Modular synthesis of N-glycans and arrays for the hetero-ligand binding analysis of HIV antibodies

A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120—a glycoprotein found on the surface of the virus envelope—thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies w...

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Published inNature chemistry Vol. 8; no. 4; pp. 338 - 346
Main Authors Shivatare, Sachin S., Chang, Shih-Huang, Tsai, Tsung-I, Tseng, Susan Yu, Shivatare, Vidya S., Lin, Yih-Shyan, Cheng, Yang-Yu, Ren, Chien-Tai, Lee, Chang-Chun David, Pawar, Sujeet, Tsai, Charng-Sheng, Shih, Hao-Wei, Zeng, Yi-Fang, Liang, Chi-Hui, Kwong, Peter D., Burton, Dennis R., Wu, Chung-Yi, Wong, Chi-Huey
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.04.2016
Springer Nature
Nature Publishing Group
Subjects
639/638/403/931
639/638/92/72
AIDS Vaccines - immunology
Aluminum
Aluminum oxide
Analytical Chemistry
Antibodies
Antibodies, Neutralizing - immunology
Arrays
Binding
Biochemistry
Carbohydrates
Cell surface
Chemistry
Chemistry, Multidisciplinary
Chemistry/Food Science
Glycan
Glycoprotein gp120
Glycoproteins
Glycosylation
HIV
HIV Antibodies - immunology
HIV Envelope Protein gp120 - immunology
HIV-1 - immunology
Human immunodeficiency virus
Human immunodeficiency virus 1
Humans
Inorganic Chemistry
Ligands
Lymphocytes
Lymphocytes T
Mannose
N-glycans
Neutralizing
Organic Chemistry
Pattern recognition
Physical Chemistry
Physical Sciences
Polysaccharides
Polysaccharides - chemical synthesis
Polysaccharides - chemistry
Polysaccharides - immunology
Science & Technology
Synthesis
Vaccines
POTENT
GALACTOSIDE ALPHA-2,3-SIALYLTRANSFERASE
RECOGNITION
ENVELOPE GLYCOPROTEINS
GLYCOSYLATION PROFILES
OLIGOSACCHARIDE MICROARRAYS
BROAD
GP120
EFFICIENT CHEMOENZYMATIC SYNTHESIS
VACCINES
Online AccessGet full text
ISSN1755-4330
1755-4349
1755-4349
DOI10.1038/nchem.2463

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Abstract A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120—a glycoprotein found on the surface of the virus envelope—thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium-oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N -glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans. The glycoprotein gp120 is found on the surface of the HIV viron; it is essential for virus entry into cells. Now, an efficient modular synthesis of N -glycans and the preparation of a mixed-glycan array on aluminium-oxide-coated glass slide is described. This is a vital step in understanding the complex compositions of gp120 and thus important for the development of new HIV therapies.
AbstractList A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120—a glycoprotein found on the surface of the virus envelope—thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium-oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N-glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans.The glycoprotein gp120 is found on the surface of the HIV viron; it is essential for virus entry into cells. Now, an efficient modular synthesis of N-glycans and the preparation of a mixed-glycan array on aluminium-oxide-coated glass slide is described. This is a vital step in understanding the complex compositions of gp120 and thus important for the development of new HIV therapies.
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120--a glycoprotein found on the surface of the virus envelope--thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium-oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N-glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans.
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120--a glycoprotein found on the surface of the virus envelope--thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium-oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N-glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans.A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120--a glycoprotein found on the surface of the virus envelope--thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium-oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N-glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans.
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120—a glycoprotein found on the surface of the virus envelope—thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium-oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N -glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans. The glycoprotein gp120 is found on the surface of the HIV viron; it is essential for virus entry into cells. Now, an efficient modular synthesis of N -glycans and the preparation of a mixed-glycan array on aluminium-oxide-coated glass slide is described. This is a vital step in understanding the complex compositions of gp120 and thus important for the development of new HIV therapies.
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120, thus renewing hope of developing carbohydrate-based HIV vaccines. However, the version of gp120 used in previous studies was not from human T cells and so the glycosylation pattern could be somewhat different to that found in the native system. Moreover, some antibodies recognized two different glycans simultaneously and this cannot be detected with the commonly used glycan microarrays on glass slides. Here, we have developed a glycan microarray on an aluminium oxide-coated glass slide containing a diverse set of glycans, including homo- and mixed N -glycans (high-mannose, hybrid and complex types) that were prepared by modular chemo-enzymatic methods to detect the presence of hetero-glycan binding behaviours. This new approach allows rapid screening and identification of optimal glycans recognized by neutralizing antibodies, and could speed up the development of HIV-1 vaccines targeting cell surface glycans.
Author Shivatare, Sachin S.
Burton, Dennis R.
Chang, Shih-Huang
Tseng, Susan Yu
Lee, Chang-Chun David
Pawar, Sujeet
Zeng, Yi-Fang
Wu, Chung-Yi
Kwong, Peter D.
Ren, Chien-Tai
Lin, Yih-Shyan
Tsai, Charng-Sheng
Shivatare, Vidya S.
Shih, Hao-Wei
Liang, Chi-Hui
Tsai, Tsung-I
Wong, Chi-Huey
Cheng, Yang-Yu
AuthorAffiliation 1 Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 115, Taiwan
2 Chemical Biology and Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica, Taiwan
5 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
3 Institute of Biochemical Sciences, National Taiwan University, 1 Roosevelt Road, Section 4, Taipei, 106, Taiwan
4 The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
6 CHO Pharma Inc., Park Street, Nangang District, Taipei-11503, Taiwan
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– name: 3 Institute of Biochemical Sciences, National Taiwan University, 1 Roosevelt Road, Section 4, Taipei, 106, Taiwan
– name: 6 CHO Pharma Inc., Park Street, Nangang District, Taipei-11503, Taiwan
– name: 1 Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Taipei 115, Taiwan
– name: 5 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
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  surname: Shivatare
  fullname: Shivatare, Sachin S.
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Chemical Biology and Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica, Institute of Biochemical Sciences, National Taiwan University, 1 Roosevelt Road, Section 4, CHO Pharma Inc., Park Street, Nangang District
– sequence: 2
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  surname: Chang
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  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Institute of Biochemical Sciences, National Taiwan University, 1 Roosevelt Road, Section 4
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  orcidid: 0000-0002-8355-6017
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  organization: The Scripps Research Institute, 10550 North Torrey Pines Road
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  orcidid: 0000-0002-5710-6960
  surname: Tseng
  fullname: Tseng, Susan Yu
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang
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  surname: Shivatare
  fullname: Shivatare, Vidya S.
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang
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  givenname: Yih-Shyan
  surname: Lin
  fullname: Lin, Yih-Shyan
  organization: CHO Pharma Inc., Park Street, Nangang District
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  givenname: Yang-Yu
  surname: Cheng
  fullname: Cheng, Yang-Yu
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang
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  givenname: Chien-Tai
  surname: Ren
  fullname: Ren, Chien-Tai
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang
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  givenname: Chang-Chun David
  surname: Lee
  fullname: Lee, Chang-Chun David
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang
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  givenname: Sujeet
  surname: Pawar
  fullname: Pawar, Sujeet
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, Chemical Biology and Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica
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  fullname: Tsai, Charng-Sheng
  organization: CHO Pharma Inc., Park Street, Nangang District
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  givenname: Hao-Wei
  surname: Shih
  fullname: Shih, Hao-Wei
  organization: CHO Pharma Inc., Park Street, Nangang District
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  givenname: Yi-Fang
  surname: Zeng
  fullname: Zeng, Yi-Fang
  organization: CHO Pharma Inc., Park Street, Nangang District
– sequence: 14
  givenname: Chi-Hui
  surname: Liang
  fullname: Liang, Chi-Hui
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, The Scripps Research Institute, 10550 North Torrey Pines Road
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  givenname: Peter D.
  surname: Kwong
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  organization: Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health
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  givenname: Dennis R.
  surname: Burton
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  organization: The Scripps Research Institute, 10550 North Torrey Pines Road
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  givenname: Chung-Yi
  surname: Wu
  fullname: Wu, Chung-Yi
  email: cyiwu@gate.sinica.edu.tw
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang
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  givenname: Chi-Huey
  surname: Wong
  fullname: Wong, Chi-Huey
  email: chwong@gate.sinica.edu.tw
  organization: Genomics Research Center, Academia Sinica, 128 Academia Road, Section 2, Nankang, The Scripps Research Institute, 10550 North Torrey Pines Road
BackLink https://www.ncbi.nlm.nih.gov/pubmed/27001729$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright Springer Nature Limited 2016
Copyright Nature Publishing Group Apr 2016
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– notice: Copyright Nature Publishing Group Apr 2016
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Issue 4
Keywords POTENT
GALACTOSIDE ALPHA-2,3-SIALYLTRANSFERASE
RECOGNITION
ENVELOPE GLYCOPROTEINS
GLYCOSYLATION PROFILES
OLIGOSACCHARIDE MICROARRAYS
BROAD
GP120
EFFICIENT CHEMOENZYMATIC SYNTHESIS
VACCINES
Language English
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Snippet A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120—a glycoprotein found on the surface of...
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120-a glycoprotein found on the surface of...
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120--a glycoprotein found on the surface of...
A new class of broadly neutralizing antibodies (bNAbs) from HIV donors has been reported to target the glycans on gp120, thus renewing hope of developing...
Source Web of Science
SourceID pubmedcentral
proquest
pubmed
webofscience
crossref
springer
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 338
SubjectTerms 639/638/403/931
639/638/92/72
AIDS Vaccines - immunology
Aluminum
Aluminum oxide
Analytical Chemistry
Antibodies
Antibodies, Neutralizing - immunology
Arrays
Binding
Biochemistry
Carbohydrates
Cell surface
Chemistry
Chemistry, Multidisciplinary
Chemistry/Food Science
Glycan
Glycoprotein gp120
Glycoproteins
Glycosylation
HIV
HIV Antibodies - immunology
HIV Envelope Protein gp120 - immunology
HIV-1 - immunology
Human immunodeficiency virus
Human immunodeficiency virus 1
Humans
Inorganic Chemistry
Ligands
Lymphocytes
Lymphocytes T
Mannose
N-glycans
Neutralizing
Organic Chemistry
Pattern recognition
Physical Chemistry
Physical Sciences
Polysaccharides
Polysaccharides - chemical synthesis
Polysaccharides - chemistry
Polysaccharides - immunology
Science & Technology
Synthesis
Vaccines
Title Modular synthesis of N-glycans and arrays for the hetero-ligand binding analysis of HIV antibodies
URI https://link.springer.com/article/10.1038/nchem.2463
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https://www.ncbi.nlm.nih.gov/pubmed/27001729
https://www.proquest.com/docview/1780953062
https://www.proquest.com/docview/3143076007
https://www.proquest.com/docview/1775381242
https://www.proquest.com/docview/1794503348
https://pubmed.ncbi.nlm.nih.gov/PMC4806563
Volume 8
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