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WO2010143983A1 - Essais de détection sérologique de la syphilis - Google Patents

Essais de détection sérologique de la syphilis Download PDF

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Publication number
WO2010143983A1
WO2010143983A1 PCT/NZ2010/000111 NZ2010000111W WO2010143983A1 WO 2010143983 A1 WO2010143983 A1 WO 2010143983A1 NZ 2010000111 W NZ2010000111 W NZ 2010000111W WO 2010143983 A1 WO2010143983 A1 WO 2010143983A1
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WO
WIPO (PCT)
Prior art keywords
cis
acid
peptide
rbcs
integer
Prior art date
Application number
PCT/NZ2010/000111
Other languages
English (en)
Inventor
Stephen Micheal Henry
Venkata Sarvani Komarraju
Eleanor Christine Williams
Original Assignee
Kode Biotech Limited
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Kode Biotech Limited filed Critical Kode Biotech Limited
Priority to AU2010259360A priority Critical patent/AU2010259360B2/en
Publication of WO2010143983A1 publication Critical patent/WO2010143983A1/fr

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Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
    • G01N33/56911—Bacteria
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
    • C07K17/02—Peptides being immobilised on, or in, an organic carrier
    • C07K17/08—Peptides being immobilised on, or in, an organic carrier the carrier being a synthetic polymer
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving viable microorganisms
    • C12Q1/04—Determining presence or kind of microorganism; Use of selective media for testing antibiotics or bacteriocides; Compositions containing a chemical indicator therefor
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
    • G01N33/5091—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing the pathological state of an organism
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
    • G01N2333/195—Assays involving biological materials from specific organisms or of a specific nature from bacteria
    • G01N2333/20—Assays involving biological materials from specific organisms or of a specific nature from bacteria from Spirochaetales (O), e.g. Treponema, Leptospira
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2405/00—Assays, e.g. immunoassays or enzyme assays, involving lipids

Definitions

  • the invention relates to methods for the diagnosis of infection with Treponema palladium.
  • the invention relates to methods for the diagnosis of infection with Treponema palladium in donors of blood intended for transfusion.
  • TTIs transfusion transmitted infections
  • Treponema palladium A pathogen of particular concern in transfusion medicine is Treponema palladium. This organism is the causal agent of syphilis. Research has been performed to identify those antigens of Treponema palladium that may be responsible for eliciting an immunogenic response. The presence of antibody in the sera of donors is indicative of infection.
  • Known assays for the serological diagnosis of syphilis include the rapid plasma reagin (RPR) card test (Becton Dickinson Microbiology Systems, Cockeysville, MD) and the solid phase erythrocyte adherence (SPEA) assay CAPTURE-STM (Immucor, Inc., Norcross, GA) (Stone et al (1997)).
  • RPR rapid plasma reagin
  • SPEA solid phase erythrocyte adherence
  • the solid phase erythrocyte adherence assay provides additional benefits of ease of use, accommodation of high-volume testing, and the potential for automation, e.g. the GALILEO ECHOTM platform (Immucor, Inc., Norcross, GA).
  • the invention provides a method for determining the likelihood of infection of a subject with Treponema palladium comprising the steps of:
  • F is a peptide comprising the sequence:
  • L is a lipid selected from the group consisting of diacyl- and dialkyl-glycerolipids, including glycerophospholipids;
  • the degree of agglutination indicates the likelihood of infection of the subject.
  • the method includes prior to determining the degree of agglutination of the cells of the mixture the intermediate step of:
  • the subject is a human.
  • the cells are RBCs.
  • the plasma or serum of a subject is obtained from a donated sample of blood.
  • the anti-subject globulin antibody is anti-human globulin (AHG) antibody.
  • S is selected to provide a construct that is water soluble.
  • the peptide-lipid construct is of the structure:
  • Ri and R 2 are independently selected from the group consisting of: alkyl or alkenyl substituents of the fatty acids trans-3-hexadecenoic acid, cis-5-hexadecenoic acid, cis-7-hexadecenoic acid, cis-9-hexadecenoic acid, cis-6- octadecenoic acid, cis-9-octadecenoic acid, trans-9- octadecenoic acid, trans-11-octadecenoic acid, cis-11- octadecenoic acid, cis-11-eicosenoic acid or cis-13- docsenoic acid;
  • n is the integer 3, 4 or 5;
  • n is the integer 1, 2 or 3;
  • M is a monovalent cation such as H + , Na + , K + or NH 4 + .
  • n is the integer 2.
  • the invention provides a method of testing donated blood for the presence of antibodies indicative of the donor being infected with Treponema palladium comprising the steps of:
  • modified RBCs have been modified to incorporate a peptide-lipid construct of the structure F-S-L where:
  • F is a peptide comprising the sequence:
  • S is a spacer covalently linking F to L;
  • L is a lipid selected from the group consisting of diacyl- and dialkyl-glycerolipids, including glycerophospholipids;
  • the degree of adherence is indicative of the likelihood of the antibodies being present.
  • the determining the degree of adherence of the antiglobulin coated indicator cells to the immobilized layer of modified RBCs is by centrifugation to pellet unbound antiglobulin coated indicator cells.
  • S is selected to provide a construct that is water soluble.
  • the peptide-lipid construct is of the structure:
  • Ri and R 2 are independently selected from the group consisting of: alkyl or alkenyl substituents of the fatty acids trans-3-hexadecenoic acid, cis-5-hexadecenoic acid, cis-7-hexadecenoic acid, cis-9-hexadecenoic acid, cis-6- octadecenoic acid, cis-9-octadecenoic acid, trans-9- octadecenoic acid, trans-11-octadecenoic acid, cis-11- octadecenoic acid, cis-11-eicosenoic acid or cis-13- docsenoic acid;
  • n is the integer 3, 4 or 5;
  • n is the integer 1, 2 or 3;
  • M is a monovalent cation such as H + , Na + , K + or NH 4 + .
  • m is the integer 5 and n is the integer 2.
  • the invention provides a water soluble peptide-lipid construct of the structure F-S-L where:
  • F is a peptide comprising the sequence:
  • S is a spacer covalently linking F to L;
  • L is a lipid selected from the group consisting of diacyl- and dialkyl-glycerolipids, including glycerophospholipids.
  • the water soluble peptide-lipid construct is of the structure:
  • Ri and R 2 are independently selected from the group consisting of: alkyl or alkenyl substituents of the fatty acids trans-3-hexadecenoic acid, cis-5-hexadecenoic acid, cis-7-hexadecenoic acid, cis-9-hexadecenoic acid, cis-6- octadecenoic acid, cis-9-octadecenoic acid, trans-9- octadecenoic acid, trans-11-octadecenoic acid, cis-11- octadecenoic acid, cis-11-eicosenoic acid or cis-13- docsenoic acid;
  • n is the integer 3, 4 or 5;
  • n is the integer 1, 2 or 3;
  • M is a monovalent cation such as H + , Na + , K + or NH 4 + .
  • n is the integer 2.
  • Antibody reactive to an antigen means an immunoglobulin, the presence of which in the serum of a subject is indicative of a phenotype or pathological condition of the subject.
  • PCV packed cell volume
  • Pigma means the colourless fluid part of blood or lymph, in which corpuscles or fat globules are suspended.
  • RBC red blood cell
  • Saline means a solution of one or more salts.
  • “Serum” means the amber-coloured, protein-rich liquid which separates out when blood coagulates.
  • Solid phase immunoassay means an assay in which one component of the immunological reaction, either antigen or antibody, is immobilized onto the surface of a solid phase support and in this context the term "antigen” includes mammalian cells such as erythrocytes (RBCs), leukocytes, lymphocytes, platelets and components of such cells including components prepared by lysing the cells.
  • RBCs erythrocytes
  • leukocytes erythrocytes
  • lymphocytes lymphocytes
  • platelets components of such cells including components prepared by lysing the cells.
  • Solid phase support means an article of manufacture composed of an organic polymer such as polystyrene, polypropylene, polyvinylchloride or nylon, or other materials that are capable of binding a monolayer of mammalian cells, or capable of being adapted to bind a monolayer of mammalian cells, such as glass.
  • Synthetic means made by chemical synthesis.
  • Water soluble means a stable, single phase system is formed when the construct is contacted with water or saline (such as PBS) at a concentration of at least 100 ⁇ g/ml and in the absence of organic solvents or detergents.
  • soluble and disersible are used synonymously.
  • amino acid residues of peptides are identified according to Table 3 of Appendix 2 of Annex C of the Administrative Instructions under the Patent Cooperation Treaty dated 7 February 2007 and in accordance with the convention:
  • FIG. 1 The structure of a peptide-lipid construct (F-S-L) of the invention comprising the peptide sequence:
  • immunogenic peptide sequences are known to be immunogenic, i.e. capable of eliciting the production of antibody.
  • immunogenic peptide sequences are not equally capable of interacting with elicited antibody and therefore providing the basis for a diagnostic assay.
  • SYPH3 This selected peptide sequence (designated SYPH3) has been demonstrated to be superior to the following peptide sequences when used in the diagnostic method described in the specification accompanying international application no. PCT/NZ2008/000239 (publ. no. WO 2009/035347) :
  • ArgValMetTyrAlaSerSerGly (SEQID N0:l) designated SYPHl and:
  • ProGluLysAlaPheArgGluLeu SEQID NO:2
  • the peptides were prepared in the form of peptide-lipid constructs (F-S-L) as described in the specification accompanying international application no. PCT/NZ2008/000266 (publ. no. WO 2009/048343). Each peptide was conjugated via the sulfhydryl residue of a Cys residue located at the carboxy terminus of the sequence (of. Figure 1).
  • RBCs were modified by contacting a suspension of the cells (1 part pcv) with a dispersion of construct at a concentration of 100 ⁇ g/mL or 50 ⁇ g/mL (2 parts pcv) at 37 0 C for 1 hour. Modified cells (kodecytes) were washed three times in phosphate buffered saline (PBS) and resuspended.
  • PBS phosphate buffered saline
  • a suspension of 3% (pcv/v) kodecytes is prepared in PBS and 30 ⁇ l of the suspension mixed with 30 ⁇ l of sample plasma or serum. The mixtures are then incubated for 45 min at 37 0 C. Following incubation the kodecytes are centrifuged for 10 s in an ImmufugeTM (setting: "high") and observed for agglutination before being washed 3 times with PBS.
  • Test Method 1 Both Test Method 1 and Test Method 2 were performed on a GALILEO ECHOTM automated blood bank instrument (Immucor Gamma) .
  • SYPH3-10 kodecytes were created by suspending a packed cell volume (pcv) of group 0 red blood red cells in an equal volume of a solution containing the FSL-SYPH3 construct at a concentration of 10 ⁇ g/ml and incubating for 120 mins at 37 0 C, followed by washing.
  • pcv packed cell volume
  • CAPTURE-FSL-SYPH3TM plates were then prepared mutatis mutandis according to the methods described in Sinor et al (1989), Sinor et al (1990) and Sinor and Eatz (1991).
  • a MICROTITRETM plate having a plurality of recessed wells is first treated with a sufficient quantity of Alcian yellow at a concentration of 0.1 mg/ml so that all of the wells are covered by the Alcian yellow solution.
  • the Alcian yellow solution is allowed to remain in contact with the MICROTITRETM plate for about 30 minutes and excess dye solution is removed.
  • a monolayer of the SYPH3-10 kodecytes is formed on the stained plate by addition of 100 ⁇ L of a 0.2% (v/v) suspension of the SYPH3-10 kodecytes in saline or reagent RBC diluent per well.
  • the SYPH3-10 kodecytes are allowed to settle by gravity for one hour at room temperature.
  • the plate is then washed at least two times with isotonic saline to remove unbound SYPH3-10 kodecytes by an automatic washing apparatus or by manual methods.
  • the MICROTITRETM plate is then placed in an inverted position into a foil packet or pouch having at least two, 2 g capacity molecular sieve dessicant packets therein.
  • the pouch is sealed with heat and dried for seven days at 2°to 8 0 C.
  • the CAPTURE-S plates and the CAPTURE-FSL-SYPH3 plates are each used according to the standard test method. Briefly, the foil package containing each plate is opened and one drop of a biological fluid such as serum or plasma or a control is added to each. Two drops of a 19 g/L solution of glycine with a preservative and a dye for colour is also added to each well.
  • a biological fluid such as serum or plasma or a control
  • Two drops of a 19 g/L solution of glycine with a preservative and a dye for colour is also added to each well.
  • the solutions are allowed to incubate in the wells at 37 0 C for 15 minutes. After the incubation period, the wells of the MICROTITRETM plate are washed three times with saline, preferably by an automatic washing apparatus such as the Bio-Tek model EL- 402.
  • the MICROTITRETM plate is centrifuged at 450 x G for one minute. The plate is then examined for adherence or lack of adherence of the indicator RBCs to the erythrocyte cell monolayer ( Figure 2) .
  • a positive reaction is seen by adherence of the indicator red cells over the reaction surface.
  • a negative reaction forms a discreet button of indicator red cells at the bottom of the wells showing no adherence ( Figure 2) .
  • the biological fluid being tested has antibodies directed towards the erythrocyte cell monolayer, it binds to the erythrocyte monolayers.
  • the anti—IgG coated indicator RBCs correspondingly bind to the antibody thus bound when they are added to the wells. This gives the positive reaction.
  • the anti-IgG coated indicator RBCs will have no complimentary immunologically component to bind to and will collect at the bottom of the well as a discreet button.
  • Test Method 1 CAPTURE-S
  • Test Method 2 CAPTURE-FSL-SYPH3
  • Test method 1 +ve assay 20 0
  • Test Method 2 (CAPTURE-FSL-SYPH3) demonstrated improved sensitivity over Test Method 1 (CAPTURE-S) .
  • Test Method 2 (CAPTURE-FSL-SYPH3) provides the additional advantage that the introduced antigen (F) of the FSL construct is expressed against the background antigens of the naturally occurring RBCs that are modified to provide the kodecytes.
  • diacylglycerol 2-phosphate could be substituted for phosphatidate (diacylglycerol 3-phosphate) and that the absolute configuration of phosphatidate could be either R or S.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Immunology (AREA)
  • Molecular Biology (AREA)
  • Organic Chemistry (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Urology & Nephrology (AREA)
  • Hematology (AREA)
  • Biomedical Technology (AREA)
  • Biotechnology (AREA)
  • Medicinal Chemistry (AREA)
  • Microbiology (AREA)
  • Analytical Chemistry (AREA)
  • Physics & Mathematics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Wood Science & Technology (AREA)
  • Food Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • Pathology (AREA)
  • General Physics & Mathematics (AREA)
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Abstract

L'invention porte sur des méthodes de diagnostic d'infections par le Treponema palladium utilisant une construction peptide-espaceur-lipide dans laquelle l'espaceur lie par covalence le peptide au lipide. Le peptide présente la séquence AlaSerGlyAlaLysGluGluAlaGluLysLysAlaAlaGluGlnArgAlaLeuLeu. Le lipide est sélectionné parmi un glycérolipide diacylique ou dialkylique comprenant des glycérophospholipides. La méthode consiste: à mettre un échantillon de plasma ou de sérum d'un sujet en contact avec une suspension de cellules modifiée pour incorporer une construction peptide-lipide et former un mélange; à incuber le mélange pour permettre l'agglutination; et à déterminer le degré d'agglutination des cellules du mélange. Une construction particulière est présentée dans la figure 1.
PCT/NZ2010/000111 2009-06-12 2010-06-14 Essais de détection sérologique de la syphilis WO2010143983A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU2010259360A AU2010259360B2 (en) 2009-06-12 2010-06-14 Assays for serological detection of syphilis

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
NZ57768909 2009-06-12
NZ577689 2009-06-12

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WO2010143983A1 true WO2010143983A1 (fr) 2010-12-16

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20150064690A1 (en) * 2011-08-31 2015-03-05 Kode Biotech Limited Facile laboratory method for localising biomolecules to the surface of cells and viruses

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001264334A (ja) * 1999-10-07 2001-09-26 Sekisui Chem Co Ltd 梅毒トレポネーマ抗体測定試薬及びその製造方法
US20030229017A1 (en) * 2001-12-07 2003-12-11 Development Center For Biotechnology Solid phase method for synthesis peptide-spacer-lipid conjugates, conjugates synthesized thereby and targeted liposomes containing the same
WO2006138324A2 (fr) * 2005-06-14 2006-12-28 Baylor College Of Medicine Antigenes de treponema pallidum pour l'elaboration de vaccin et essais diagnostiques
WO2009035347A1 (fr) * 2007-09-11 2009-03-19 Cristina-Simona Weinberg Constructions peptidiques-lipidiques et leur utilisation pour des applications diagnostiques et thérapeutiques
WO2009048343A1 (fr) * 2007-10-12 2009-04-16 Nicolai Bovin Produits de construction lipidiques fonctionnels

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001264334A (ja) * 1999-10-07 2001-09-26 Sekisui Chem Co Ltd 梅毒トレポネーマ抗体測定試薬及びその製造方法
US20030229017A1 (en) * 2001-12-07 2003-12-11 Development Center For Biotechnology Solid phase method for synthesis peptide-spacer-lipid conjugates, conjugates synthesized thereby and targeted liposomes containing the same
WO2006138324A2 (fr) * 2005-06-14 2006-12-28 Baylor College Of Medicine Antigenes de treponema pallidum pour l'elaboration de vaccin et essais diagnostiques
WO2009035347A1 (fr) * 2007-09-11 2009-03-19 Cristina-Simona Weinberg Constructions peptidiques-lipidiques et leur utilisation pour des applications diagnostiques et thérapeutiques
WO2009048343A1 (fr) * 2007-10-12 2009-04-16 Nicolai Bovin Produits de construction lipidiques fonctionnels

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20150064690A1 (en) * 2011-08-31 2015-03-05 Kode Biotech Limited Facile laboratory method for localising biomolecules to the surface of cells and viruses
US9915653B2 (en) * 2011-08-31 2018-03-13 Nikolai Vladimirovich Bovin Facile laboratory method for localising biomolecules to the surface of cells and viruses
US10514382B2 (en) 2011-08-31 2019-12-24 Ludmila Baidakova Rodionov Facile laboratory method for localising biomolecules to the surface of cells and viruses

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AU2010259360A1 (en) 2012-02-02
AU2010259360B2 (en) 2015-01-22

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