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Article ; Online: Antibody Display Technology (ADbody) to Present Challenging and Unstable Target Proteins on Antibodies.

Hsieh, Fu-Lien / Chang, Tao-Hsin

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2681, Page(s) 373–382

Abstract: ... method of a novel display technology termed antibody display technology (ADbody) (Hsieh and Chang ... Hsieh and Higgins, eLife 6:e27311, 2017). The principle of ADbody is to insert proteins of interest (POI ...

Abstract	Antibodies are the major components of adaptive immunity for the recognition of diverse antigens. Six complementarity-determining regions (CDRs) from each heavy chain and light chain present the antigen-binding site, which determines the antigen-binding specificity. Here, we describe the detailed method of a novel display technology termed antibody display technology (ADbody) (Hsieh and Chang, bioRxiv, 2021), based on the novel structure of human antibodies from malaria-endemic regions of Africa (Hsieh and Higgins, eLife 6:e27311, 2017). The principle of ADbody is to insert proteins of interest (POI) into the heavy-chain CDR3 while still retaining the biological function of POI on the antibody. In this chapter, we described how to use the ADbody method to display challenging and unstable POI on the antibody in mammalian cells. Collectively, this method is designed to provide an alternative outside the current display systems and to generate novel synthetic antibodies.
MeSH term(s)	Animals ; Humans ; Immunoglobulin Heavy Chains ; Antibodies/chemistry ; Complementarity Determining Regions ; Antigens ; Technology ; Mammals
Chemical Substances	Immunoglobulin Heavy Chains ; Antibodies ; Complementarity Determining Regions ; Antigens
Language	English
Publishing date	2023-07-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3279-6_21
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Structure of WNT inhibitor adenomatosis polyposis coli down-regulated 1 (APCDD1), a cell-surface lipid-binding protein.

Hsieh, Fu-Lien / Chang, Tao-Hsin / Gabelli, Sandra B / Nathans, Jeremy

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 20, Page(s) e2217096120

Abstract: Diverse extracellular proteins negatively regulate WNT signaling. One such regulator is adenomatosis polyposis coli down-regulated 1 (APCDD1), a conserved single-span transmembrane protein. In response to WNT signaling in a variety of tissues, ...

Abstract	Diverse extracellular proteins negatively regulate WNT signaling. One such regulator is adenomatosis polyposis coli down-regulated 1 (APCDD1), a conserved single-span transmembrane protein. In response to WNT signaling in a variety of tissues,
MeSH term(s)	Humans ; Membrane Proteins/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Wnt Signaling Pathway ; Adenomatous Polyposis Coli ; Lipids ; beta Catenin/genetics ; beta Catenin/metabolism
Chemical Substances	Membrane Proteins ; Intracellular Signaling Peptides and Proteins ; Lipids ; beta Catenin ; APCDD1 protein, human
Language	English
Publishing date	2023-05-08
Publishing country	United States
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	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2217096120
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Article ; Online: Antibody Display of cell surface receptor Tetraspanin12 and SARS-CoV-2 spike protein

Hsieh, Fu-Lien / Chang, Tao-Hsin

bioRxiv

Abstract: In previous work, Hsieh and Higgins presented a novel structure of antibodies identified ...

Abstract	In previous work, Hsieh and Higgins presented a novel structure of antibodies identified from malaria-exposed individuals, in which the extracellular immunoglobulin (Ig)-like domain of leukocyte-associated immunoglobulin-like receptor 1 (LAIR1) is presented on the third complementarity determining regions (CDR3) of the Ig heavy chain. Here we develop an Antibody Display technology based on this LAIR1-containing antibody, by grafting proteins of interest (POI) onto the heavy chain CDR3 while retaining the biological properties of the POI. As a proof of principle, we displayed the second extracellular domain of Tetraspanin12 (Tspan12EC2) and the receptor-binding domain (RBD) of SARS-CoV-2 spike protein on the heavy chain CDR3. Our data revealed that Antibody Display Tspan12EC2 bound to Norrie Disease Protein (Norrin) and Antibody Display SARS-CoV-2 RBD bound to angiotensin-converting enzyme 2 (ACE2) and neutralizing nanobodies. Collectively, Antibody Display technology offers the general strategy of designing novel antibodies by grafting POI onto the CDR3.
Keywords	covid19
Language	English
Publishing date	2021-05-30
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.05.29.446300
Database	COVID19

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Article ; Online: Structural insights into plasmalemma vesicle-associated protein (PLVAP): Implications for vascular endothelial diaphragms and fenestrae.

Chang, Tao-Hsin / Hsieh, Fu-Lien / Gu, Xiaowu / Smallwood, Philip M / Kavran, Jennifer M / Gabelli, Sandra B / Nathans, Jeremy

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 14, Page(s) e2221103120

Abstract: In many organs, small openings across capillary endothelial cells (ECs) allow the diffusion of low-molecular weight compounds and small proteins between the blood and tissue spaces. These openings contain a diaphragm composed of radially arranged fibers, ...

Abstract	In many organs, small openings across capillary endothelial cells (ECs) allow the diffusion of low-molecular weight compounds and small proteins between the blood and tissue spaces. These openings contain a diaphragm composed of radially arranged fibers, and current evidence suggests that a single-span type II transmembrane protein, plasmalemma vesicle-associated protein-1 (PLVAP), constitutes these fibers. Here, we present the three-dimensional crystal structure of an 89-amino acid segment of the PLVAP extracellular domain (ECD) and show that it adopts a parallel dimeric alpha-helical coiled-coil configuration with five interchain disulfide bonds. The structure was solved using single-wavelength anomalous diffraction from sulfur-containing residues (sulfur SAD) to generate phase information. Biochemical and circular dichroism (CD) experiments show that a second PLVAP ECD segment also has a parallel dimeric alpha-helical configuration-presumably a coiled coil-held together with interchain disulfide bonds. Overall, ~2/3 of the ~390 amino acids within the PLVAP ECD adopt a helical configuration, as determined by CD. We also determined the sequence and epitope of MECA-32, an anti-PLVAP antibody. Taken together, these data lend strong support to the model of capillary diaphragms formulated by Tse and Stan in which approximately ten PLVAP dimers are arranged within each 60- to 80-nm-diameter opening like the spokes of a bicycle wheel. Passage of molecules through the wedge-shaped pores is presumably determined both by the length of PLVAP-i.e., the long dimension of the pore-and by the chemical properties of amino acid side chains and N-linked glycans on the solvent-accessible faces of PLVAP.
MeSH term(s)	Diaphragm/metabolism ; Endothelial Cells/metabolism ; Carrier Proteins/metabolism ; Endothelium, Vascular/metabolism ; Disulfides/metabolism ; Circular Dichroism
Chemical Substances	Carrier Proteins ; Disulfides
Language	English
Publishing date	2023-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2221103120
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Article ; Online: The structure of a LAIR1-containing human antibody reveals a novel mechanism of antigen recognition.

Hsieh, Fu-Lien / Higgins, Matthew K

eLife

2017 Volume 6

Abstract: Antibodies are critical components of the human adaptive immune system, providing versatile scaffolds to display diverse antigen-binding surfaces. Nevertheless, most antibodies have similar architectures, with the variable immunoglobulin domains of the ... ...

Abstract	Antibodies are critical components of the human adaptive immune system, providing versatile scaffolds to display diverse antigen-binding surfaces. Nevertheless, most antibodies have similar architectures, with the variable immunoglobulin domains of the heavy and light chain each providing three hypervariable loops, which are varied to generate diversity. The recent identification of a novel class of antibody in humans from malaria endemic regions of Africa was therefore surprising as one hypervariable loop contains the entire collagen-binding domain of human LAIR1. Here, we present the structure of the Fab fragment of such an antibody. We show that its antigen-binding site has adopted an architecture that positions LAIR1, while itself being occluded. This therefore represents a novel means of antigen recognition, in which the Fab fragment of an antibody acts as an adaptor, linking a human protein insert with antigen-binding potential to the constant antibody regions which mediate immune cell recruitment.
Language	English
Publishing date	2017-05-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.27311
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Article ; Online: The structure of a LAIR1-containing human antibody reveals a novel mechanism of antigen recognition

Fu-Lien Hsieh / Matthew K Higgins

eLife, Vol

2017 Volume 6

Abstract	Antibodies are critical components of the human adaptive immune system, providing versatile scaffolds to display diverse antigen-binding surfaces. Nevertheless, most antibodies have similar architectures, with the variable immunoglobulin domains of the heavy and light chain each providing three hypervariable loops, which are varied to generate diversity. The recent identification of a novel class of antibody in humans from malaria endemic regions of Africa was therefore surprising as one hypervariable loop contains the entire collagen-binding domain of human LAIR1. Here, we present the structure of the Fab fragment of such an antibody. We show that its antigen-binding site has adopted an architecture that positions LAIR1, while itself being occluded. This therefore represents a novel means of antigen recognition, in which the Fab fragment of an antibody acts as an adaptor, linking a human protein insert with antigen-binding potential to the constant antibody regions which mediate immune cell recruitment.
Keywords	antibody structure ; LAIR1 ; novel antigen recognition ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2017-05-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Structure of the RECK CC domain, an evolutionary anomaly.

Chang, Tao-Hsin / Hsieh, Fu-Lien / Smallwood, Philip M / Gabelli, Sandra B / Nathans, Jeremy

Proceedings of the National Academy of Sciences of the United States of America

2020 Volume 117, Issue 26, Page(s) 15104–15111

Abstract: Five small protein domains, the CC-domains, at the N terminus of the RECK protein, play essential roles in signaling by WNT7A and WNT7B in the context of central nervous system angiogenesis and blood-brain barrier formation and maintenance. We have ... ...

Abstract	Five small protein domains, the CC-domains, at the N terminus of the RECK protein, play essential roles in signaling by WNT7A and WNT7B in the context of central nervous system angiogenesis and blood-brain barrier formation and maintenance. We have determined the structure of CC domain 4 (CC4) at 1.65-Å resolution and find that it folds into a compact four-helix bundle with three disulfide bonds. The CC4 structure, together with homology modeling of CC1, reveals the surface locations of critical residues that were shown in previous mutagenesis studies to mediate GPR124 binding and WNT7A/WNT7B recognition and signaling. Surprisingly, sequence and structural homology searches reveal no other cell-surface or secreted domains in vertebrates that resemble the CC domain, a pattern that is in striking contrast to other ancient and similarly sized domains, such as Epidermal Growth Factor, Fibronectin Type 3, Immunoglobulin, and Thrombospondin type 1 domains, which are collectively present in hundreds of proteins.
MeSH term(s)	Amino Acid Sequence ; Animals ; Caenorhabditis elegans ; Evolution, Molecular ; GPI-Linked Proteins/chemistry ; GPI-Linked Proteins/genetics ; GPI-Linked Proteins/metabolism ; Humans ; Mice ; Protein Domains ; Sequence Alignment
Chemical Substances	GPI-Linked Proteins ; Reck protein, mouse
Language	English
Publishing date	2020-06-15
Publishing country	United States
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	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2006332117
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Article ; Online: The structural basis for CD36 binding by the malaria parasite.

Hsieh, Fu-Lien / Turner, Louise / Bolla, Jani Reddy / Robinson, Carol V / Lavstsen, Thomas / Higgins, Matthew K

Nature communications

2016 Volume 7, Page(s) 12837

Abstract: CD36 is a scavenger receptor involved in fatty acid metabolism, innate immunity and angiogenesis. It interacts with lipoprotein particles and facilitates uptake of long chain fatty acids. It is also the most common target of the PfEMP1 proteins of the ... ...

Abstract	CD36 is a scavenger receptor involved in fatty acid metabolism, innate immunity and angiogenesis. It interacts with lipoprotein particles and facilitates uptake of long chain fatty acids. It is also the most common target of the PfEMP1 proteins of the malaria parasite, Plasmodium falciparum, tethering parasite-infected erythrocytes to endothelial receptors. This prevents their destruction by splenic clearance and allows increased parasitaemia. Here we describe the structure of CD36 in complex with long chain fatty acids and a CD36-binding PfEMP1 protein domain. A conserved hydrophobic pocket allows the hugely diverse PfEMP1 protein family to bind to a conserved phenylalanine residue at the membrane distal tip of CD36. This phenylalanine is also required for CD36 to interact with lipoprotein particles. By targeting a site on CD36 that is required for its physiological function, PfEMP1 proteins maintain the ability to tether to the endothelium and avoid splenic clearance.
Language	English
Publishing date	2016-09-26
Publishing country	England
Document type	Journal Article
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/ncomms12837
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The structural basis for CD36 binding by the malaria parasite

Fu-Lien Hsieh / Louise Turner / Jani Reddy Bolla / Carol V. Robinson / Thomas Lavstsen / Matthew K. Higgins

Nature Communications, Vol 7, Iss 1, Pp 1-

2016 Volume 11

Abstract: Targeting of the CD36 scavenger receptor by the malaria parasite effector PfEMP1 prevents splenic clearance of infected erythrocytes. Here, the authors propose that diverse PfEMP1 achieve this by binding to a conserved phenylalanine residue in CD36 that ... ...

Abstract	Targeting of the CD36 scavenger receptor by the malaria parasite effector PfEMP1 prevents splenic clearance of infected erythrocytes. Here, the authors propose that diverse PfEMP1 achieve this by binding to a conserved phenylalanine residue in CD36 that is also required for lipoprotein binding.
Keywords	Science ; Q
Language	English
Publishing date	2016-09-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Structure and functional properties of Norrin mimic Wnt for signalling with Frizzled4, Lrp5/6, and proteoglycan.

Chang, Tao-Hsin / Hsieh, Fu-Lien / Zebisch, Matthias / Harlos, Karl / Elegheert, Jonathan / Jones, E Yvonne

eLife

2015 Volume 4

Abstract: Wnt signalling regulates multiple processes including angiogenesis, inflammation, and tumorigenesis. Norrin (Norrie Disease Protein) is a cystine-knot like growth factor. Although unrelated to Wnt, Norrin activates the Wnt/β-catenin pathway. Signal ... ...

Abstract	Wnt signalling regulates multiple processes including angiogenesis, inflammation, and tumorigenesis. Norrin (Norrie Disease Protein) is a cystine-knot like growth factor. Although unrelated to Wnt, Norrin activates the Wnt/β-catenin pathway. Signal complex formation involves Frizzled4 (Fz4), low-density lipoprotein receptor related protein 5/6 (Lrp5/6), Tetraspanin-12 and glycosaminoglycans (GAGs). Here, we report crystallographic and small-angle X-ray scattering analyses of Norrin in complex with Fz4 cysteine-rich domain (Fz4CRD), of this complex bound with GAG analogues, and of unliganded Norrin and Fz4CRD. Our structural, biophysical and cellular data, map Fz4 and putative Lrp5/6 binding sites to distinct patches on Norrin, and reveal a GAG binding site spanning Norrin and Fz4CRD. These results explain numerous disease-associated mutations. Comparison with the Xenopus Wnt8-mouse Fz8CRD complex reveals Norrin mimics Wnt for Frizzled recognition. The production and characterization of wild-type and mutant Norrins reported here open new avenues for the development of therapeutics to combat abnormal Norrin/Wnt signalling.
MeSH term(s)	Binding Sites ; Crystallography, X-Ray ; Eye Proteins/chemistry ; Eye Proteins/genetics ; Eye Proteins/metabolism ; Frizzled Receptors/chemistry ; Frizzled Receptors/metabolism ; Humans ; Low Density Lipoprotein Receptor-Related Protein-5/metabolism ; Low Density Lipoprotein Receptor-Related Protein-6/metabolism ; Mutant Proteins/chemistry ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Protein Conformation ; Proteoglycans/chemistry ; Proteoglycans/metabolism ; Scattering, Small Angle
Chemical Substances	Eye Proteins ; FZD4 protein, human ; Frizzled Receptors ; Low Density Lipoprotein Receptor-Related Protein-5 ; Low Density Lipoprotein Receptor-Related Protein-6 ; Lrp5 protein, mouse ; Lrp6 protein, mouse ; Mutant Proteins ; NDP protein, human ; Nerve Tissue Proteins ; Proteoglycans
Language	English
Publishing date	2015-07-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.06554
Database	MEDical Literature Analysis and Retrieval System OnLINE

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