Isolation and characterization of antibody fragment selective for human Alzheimer’s disease brain-derived tau variants
Reagents that can selectively recognize specific toxic tau variants associated with onset and progression of Alzheimer’s disease (AD) and other tauopathies can be effective diagnostic and therapeutic tools. We utilized a novel atomic force microscopy–based biopanning protocol to isolate antibody fra...
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| Published in | Neurobiology of aging Vol. 94; pp. 7 - 14 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
01.10.2020
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| Abstract | Reagents that can selectively recognize specific toxic tau variants associated with onset and progression of Alzheimer’s disease (AD) and other tauopathies can be effective diagnostic and therapeutic tools. We utilized a novel atomic force microscopy–based biopanning protocol to isolate antibody fragments (single chain variable fragments, scFvs) that selectively bind tau variants present in human AD but not cognitively normal age-matched brain tissue. We identified 6 scFvs [Alzheimer's disease tau (ADT)-1 through 6] that readily distinguished between AD and control tissue and sera samples. We utilized 3 of the scFvs (ADT-2, ADT-4, and ADT-6) to analyze longitudinal plasma samples from 50 human patients, 25 patients which converted to AD during the study and 25 that remained cognitively normal. All 3 scFvs could distinguish the AD from control samples with higher tau levels in apolipoprotein E3/3 AD cases compared to apolipoprotein E3/4. Immunohistochemical analyses of human AD brain slices indicated several but not all tau variants overlapping with phosphorylated tau staining. Several reagents also showed therapeutic potential, protecting neuronal cells against AD tau-induced toxicity.
•Identified antibody fragments that selectively bind tau variants present in human postmortem AD brain tissue.•All reagents selectively react with human postmortem AD brain tissue and sera samples but not age-matched cognitively normal control samples.•Reagents selectively react with longitudinal human plasma samples from patients that converted to AD indicating early, presymptomatic diagnostic capability.•Reagents selectively label tau variants in human brain tissue samples.•Reagents block toxicity of tua variants isolated from human AD brain tissue toward a human neuronal cell line. |
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| AbstractList | Reagents that can selectively recognize specific toxic tau variants associated with onset and progression of Alzheimer's disease (AD) and other tauopathies can be effective diagnostic and therapeutic tools. We utilized a novel atomic force microscopy-based biopanning protocol to isolate antibody fragments (single chain variable fragments, scFvs) that selectively bind tau variants present in human AD but not cognitively normal age-matched brain tissue. We identified 6 scFvs [Alzheimer's disease tau (ADT)-1 through 6] that readily distinguished between AD and control tissue and sera samples. We utilized 3 of the scFvs (ADT-2, ADT-4, and ADT-6) to analyze longitudinal plasma samples from 50 human patients, 25 patients which converted to AD during the study and 25 that remained cognitively normal. All 3 scFvs could distinguish the AD from control samples with higher tau levels in apolipoprotein E3/3 AD cases compared to apolipoprotein E3/4. Immunohistochemical analyses of human AD brain slices indicated several but not all tau variants overlapping with phosphorylated tau staining. Several reagents also showed therapeutic potential, protecting neuronal cells against AD tau-induced toxicity. Reagents that can selectively recognize specific toxic tau variants associated with onset and progression of Alzheimer’s disease (AD) and other tauopathies can be effective diagnostic and therapeutic tools. We utilized a novel atomic force microscopy–based biopanning protocol to isolate antibody fragments (single chain variable fragments, scFvs) that selectively bind tau variants present in human AD but not cognitively normal age-matched brain tissue. We identified 6 scFvs [Alzheimer's disease tau (ADT)-1 through 6] that readily distinguished between AD and control tissue and sera samples. We utilized 3 of the scFvs (ADT-2, ADT-4, and ADT-6) to analyze longitudinal plasma samples from 50 human patients, 25 patients which converted to AD during the study and 25 that remained cognitively normal. All 3 scFvs could distinguish the AD from control samples with higher tau levels in apolipoprotein E3/3 AD cases compared to apolipoprotein E3/4. Immunohistochemical analyses of human AD brain slices indicated several but not all tau variants overlapping with phosphorylated tau staining. Several reagents also showed therapeutic potential, protecting neuronal cells against AD tau-induced toxicity. •Identified antibody fragments that selectively bind tau variants present in human postmortem AD brain tissue.•All reagents selectively react with human postmortem AD brain tissue and sera samples but not age-matched cognitively normal control samples.•Reagents selectively react with longitudinal human plasma samples from patients that converted to AD indicating early, presymptomatic diagnostic capability.•Reagents selectively label tau variants in human brain tissue samples.•Reagents block toxicity of tua variants isolated from human AD brain tissue toward a human neuronal cell line. |
| Author | Sierks, Michael R. He, Ping Venkataraman, Lalitha Schulz, Philip |
| Author_xml | – sequence: 1 givenname: Lalitha surname: Venkataraman fullname: Venkataraman, Lalitha organization: Department of Neuroscience, School of Life Sciences, Arizona State University, Tempe, AZ, USA – sequence: 2 givenname: Ping surname: He fullname: He, Ping organization: Department of Chemical Engineering, School for Engineering, Matter, Transport and Energy, Arizona State University, Tempe, AZ, USA – sequence: 3 givenname: Philip surname: Schulz fullname: Schulz, Philip organization: Department of Chemical Engineering, School for Engineering, Matter, Transport and Energy, Arizona State University, Tempe, AZ, USA – sequence: 4 givenname: Michael R. orcidid: 0000-0001-7301-230X surname: Sierks fullname: Sierks, Michael R. email: sierks@asu.edu organization: Department of Chemical Engineering, School for Engineering, Matter, Transport and Energy, Arizona State University, Tempe, AZ, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32497877$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1007_s12035_024_04035_5 crossref_primary_10_1093_abt_tbab004 crossref_primary_10_3390_ijms232415670 crossref_primary_10_1186_s12868_020_00586_0 |
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| Keywords | Tau Biomarker Alzheimer’s disease Single chain antibody fragment |
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