-14, bound into the sialic acid binding site and made contacts with haemagglutinin residues that were conserved in the great majority of 2016-2017 H7N9 isolates. However, only 3 of the 17 neutralizing antibodies retained activity for the Yangtze River Delta lineage viruses isolated in 2016-2017 that have undergone antigenic change, which emphasizes the need for updated H7N9 vaccines.
MeSH term(s)	Animals ; Antibodies, Monoclonal/administration & dosage ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibodies, Neutralizing/administration & dosage ; Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/metabolism ; Antibodies, Viral/administration & dosage ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Binding Sites ; Cross Reactions/immunology ; Disease Models, Animal ; Epitopes ; Female ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Humans ; Influenza A Virus, H7N9 Subtype/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Mice, Inbred BALB C ; Protein Conformation
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Hemagglutinin Glycoproteins, Influenza Virus ; hemagglutinin, avian influenza A virus
Language	English
Publishing date	2018-11-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2058-5276
ISSN (online)	2058-5276
DOI	10.1038/s41564-018-0303-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

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