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Patent US7510881 - Using gold-particle labelled reagents and an antibody conjugate to bind to a ... - Google PatentsSearch Images Maps Play YouTube News Gmail Drive More »Sign inAdvanced Patent SearchPatentsA method and kit for quantitatively and/or qualitatively detecting one or more components in samples, including the use of metal-particle labelled reagents and an antibody conjugate are disclosed. The components are capable of binding to a probe. A kit and method for staining components in cell and tissue...http://www.google.com/patents/US7510881?utm_source=gb-gplus-sharePatent US7510881 - Using gold-particle labelled reagents and an antibody conjugate to bind to a probe; cost efficiency, environmentally friendly; colorimetric analysis; staining cells and tissues; diagnosing papillomavirus; incubating with poly- or monoclonal antibody, antibody conjugate, metal enhancer or polypeptideAdvanced Patent SearchPublication numberUS7510881 B2Publication typeGrantApplication numberUS 10/569,713PCT numberPCT/EP2003/009393Publication dateMar 31, 2009Filing dateAug 25, 2003Priority dateAug 25, 2003Fee statusPaidAlso published asDE60325107D1, EP1658497A1, EP1658497B1, US20060286546, WO2005019820A1Publication number10569713, 569713, PCT/2003/9393, PCT/EP/2003/009393, PCT/EP/2003/09393, PCT/EP/3/009393, PCT/EP/3/09393, PCT/EP2003/009393, PCT/EP2003/09393, PCT/EP2003009393, PCT/EP200309393, PCT/EP3/009393, PCT/EP3/09393, PCT/EP3009393, PCT/EP309393, US 7510881 B2, US 7510881B2, US-B2-7510881, US7510881 B2, US7510881B2InventorsMarc Ramael, Jean-Paul SandersOriginal AssigneeMarc Ramael, Jean-Paul SandersExport CitationBiBTeX, EndNote, RefManPatent Citations (7), Non-Patent Citations (5), Referenced by (1), Classifications (18), Legal Events (2) External Links: USPTO, USPTO Assignment, EspacenetUsing gold-particle labelled reagents and an antibody conjugate to bind to a probe; cost efficiency, environmentally friendly; colorimetric analysis; staining cells and tissues; diagnosing papillomavirus; incubating with poly- or monoclonal antibody, antibody conjugate, metal enhancer or polypeptide
US 7510881 B2Abstract
13. The method according to claim 1, wherein the metal particle is gold. Description
This application is the U.S. National Phase under 35 U.S.C. �371 of International Application PCT/EP2003/009393, filed Aug. 25, 2003.
U.S. Pat. No. 6,451,980 discloses a technique for signal enhancement of bi-specific antibody-polymer probe for use in immunoassay. Therein is described the use of bispecific antibodies where one part of the antibody complex recognises the antigen and the other part binds the polymer probe consisting of a poly-L-lysine backbone coated with �detectable signals�.
For the detection of low concentrations of molecule components in the field of diagnostics, the methods of chemiluminescence and electrochemiluminescence are widely used. These methods provides a means to detect low concentrations of components by amplifying the number of luminescent molecules or photon generating events manyfold, the resulting �signal amplification� then allowing for detection of low concentration components. However, the above mentioned methods of signal amplification have associated limitations which makes the detection of components by these methods complicated, not easy to use, time consuming, and costly.
Problems of interference of chemical or enzymatic reactions, contamination, complicated and multi-step procedures, limited adaptability to single step �homogeneous� (non-separation) formats, and the requirement of costly and sophisticated instrumentation are areas that those in the art are constantly trying to improve.
one or more antibodies, anti-A, directed against immunoglobulins of species A,�one or more antibodies, anti-B, directed against immunoglobulins of species B,
a) applying one or more probes onto a solid support, and step c) is c) incubating solid supports with tag-labelled sample, Another embodiment of the present invention is a method as described above wherein step c) is absent and step d) is
d) incubating solid supports with metal-particle-labelled anti-component monoclonal or polyclonal antibody, said antibody raised in species A. Another embodiment of the present invention is a method as described above further comprising the steps, after step f), of:
f-1) repeating steps e) to f), and f-2) optionally repeating step f-1). Another embodiment of the present invention is a method as described above wherein the solid support is supplied with probe pre-applied, and step a) is not performed by the user.
Another embodiment of the present invention is a kit as described above for use in detecting, diagnosing and/or monitoring the progress infections caused by one or more of one or more of HCV, HIV, HBV, HTLV, mycobacteria, Staphylococcus aureus. Another embodiment of the present invention is a kit as described above for use in detecting, diagnosing and/or monitoring the progress neurodegenerative diseases by detecting one or more of beta-amyloids, hTAU, phosphoTAU and APOE.
Another embodiment of the present invention is a kit as described above for use in environmental testing of food components for genetically modified components, listeria and salmonella. Another embodiment of the present invention is a method for staining components in cell and/or tissue sections suitable for visualisation using microscopy comprising the steps of:
k) incubating section with metal particle labelled anti-component monoclonal or polyclonal antibody, said antibody raised in species A. Another embodiment of the present invention is a method as described above further comprising the steps, after step m), of:
m-1) repeating steps l) to m), and m-2) optionally repeating step m-1). Another embodiment of the present invention is a kit for staining components in cell and/or tissue sections suitable for visualisation using microscopy comprising:
A �sample� as used herein means any sample that contains one or more components to be tested, said components capable of binding to a probe enabling identification of said component. Examples of samples or components include, but are not limited to DNA, cDNA, mRNA, RNA, nucleic acids, proteins, polypeptides, glycoproteins, receptors, ligands, metabolites, toxins etc. Other examples of samples include, but are not limited to blood, blood components, other bodily fluids, tissues, drinking water, soil, domestic waste, industrial waste, any food stuff�liquid or solid, crops.
A �probe� as used herein means any compound capable of specific binding to a component. For example, a nucleic acid oligomer binding to a gene, a ligand binding to a receptor are examples of probe/component interactions according to the invention. According to the present invention, the affinity of binding between a probe and a component is better than 10 uM, 5 uM, 2 uM, 1 uM, 0.1 uM, 0.01 uM or 1 nM. Examples of probes include but are not limited to nucleic acids, PNAs, proteins, peptides, antibodies, ligands, receptors etc.
A �tag� as used here means any type of substance which is capable of being recognised by an antibody. Examples of such tags include, but are not limited to polypeptides, proteins, polysaccharides, amino acids, vitamins (such as biotin), natural or synthetic substances, enzymes (such as AP and HRP), dyes (such as FITC and TR), nucleic acids, PNA, DNP, digoxygenin, streptavidin, Psoralen. A �tag� as used here also means a metal, metals or organometallic substances. According to one aspect of the invention, the probe is tagged.
By �solid support� herein is meant any solid support which is capable of immobilising components and/or samples. Such solid supports are known in the art and include, but are not limited to, nitrocellulose, glass slides, nylon, silane coated slides, nitrocellulose coated slides, plastics. The solid support preferably comprises nitrocellulose.
An �antibody conjugate� refers to a complex comprising a bridging compound with an antibody directed against antibodies raised in one species (anti-A, e.g. against part of the constant region of mouse antibodies) and/or an antibody directed against antibodies raised in a different species (anti-B, e.g. against part of the constant region of rabbit antibodies). Attachment may be by covalent or non-covalent means. Examples of species against which said attached antibodies may be raised include, but are not limited to rabbit, human, goat, mouse, rat, cow, calf, camel, llama, monkey, donkey, guinea pig, chicken and sheep.
By �applying� as used herein in reference to applying one or more samples or probes to a solid support, is meant deposition of one or more synthetic or biological substances on a solid support. The deposition may be by a manual method or by using a device, resulting in an action including, but not limited to spotting, pipetting, printing, jet printing, dropping etc.
By �reading� as used herein means determining from the change in the properties of the solid support at the position where the sample or probe is applied, the concentration of the components. According to the invention a change in the property of the solid support may be a colour change and/or a change in electrical conductivity or electrical current at the position where the sample or probe is applied.
The �metal enhancement reagent� of step g) is any metal-containing reagent wherein the metal precipitates due to reduction. Examples include but are not limited to a silver enhancement reagent by Aurion (the Netherlands), BBI (UK), Sigma-Aldrich (USA), or Amersham (UK).
The �polypeptide capable of recognition by anti-B antibodies� in step f) can be any polypeptide or substance which is recognised by the anti-B antibody attached to the antibody conjugate of step e). If it is a polypeptide, it might be an antibody raised in species B, or an antigenic part thereof. If it is another substance, it might be polysaccharides, amino acid, natural or synthetic substances, nucleic acids, PNA, which is capable of binding to the complimentary determining region of the anti-B antibody of step e).
It is one advantage of the invention that it does not necessarily require an optical reading device such as a laser scanner or back-scatter measuring equipment, and hence is convenient for use in environments away from laboratory conditions. The invention allows quantitative and/or qualitative results to be obtained at the location at which the sample was taken, for example, in a general practitioner's surgery, in an individual's home, in hospitals, generally �in the field� without any specialist analytical instruments. Furthermore, the invention provides an assay that is as sensitive as, or more sensitive than assays which use fluorescence. Furthermore, since specialised measuring equipment is not necessarily required, the assay could be performed by a non-specialist.
cystic fibrosis transmembrane conductance regulator, ATP-
amyloid beta (A4) precursor protein (protease nexin-II,
huntington (Huntington disease)
dystrophin (muscular dystrophy, Duchenne and Becker
cyclin-dependent kinase inhibitor 2A (melanoma, p16,
hypoxanthine phosphoribosyltransferase 1 (Lesch-Nyhan
Mdm2, transformed 3T3 cell double minute 2, p53 binding
runt-related transcription factor 1 (acute myeloid leukemia
superoxide dismutase 1, soluble (amyotrophic lateral
neurofibromin 1 (neurofibromatosis, von Recklinghausen
phosphatase and tensin homolog (mutated in multiple
fibroblast growth factor receptor 3 (achondroplasia,
epidermal growth factor receptor (erythroblastic leukemia
androgen receptor (dihydrotestosterone receptor; testicular
transforming growth factor, beta 1 (Camurati-Engelmann
ret proto-oncogene (multiple endocrine neoplasia and
cytochrome P450, subfamily I (aromatic compound-
catenin (cadherin-associated protein), beta 1 (88 kD)
v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene
ATPase, Cu++ transporting, beta polypeptide (Wilson
v-jun sarcoma virus 17 oncogene homolog (avain)
cytochrome P450, subfamily IIC (mephenytoin 4-
fibroblast growth factor receptor 2 (bacteria-expressed
fibroblast growth factor receptor 1 (fms-related tyrosine
CD44 antigen (homing function and Indian blood group
matrix metalloproteinase 9 (gelatinase B, 92 kD gelatinase,
ABO blood group (transferase A, alpha 1-3-N-
small inducible cytokine A2 (monocyte chemotactic protein
clusterin (complement lysis inhibitor, SP-40, 40, sulfated
caspase 1, apoptosis-related cysteine protease (interleukin
major histocompatibility complex, class I, A, B, C
apolipoprotein A�I
intercellular adhesion molecule 1 (CD54), human rhinovirus
cytochrome P450, subfamily XIX (aromatization of
coagulation factor VII (serum prothrombin conversion
glucokinase (hexokinase 4, maturity onset diabetes of the
secreted phosphoprotein 1 (osteopontin, bone sialoprotein
ubiquitin protein ligase E3A (human papilloma virus E6-
cytochrome P450, subfamily I (dioxin-inducible),
tissue inhibitor of metalloproteinase 1 (erythroid potentiating
signal transducer and activator of transcription 3 (acute-
cell division cycle 42 (GTP binding protein, 25 kD)
transforming growth factor, beta receptar II (70�80 kD)
cytochnome P450, subfamily IIA (phenobarbital-inducible),
heat shock 90 kD protein 1, alpha
gap junction protein, beta 1, 32 kD (connexin 32, Charcot-
ADP-ribosyltransferase (NAD+; poly (ADP-ribose)
platelet-derived growth factor beta polypeptide (simian
protein phosphatase 3 (formerly 2B), regulatory subunit B
collagen, type III, alpha 1 (Ehlers-Danlos syndrome type IV,
coagulation factor IX (plasma thromboplastic component,
v-myc myelocytomatosis viral related oncogene,
IiIL12B
interleukin 12B (natural killer cell stimulatory factor 2,
cytochrome P450, subfamily IIE (ethanol-inducible)
ATPase, Cu++ transporting, alpha polypeptide (Menkes
transcription factor 1, hepatic; LF-B1, hepatic nuclear factor
cytochrome P450, subfamily XVII (steroid 17-alpha-
excision repair cross-complementing rodent repair
transforming growth factor, beta-induced, 68 kD
potassium voltage-gated channel, KQT-like subfamily,
interleukin 2 receptor, gamma (severe combined
colony stimulating factor 1 receptor, formerly McDonough
SHC (Src homology 2 domain containing) transforming
chemokine (C�X�C motif), receptor 4 (fusin)
membrane metallo-endopeptidase (neutral endopeptidase,
hypoxia-inducible factor 1, alpha subunit (basic helix-loop-
caspase 2, apoptosis-related cysteine protease (neural
thyroid hormone receptor, alpha (erythroblastic leukemia
ATPase, H+ transporting, lysosomal (vacuolar proton
thyroid hormone receptor, beta (erythroblastic leukemia
signal transducer and activator of transcription 6,
elastin (supravalvular aortic stenosis, Williams-Beuren
integrin, beta 2 (antigen CD18 (p95), lymphocyte function-
prostaglandin-endoperoxide synthase 1 (prostaglandin G/H
spinocerebellar ataxia 1 (olivopontocerebellar ataxia 1,
matrix metalloproteinase 13 (callagenase 3)
rhodopsin (opsin 2, rod pigment) (retinitis pigmentosa 4,
topoisomerase (DNA) II alpha (170 kD)
cytochrome b-245, beta polypeptide (chronic
laminin receptor 1 (67 kD, ribosomal protein SA)
interleukin 12A (natural killer cell stimulatory factor 1,
cytochrome P450, subfamily XXIA (steroid 21-hydroxylase,
solute carrier family 2 (facilitated glucose transporter),
interferon gamma receptor 2 (interferon gamma transducer
gap junction protein, alpha 1, 43 kD (connexin 43)
chemokine (C�C motif) receptor 2
catenin (cadherin-associated protein), alpha 1 (102 kD)
myosin VIIA (Usher syndrome 1B (autosomal recessive,
transforming growth factor, beta receptor I (activin A
ras-related C3 botulinum toxin substrate 1 (rho family, small
The antibody conjugate is already defined herein. The introduction of other steps into the method, such as wash steps, for example, may be known by the skilled artisan practicing in the field of immunohistochemistry. The �metal enhancement reagent� of step q) is already defined herein for step i). The sections described above are visualised by observing the dye, by observing the metal, by metal enhancement and/or by making use of the enzyme that catalyses the colour change attached to the antibody conjugate. It is an aspect of the invention to visualise the samples using metal enhancement alone. It is an aspect of the invention to visualise the samples by observing the dye alone. It is an aspect of the invention to visualise the samples by observing the metal without metal enhancement. It is an aspect of the invention to visualise the samples using only enzyme-linked colour change. It is an aspect of the invention to visualise the samples using one or more of the aforementioned visualisations.
Target: 5′ GGATTATTGTTAAATATTGATAAGGAT 3′ Visualisation 5′ ATCCTTATCAATATT 3′ oligo: Oligo op drager: 5′ TAACAATAATCC 3′ The above mentioned oligonucleotides are derived from the Anthrax lethal factor genome.
Mofified DNA oligonucleotides were custom made by Qbiogene (France) and in varying concentrations dissolved in printing buffer (6�SSC).
Micro-arrays were manufactured by printing varying oligonucleotide concentrations ranging from 0.001 μM to 20 μM on the coated glass slide. Negative controls consisted of printing buffer without DNA oligonucleotides and printing buffer with a DNA oligonucleotide complementary to a non-related sequence in the same concentration as the capturing oligonucleotide of interest. After drying during 30 minutes at room temperature, the slides were baked at 80� C. during 30 minutes. DNA printed at Nytran coated slides was cross linked using UV radiation according to previously described protocols.
Slides were stored dustfree at 4� C. until further analysis.
Micro-arrays were manufactured by printing varying oligonucleotide concentrations ranging from 0.001 μM to 20 μM on the activated silane coated glass slide. After drying during 30 minutes at room temperature, the printed slides were stored dustfree at 4� C.
Classical microscopical glass slides were washed with bidistilled water followed by immersion in a 10% NaOH solution at room temperature after an ultrasound treatment during 30 minutes. After several washes in running tap water, slides were washed several times with bidistilled water. Afterwards the slides were dried at 80� C.
Part 1�Visualization Experiments of Labeled Oligonucleotides Attached at the Above Described Solid Assays
Experiment 1�part 1: Visualization of Labeled Oligonucleotides using Streptavidin
Micro-arrays were printed as described previously. All concentrations ranging from 0.001 μM to 20 μM were spotted in sixfold. Micro-arrays were baked at 80� C. during 30 minutes and stored dust-free at 4� C. until use.
Experiment 2�Part 1: Visualization of Labeled Oligonucleotides using Streptavin Labeled with Gold Particles
Micro-arrays were printed like described previously. All concentrations ranging from 0.001 μM to 20 μM were spotted in sixfold. Micro-arrays were baked at 80� C. during 30 minutes and stored dust-free at 4� C. until use.
Experiment 3�Part 1: Visualization of Labeled Oligonucleotides using Monoclonal Antibodies Labeled with Gold Particles
Experiment 4�Part 1: Visualization of Labeled Oligonucleotides using Polyclonal Antibodies Labeled with Gold Particles
Experiment 5�Part 1: Visualization of Labeled Oligonucleotides using Monoclonal and Polyclonal Antibodies in a Polymer Enhanced Amplification Technique Visualized Enzymatically
Experiment 6�Part 1: Visualization of Labeled Oligonucleotides using Gold Labeled Monoclonal and Polyclonal Antibodies in a Polymer Enhanced Amplification Technique
Experiment 7�Part 1: Visualization of Labeled Oligonucleotides using CARD Amplification Technology Visualized Enzymatically
Experiment 8�Part 1: Visualization of Labeled Oligonucleotides using CARD Amplification Technology Visualized with Gold Labeled Streptavidin
Experiment 9�Part 1: Visualization of Labeled Oligonucleotides using CARD Amplification Technology Visualized with Gold Labeled Monoclonal or Polyclonal Antibodies
Experiment 2.1�Part 2: Visualization of Labeled Oligonucleotides using Streptavidin
Micro-arrays were printed like described previously. All concentrations ranging from 0.001 μM to 20 μM were spotted in sixfold including adequate positive and negative controls. Micro-arrays were baked at 80� C. during 30 minutes and stored dust free at 4� C. until use.
Hybridization assay was set up using target DNA and/or visualisation oligonucleotide in a concentration of 250 ng/ml hybridization mixture. Hybridization was carried out overnight at 37� C.
Slides were washed twice with 2�SSC at room temperature.
Experiment 2.2�Part 2: Visualization of Labeled Oligonucleotides using Streptavin Labeled with Gold Particles
Hybridization was carried out overnight at 37� C.
Experiment 3�Part 2: Visualization of Labeled Oligonucleotides using Monoclonal Antibodies Labeled with Gold Particles
Micro-arrays were printed like described previously. All concentrations ranging from 0.001 μM to 20 μM were spotted in sixfold. Micro-arrays were baked at 80� C. during 30 minutes and stored dustfree at 4� C. until use.
Slides were washed twice with 2�SSC at room temperature
Experiment 4�Part 2: Visualization of Labeled Oligonucleotides using Polyclonal Antibodies Labeled with Gold Particles
Experiment 5�Part 2: Visualization of Labeled Oligonucleotides using Monoclonal and Polyclonal Antibodies in a Polymer Enhanced Amplification Technique Visualized Enzymatically
Experiment 6�Part 2: Visualization of Labeled Oligonucleotides using Gold Labeled Monoclonal and Polyclonal Antibodies in a Polymer Enhanced Amplification Technique
Experiment 7�Part 2: Visualization of Labeled Oligonucleotides using CARD Amplification Technology Visualized Enzymatically
Experiment 8�Part 2: Visualization of Labeled Oligonucleotides using CARD Amplification Technology Visualized with Gold Labeled Streptavidin
Experiment 9�Part 2: Visualization of Labeled Oligonucleotides using CARD Amplification Technology Visualized with Gold Labeled Monoclonal or Polyclonal Antibodies
Experiment 1�Visualization with Streptavidin-Enzyme
Experiment 2�Visualization with Streptavidin Gold 0.8 nm and 6 nm
Experiment 3�Visualization with Monoclonal Mouse Antibodies with Gold 0.8 nm and 6 nm
Experiment 3�Visualization with Monoclonal Mouse Antibodies with Gold 40 nm
Experiment 4�Visualization with Polyclonal Goat Antibodies with Gold 0.8 nm and 6 nm
Results of Experiments with Signal Amplification�CARD-Amplification with Short Spacer:
Experiment 7�Visualization with Streptavidin-Enzyme
Experiment 8�Visualization with Streptavidin Gold 0.8 nm and 6 nm
Experiment 9�Visualization with Polyclonal Goat Antibodies with Gold 0.8 nm and 6 nm
Experiment 9�Visualization with Monoclonal Mouse Antibodies with Gold 0.8 nm and 6 nm
Experiment 9�Visualization with Monoclonal Mouse Antibodies with Gold 40 nm
Results of Experiments with Signal Amplification�CARD-Amplification with Long Spacer:
Results of Experiments with Signal Amplification�Amplification using Polymertechnology:
Experiment 5�Visualization with Monoclonal Antibodies/Polymer Labeled with Alkaline Phosphatase
Experiment 6�Visualization with Polyclonal Goat Antibodies with Gold 0.8 nm, 6 nm and 40 nm/Polymer/Monoclonal Mouse Antibodies 0.8 nm, 6 nm and 40 nm
Experiment 6�Visualization with Monoclonal Mouse Antibodies 0.8 nm, 6 nm, 40 nm/Polymer/Polyclonal Goat Antibodies with Gold 0.8 nm, 6 nm and 40 nm
Experiment 6�Visualization with Monoclonal Goat Antibodies with Gold 0.8 nm, 6 nm, 40 nm/Polymer/Monoclonal Mouse Antibodies 0.8 nm, 6 nm and 40 nm
Experiment 6�Visualization with Monoclonal Mouse Antibodies with Gold 40 nm/Polymer/Monoclonal Mouse Antibodies with Gold 40 nm
Micro-arrays were baked at 80� C. during 30 minutes and stored dust-free at 4� C. until use.
Ten microliter of the PCR amplification product was denatured with 10 μl denaturation solution (NAOH/EDTA). The denatured DNA solution was added to 2 ml of hybridization mixture. The micro-arrays were covered with a cover slip and hybridized overnight at 37� C. in a humid chamber.
Slides were washed twice with 2�SSC supplemented with 0.1% SDS at room temperature.
Sections of 5 μm were cut from paraffin embedded formalin fixed tissue of squamous lung carcinoma and adhered to poly-l-lysine coated glass slides, dried at 55� C. overnight and stored dust-free at room temperature. The sections were deparaffinized in two rinses of xylene substitute, followed by rehydratation in an descending series of alcohols down to deionized water. Slides were washed twice with PBS (pH 7.4) and incubated with anti-ema (epithelial membrane antigen) monoclonal mouse antibody (Dakopatts Denmark) according to the instructions of the manufacturer). Slides were washed twice with PBS (pH 7.4) supplemented with BSA.
After printing the micro-arrays were air dried at room temperature for 15 minutes and stored dust-free at 4� C. until use.
After printing the micro-arrays were air dried at room temperature for 15 minutes and stored dust free at 4� C. until use.
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