Method of production of polyfunctional magnetic nanoparticles based on magnetosomes of bacterial origin

FIELD: biotechnology.

SUBSTANCE: as the present invention the method for production of polyfunctional magnetic nanoparticles based on bacterial magnetosomes and the hybrid protein MGG is provided, which enables to obtain magnetosomes binding immunoglobulins of the IgG class on the fragment Fc. The result is achieved in that in the lipid membrane of bacterial magnetosomes by ultrasonic treatment the hybrid protein MGG is integrated, which amino acid sequence comprises the transmembrane domain and the binding area of immunoglobulins.

EFFECT: obtaining polyfunctional magnetic sorbent bearing on the surface of magnetic nanoparticles of ligand, that enable to connect to the particles the immunoglobulins of IgG class.

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The invention relates to the field of biotechnology, in particular to biotechnology bacteria, and due to receipt of multifunctional magnetic nanoparticles.

As the present invention, a method for embedding the immunoglobulin-binding proteins in natural membrane of bacterial magnetic nanoparticles by treatment of a suspension of particles in a solution of the target protein by ultrasound.

The results of the implementation of the present invention can be used in the development of methods for magnetic immunoassay for the detection of target antigens and are modified magnetic particles can be used as a sorption agent for isolation of immunoglobulins.

There is a method of conducting magnetic immunoassay using particles of iron oxide Fe2O3where is the surface modification of particles by chemical cross-linking of the antigen with the surface of the particles with glutaric aldehyde. Patent RU (11) 2290641 (13) C1.

A method of obtaining modified magnetic nanoparticles of bacterial origin, in which the embedding target protein molecules in the membrane of the nanoparticles is carried out by genetic transformation of bacteria producing magnetic nanoparticles vector, which includes the gene encoding in trively protein. Embedding the desired protein into the membrane of magnetic nanoparticles is the result of natural biochemical processes inside living cells (U.S. Patent US 20100292495).

Also known is a method of obtaining modified magnetic nanoparticles of bacterial origin, in which the embedding target protein molecules in the membrane of the nanoparticles is carried out by expression of a hybrid protein MagA/target protein in cells magnetotacticum bacteria CA-1, what is this method similar to the previous (U.S. Patent US 5861285).

A method of obtaining modified magnetic nanoparticles of bacterial origin, which is conducted by chemical cross-linking of antibodies against the target protein (Bt-toxin of the bacterium Bacillus thuringiensis) with the bacterial membrane magnetosome bacteria by the method of carboxymethylate (EU patent CN 1024193 70 (A)).

The disadvantages of the above methods is either insufficient specificity of binding the target substance to the surface of magnetic particles (as is the case with chemical blending) or uncontrolled embedding level of the modifying agent in the membrane magnetosome (case of genetic modification).

The analysis of patent sources shows that despite the continuously increasing flow of information about how to use bacterial magnetic on what acustic (magnetism), there is an urgent need for a relatively simple and effective methods of surface modification of magnetism for the purpose of placement on the outer membrane of the desired target compounds. Obtained by such methods modified magnetosome can be used in the future for research in fundamental science and to solve applied problems - targeted drug delivery, magnetic resonance therapy of diseases, development of methods of magnetic immunoassay diagnostics and so on.

The objective of the proposed method is highly effective embedding of the immunoglobulin-binding proteins in the natural membrane magnetism that allows you to get polyfunctional (due to the possibility of further binding of the built-protein antibodies of different specificity) magnetic nanoparticles based on magnetism of bacterial origin. As the source of magnetism was selected bacterium Magnetospirillum strain SO-1, isolated from coastal sediments ragovka (Kislovodsk). This strain differs from the known cultivated magnetotacticum bacteria increased aerotolerant, high growth rate and sustainable products magnetism in a wide range of culture conditions.

Thus, the invention is a method of obtaining multifunctional magnetic nanoparticles based on magnetosome bacterial origin should:

a) to ensure the integration of the hybrid protein MGG [1] (SEQ ID No. 1) in the bacterial membrane magnetosome the result is ultrazvukovoy processing.

N-end of the hybrid protein (amino acid nos 1-124) contains the sequence of amino acids with hydrophobic properties, the corresponding protein Mam12 membrane magnetosome bacteria Magnetospirillum magnetotacticum MS-1, which provides a consolidation of protein molecules in the lipoprotein membrane bacterial nanoparticles. With the end (amino acid No. 130-284) is a tandemly repeated synthetic analogue of a fragment of the immunoglobulin-binding protein a of Staphylococcus aureus. N - and C-ends of the protein are linked glycine-serine hinge (amino acid No. 125-129)ensuring the independence of the folding of the two domains of the protein;

b) to ensure the binding of the antibody of class IgG for Fc-fragment

The implementation of the invention

Cell lines and culture medium for growth of cells

E. coli strain BL21 (DE3) (F-ompT hsdSB (rB-mB-) gal dcm (DE3)) (Novagene, USA), Magnetospirillum sp.SO-1.

Obtaining and study of the activity of the immunoglobulin-binding protein MGG

The expression of protein MGG held in the cells of E. coli strain BL21 (DE3), transformed with the expression vector pET23a(+)/mGG method autoinduction [2].

Purification of the hybrid protein MGG was performed using metallogenetic affinity chromatography (MOSSES) preparation of membrane fractions of proteins, which is suspended in buffer A (20 mm Tris-HCl, pH 8.0, 500 mm NaCl, 5% glycerol, 10 mm β-mercaptoethanol, 10 mm imidazole, 2 mm PMSF, 15% lauryl sarcosine), and incubated for one hour at room temperature. Solubilizing membrane fraction was applied onto the sorbent Ni-NTA agarose" (Invitrogen, USA), pre-balanced with buffer A. Then carried out the first washing buffer And at least 3 volumes of sorbent), and then buffer A: 20 mm Tris-HCl, pH 8.0, 1 M NaCl, 5% glycerol, 5 mm imidazole, 1% lauryl sarcosine (at least 3 volumes of sorbent). The elution of the target protein was buffer containing 20 mm Tris-HCl, pH 7.5, 130 mm NaCl, 5% glycerol, 500 mm imidazole, 0.5% lauryl sarcosine. The eluate were dialyzed in 20 mm Tris-HCl, pH 7.5 buffer containing 50 mm NaCl, 10% glycerol; 14.6 mm laurylsarcosine over night at +4°C. the Presence of getservletinfo sequence at the C-end of the hybrid proteins has allowed one to obtain highly purified preparation of proteins using MOSSES.

The binding ability of the modified protein antibodies were determined using ELISA. In the wells barbirolli 1 mg of human insulin over night at +4°C. Residual sorption blocked 1.5% solution of BSA in PBST buffer (137 mm NaCl, 2.7 mm KS1, 10 mm Na2HPO4, 1.8 mm KH2PO4, 0.01% NaN3, 0.05% Tween 20) for one hour. Next was added 100 μl (1 μg/ml) monoclonal mouse antibodies against human insulin (Imtek, Russia), and incubated for one hour at room temperature. The wells were washed 4 times with PBST buffer, and then applied with the specified dilutions hybrid of the first protein and incubated at room temperature for 1 h After the same washing for 1 h were incubated with 0.1 µg of mouse antibodies against his-tag tag (Imtek, Russia); system detection - peroxide/peroxidase horseradish, chromogenic substrate TMB (Sigma, USA). As a negative control used a polypeptide carrying the his-tag tag at the C-end.

The specificity of the interaction was determined by calculating the dissociation constant of the complex hybrid protein with the antibody according to [3]. To each well was applied at 1 µg of the hybrid protein. After blocking the surface of the wells was added to the rabbit antibodies to the Fc fragment of mouse immunoglobulin G conjugated with horseradish peroxidase at specified dilutions. To compare the level of nonspecific binding of the antibody protein MGG, a similar image was obtained hybrid protein MZZ, consisting of protein Mat 12 and the two domains Z (widely used in biotechnology synthetic analogues domain of protein A of S. Aureus). It is shown that proteins MGG and MZZ exhibit a high level of specificity of interaction with antibodies: Kaff(MGG)=1.59±0.12 nm Kaff(MZZ)=1.44±0.16 nm. Based on these results, the conclusion is made about the immunoglobulin-binding activity double G domain, not inferior to the previously known double Z domain.

From literature data [4] it is known that the B-domain of protein A of Staphylococcus aureus is able to communicate only with the Fc fragment of them is noglobulins IgG class.

Selection magnetosome from Magnetospirillum strain SO-1

Biomass Magnetospirillum strain SO-1 was obtained from 1.5 l of culture fluid by centrifugation at 10,000 rpm for 10 min. the Precipitated cells (4 g raw biomass) resuspendable in 20 ml of 20 mm HEPES buffer with pH=7.4 with the addition of EDTA (4 mm) and phenylmethylsulfonyl (0.1 mm) to prevent the destruction of membrane proteins by magnetosome cellular proteases. For more effective destruction of bacterial cells was carried out twice, the procedure of freezing and thawing, the resulting suspension. The final destruction of the cells was measured with an ultrasonic disintegrator Sonopuls UW2070 (Bandelin, Germany) with a frequency of 20 kHz for 10 minutes, the Suspension is destroyed cells was transferred into a clean test tube, and the magnetic fraction was collected on a magnetic stand Promega. To get rid of the destroyed remnants of the bacterial cells magnetic nanoparticles twice washed with 20 mm HEPES-buffer pH=7.4 with the addition of 200 mm NaCl, followed by ten-fold flush magnetosome 20 mm HEPES-buffer pH=7.4 magnetic stand Promega.

Check purity and physicochemical properties of bacterial magnetosome

The purity of the drug magnetism and their physicochemical properties were characterized using the methods of atomic force microscopy (AFM) (INTEGRA prima, NT-MDT, Russia) (FIGURE 1). It is established that magnetos is s, isolated from Magnetospirillum strain SO-1, have the same shape, size magnetic crystals ranged from 45 to 60 nm. Data microscopy indicate the presence of intact lipoprotein membrane. The elemental composition is determined using the method of energy dispersive x-ray spectroscopy. It is shown that the crystals magnetosome consist of magnetite (Fe3O4). Thus, the developed method allows to isolate the magnetic nanoparticles of bacteria Magneto spirillum sp.SO-1 with intact membranes required for subsequent modification by magnetism.

Immobilization of protein MGG on the surface of magnetism. The obtained protein MGG immobilizer on the membrane magnetosome using ultrasonic treatment. Embedding of the protein was carried out in the presence of 10 mm of lauroylsarcosinate sodium and 100 mm NaCl. For modification of bacterial nanoparticles, 1 ml (10 mg/ml) drug magnetosome in 20 mm HEPES-buffer pH=7.4 was mixed with 1 ml (5 mg/ml) protein MGG, with 100 μl NaCl and 10 μl of lauroylsarcosinate sodium. Then there was the sound of the mixture using an ultrasonic disintegrator Sonopuls UW2070 (Bandelin, Germany) with a frequency of 10 kHz (0.5 s/0.5 s) for 1 min Polyfunctional bacterial magnetosome collected on a magnetic stand and washed three times 20 mm HEPES-buffer pH=7.4. Embedding the hybrid protein was checked by AFM method (INTEGRA prima, NT-MDT, Rho is this) (FIG. 2) the Functional activity of the modified method proposed by magnetism was examined using magnetic immunoassay. For this purpose, 10 μl (1 MT/ml) of modified bacterial magnetosome was added to 1 ml of mouse antibodies against the Fc fragment of human immunoglobulin conjugated to horseradish peroxidase, with the specified dilutions and incubated for 30 min at room temperature. Then magnetosome washed 5 times on the magnetic stand 1 ml of 20 mm HEPES-buffer, pH=7.4 to get rid of unbound antibodies. The level of binding is determined spectrophotometrically by a color reaction of peroxidase with tetramethylbenzidine (FIGURE 3).

An example of implementation of the proposed method

10 μl (1 mg/ml) polyfunctional bacterial magnetosome was added to 1 ml of mouse antibodies against human insulin with the specified dilutions and incubated for 30 min at room temperature. With the aim of getting rid of unbound antibody magnetosome washed 5 times on the magnetic stand 1 ml of 20 mm HEPES-buffer, pH=7.4. After which was added 1 ml (1 mg/ml) of rabbit antibodies against the Fc fragment of mouse immunoglobulin conjugated with horseradish peroxidase and incubated for 30 minutes After the same washing unbound antibody was added to 100 μl of chromogenic substrate tetramethylbenzidine, the reaction was stopped by 20 ál of 1 M HCl Optical density of the solution was measured on a spectrophotometer at a wavelength of 405 nm (FIG.No. 4). The data obtained indicate that the multifunctional bacterial magnetosome can be used as a magnetic sorbent for conducting ELISA high sensitivity.

Literature

1. Dscruggs, Mavzuna, Assersion, Bab. Obtaining and study of the activity of the modified proteins of the membrane magnetosome. // Applied biochemistry and Microbiology.// In printing.

2. Studier F.W. // Protein Expression and Purification. 2005. No. 41. P.207-234.

3. Loomans E.M.G., Roelen A.J.M., Van Damme H.S., Bloemers H.P.J., Gribau T.C.J., Schielen W.J.C. // J. Immunol. Methods. 1995. No. 184. P.207-217.

4. A.Karimi, A., Matsumura, M., Wright, P.E. & Dyson, H.J. //Characterization of monomeric and dimeric In the domain of Staphyloccocal protein A.// J. Peptide Res., 1999, No. 54, P.344±352.

Sequence listing

SEQ ID No. 1, amino acid sequence of the protein MGG

MPFHLAPYLAKSVPGVGVLGALVGGAAALAKNVRLLKEKRITNTEAAIDTGKETVGAGLATALSAVAATAVGGGLVVSLGTALVAGVAAKYAWDRGVDLVEKELNRGKAANGASDEDILRDELAGSGSGDNKFNKGQQNAFYEILHLPNLNEEQRNGLIQSLKDDPSQSANLLAEAKKLNDAQAPKGSGSGDNKFNKGQQNAFYEILHLPNLNEEQRNGLIQSLKDDPSQSANLLAEAKKLNDAQAPKHHHHHH

The method of obtaining multifunctional magnetic nanoparticles based on magnetosome obtained from strain SO-1 bacteria Magnetospirillum, including immobilization of the hybrid protein MGG, having amino acid sequence SEQ ID No. 1 (MPFHLAPYLAKSVPGVGVLGALVGGAAALAKNVRLLKEKRITNTEAAIDTGKETVGAGLATALSAVAATAVGGGLVVSLGTALVAGVAAKYAWDRGVDLVEKELNRGKAANGASDEDILRDELAGSGSGDNKFNKGQQNAFYEILHLPNLNEEQRNGLIQSLKDDPSQSANLLAEAKKLNDAQAPKGSGSGDNKFNKGQQNAFYEILHLPNLNEEQRNGLIQSLKDDPSQSANLLAEAKKLNDAQAPKHHHHHH), in the presence of 10 mm of lauroylsarcosinate sodium and 100 mm NaCl on the surface the bacterial magnetosome by ultrasonic impact frequency of 10 kHz (0.5 s/0.5 s) within 1 min



 

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