Surface-Matrix Screening Identifies Semi-specific Interactions that Improve Potency of a Near Pan-reactive HIV-1-Neutralizing Antibody

Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the la...

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Published inCell reports (Cambridge) Vol. 22; no. 7; pp. 1798 - 1809
Main Authors Kwon, Young D., Chuang, Gwo-Yu, Zhang, Baoshan, Bailer, Robert T., Doria-Rose, Nicole A., Gindin, Tatyana S., Lin, Bob, Louder, Mark K., McKee, Krisha, O’Dell, Sijy, Pegu, Amarendra, Schmidt, Stephen D., Asokan, Mangaiarkarasi, Chen, Xuejun, Choe, Misook, Georgiev, Ivelin S., Jin, Vivian, Pancera, Marie, Rawi, Reda, Wang, Keyun, Chaudhuri, Rajoshi, Kueltzo, Lisa A., Manceva, Slobodanka D., Todd, John-Paul, Scorpio, Diana G., Kim, Mikyung, Reinherz, Ellis L., Wagh, Kshitij, Korber, Bette M., Connors, Mark, Shapiro, Lawrence, Mascola, John R., Kwong, Peter D.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 13.02.2018
Elsevier
Subjects
10E8
Antibodies, Neutralizing - immunology
antibody improvement
BASIC BIOLOGICAL SCIENCES
broadly neutralizing antibody
Cell Membrane - metabolism
Half-Life
HIV Antibodies - immunology
HIV Envelope Protein gp41 - metabolism
HIV-1
HIV-1 - immunology
Humans
membrane-proximal external region
MPER
Neutralization Tests
Polysaccharides - metabolism
Protein Binding
surface-matrix screening
HIV-1
broadly neutralizing antibody
membrane-proximal external region
antibody improvement
MPER
10E8
surface-matrix screening
Online AccessGet full text
ISSN2211-1247
2211-1247
DOI10.1016/j.celrep.2018.01.023

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Abstract Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ∼10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth. [Display omitted] •Development of a surface-matrix screening approach to improve antibody function•Identified hydrophobic mutations that improved 10E8 interaction with HIV-1 membrane•Identified positively charged mutations that improved interactions with HIV-1 glycan•Optimizing semi-specific interactions can improve potency while maintaining breadth Antibodies could impact the treatment and prevention of HIV-1 if they were sufficiently potent to allow cost-effective delivery. Kwon et al. used a surface-matrix screening approach to improve the potency of antibody 10E8 by ∼10-fold. The improved antibody, 10E8v4-5R+100cF, has among the best breadth and potency of current HIV-1-neutralizing antibodies.
AbstractList Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ~10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth. Antibodies could impact the treatment and prevention of HIV-1 if they were sufficiently potent to allow cost-effective delivery. Kwon et al. used a surface-matrix screening approach to improve the potency of antibody 10E8 by ~10-fold. The improved antibody, 10E8v4-5R+100cF, has among the best breadth and potency of current HIV-1-neutralizing antibodies.
Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ∼10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth.
Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ∼10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth.Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ∼10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth.
Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ~10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth.
Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an antibody capable of near pan-HIV-1 neutralization, we engineered 10E8-surface mutants and screened for improved neutralization. Variants with the largest functional enhancements involved the addition of hydrophobic or positively charged residues, which were positioned to interact with viral membrane lipids or viral glycan-sialic acids, respectively. In both cases, the site of improvement was spatially separated from the region of antibody mediating molecular contact with the protein component of the antigen, thereby improving peripheral semi-specific interactions while maintaining unmodified dominant contacts responsible for broad recognition. The optimized 10E8 antibody, with mutations to phenylalanine and arginine, retained the extraordinary breadth of 10E8 but with ∼10-fold increased potency. We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth. [Display omitted] •Development of a surface-matrix screening approach to improve antibody function•Identified hydrophobic mutations that improved 10E8 interaction with HIV-1 membrane•Identified positively charged mutations that improved interactions with HIV-1 glycan•Optimizing semi-specific interactions can improve potency while maintaining breadth Antibodies could impact the treatment and prevention of HIV-1 if they were sufficiently potent to allow cost-effective delivery. Kwon et al. used a surface-matrix screening approach to improve the potency of antibody 10E8 by ∼10-fold. The improved antibody, 10E8v4-5R+100cF, has among the best breadth and potency of current HIV-1-neutralizing antibodies.
Author Zhang, Baoshan
Chaudhuri, Rajoshi
Connors, Mark
Manceva, Slobodanka D.
Louder, Mark K.
Jin, Vivian
Kim, Mikyung
Kwong, Peter D.
Pancera, Marie
Asokan, Mangaiarkarasi
McKee, Krisha
Korber, Bette M.
Kueltzo, Lisa A.
Todd, John-Paul
Schmidt, Stephen D.
Georgiev, Ivelin S.
Choe, Misook
Gindin, Tatyana S.
Reinherz, Ellis L.
O’Dell, Sijy
Scorpio, Diana G.
Lin, Bob
Pegu, Amarendra
Rawi, Reda
Kwon, Young D.
Wang, Keyun
Mascola, John R.
Chuang, Gwo-Yu
Doria-Rose, Nicole A.
Chen, Xuejun
Wagh, Kshitij
Bailer, Robert T.
Shapiro, Lawrence
AuthorAffiliation 1 Vaccine Research Center, National Institute of Allergy and Infectious Diseases (NIAID), NIH, Bethesda, MD 20892, USA
3 Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02215, USA
6 Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA
5 Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA
2 Department of Pathology and Cell Biology, Columbia University, New York, NY 10032, USA
4 Los Alamos National Laboratory, Los Alamos, NM 87545, USA
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/29444432$$D View this record in MEDLINE/PubMed
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Issue 7
Keywords HIV-1
broadly neutralizing antibody
membrane-proximal external region
antibody improvement
MPER
10E8
surface-matrix screening
Language English
License This is an open access article under the CC BY-NC-ND license.
Published by Elsevier Inc.
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
W-31-109-Eng-38
National Institutes of Health (NIH)
Lead Contact
These authors contributed equally
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Snippet Highly effective HIV-1-neutralizing antibodies could have utility in the prevention or treatment of HIV-1 infection. To improve the potency of 10E8, an...
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StartPage 1798
SubjectTerms 10E8
Antibodies, Neutralizing - immunology
antibody improvement
BASIC BIOLOGICAL SCIENCES
broadly neutralizing antibody
Cell Membrane - metabolism
Half-Life
HIV Antibodies - immunology
HIV Envelope Protein gp41 - metabolism
HIV-1
HIV-1 - immunology
Humans
membrane-proximal external region
MPER
Neutralization Tests
Polysaccharides - metabolism
Protein Binding
surface-matrix screening
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Title Surface-Matrix Screening Identifies Semi-specific Interactions that Improve Potency of a Near Pan-reactive HIV-1-Neutralizing Antibody
URI https://dx.doi.org/10.1016/j.celrep.2018.01.023
https://www.ncbi.nlm.nih.gov/pubmed/29444432
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https://pubmed.ncbi.nlm.nih.gov/PMC5889116
https://doaj.org/article/20803a2ba97341ed985e9c54c91c448e
Volume 22
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