Purification / disinfection apparatus and method

Abstract

This invention provides an apparatus for the control and removal of viruses, microorganisms, and pathogens. The provided apparatus includes a carrier material and a binder, the carrier material comprising a carbohydrate-based polymer. The binder is linked to the carrier material via one or more covalent bonds, and the binder can bind to a target, the target being one or more of biotoxins, viruses, microorganisms, and microbial components. The invention also provides a method for removing biotoxins, viruses, microorganisms, and / or microbial components using such an apparatus, and a method for manufacturing said apparatus, comprising providing a carrier material comprising a carbohydrate-based polymer; treating the carrier with an oxidant to generate acid and / or aldehyde groups; and contacting the treated carrier with a binder comprising one or more lectins, glycoproteins, and glycoconjugates, such that the binder is linked to the carbohydrate-based polymer via one or more covalent bonds.

Description

Technical Field

[0001] This invention belongs to the field of virus, microorganism and pathogen control and removal. Background Technology

[0002] A key issue in modern society is how to prevent the spread of viruses, bacteria, and other microorganisms and their components, especially when these substances are harmful to human or other organisms. Since the spread of these substances can typically occur through survival on surfaces and transfer between surfaces, or through air or liquids, it is necessary to remove viruses, microorganisms, and microbial components from these surfaces.

[0003] Of course, the removal of pathogens is especially necessary, but for various purposes, such as maintaining a sterile environment or avoiding contamination in scientific or industrial processes, the collection or removal of harmless microorganisms is often also desirable.

[0004] Most methods designed to remove microbial or viral loads from surfaces attempt to denature or otherwise destroy the target. For example, alcohols and other preservatives, strong chemical disinfectants (often oxidants such as bleach, although reducing agents can be used), antibiotics, extreme heat and radiation, such as shortwave ultraviolet light or non-thermal (cold) plasma, are commonly used to destroy or denature viruses and microorganisms.

[0005] This approach has several major drawbacks, primarily the potential for varying effectiveness because microorganisms can develop or become resistant to almost all eradication methods. Some microorganisms are able to produce spores that are highly resistant to heat, chemicals, drugs, and ultraviolet radiation, thus proving difficult to destroy. Many viruses are inherently resistant to conventional methods of destruction, immune to antimicrobial agents such as antibiotics, and lack cellular processes that can be disrupted. The biotoxins and components of microorganisms or viruses may also be resistant to mechanisms designed to kill living organisms, making them difficult to eradicate as well.

[0006] Furthermore, the methods used for disinfection may themselves be harmful to users. This is especially true for strong chemical disinfectants, while other methods, such as antibiotics, can cause allergic reactions, and the use of ultraviolet light can damage the skin and may be carcinogenic. In many cases, applying these methods may also be impractical; for example, heating surfaces to high temperatures for disinfection is not always feasible.

[0007] Even if the target microorganism or virus is destroyed, harmful substances may remain, such as protein-based or non-protein-based bacterial toxins, like lipopolysaccharides (endotoxins), or enterotoxins, such as those produced by Vibrio cholerae. Other biotoxins, such as those produced by plants and animals, also present similar problems.

[0008] Perhaps most importantly, chemical and antibiotic resistance can evolve in microorganisms and be retained in their offspring, even at the level of gene transfer. Therefore, the use of strong chemical disinfectants and hygiene products is an additional risk factor that can promote mutations and inefficient eradication programs. Many important antimicrobial agents, including the most potent antibiotics and chemicals, have become ineffective, leading to increased human (and animal) mortality, global pandemic threats, and increased healthcare costs. This is equally concerning with biothreat agents, as they could cause widespread fear and harm to human and animal lives without proper control measures.

[0009] Therefore, there is a need for methods and apparatus that can effectively remove biotoxins, viruses, microorganisms and microbial components (including components that may be resistant to conventional removal or destruction methods) and effectively retain these contaminants for subsequent analysis and / or disposal.

[0010] Existing devices designed to remove target biotoxins, viruses, microorganisms, and microbial components by retaining them within a material or carrier are ineffective at retaining these targets because the interactions between the biotoxins, viruses, microorganisms, and microbial components and the material or carrier are often not strong enough. For example, the removed target may simply be adsorbed onto or into the material or carrier, for example, through hydrogen bonds or similar interactions. These methods result in inefficient target absorption and the release of temporarily bound targets when the material or carrier encounters another surface.

[0011] The present invention provides an apparatus and method for removing biotoxins, viruses, microorganisms and microbial components from contaminated surfaces and stably retaining them within a carrier material. Summary of the Invention

[0012] In a first aspect, the present invention provides an apparatus (e.g., adapted to remove biotoxins, viruses, microorganisms, and / or microbial components from a surface and / or from a gas or liquid) comprising a carrier material containing at least one carbohydrate-based polymer and a binder. The binder is linked to the carrier material via one or more covalent bonds and can bind to a target, said target being one or more of biotoxins, viruses, microorganisms, and microbial components.

[0013] The carrier material may include cellulose as a carbohydrate-based polymer, and may include one or more of cotton and paper. When the carrier material includes cellulose, the binder may be linked to the cellulose via one or more covalent bonds.

[0014] The device may include a fluid in which a carrier material is dissolved, suspended, dispersed, emulsified, or otherwise carried.

[0015] The binding agent may include one or more of the following: antithrombotic agents, anti-inflammatory agents, antibodies, antigens, adhesins, immunoglobulins, enzymes, hormones, neurotransmitters, cytokines, proteins, globular proteins, cell adhesion proteins, peptides, cell adhesion peptides, proteoglycans, toxins, polysaccharides, carbohydrates, fatty acids, drugs, vitamins, DNA fragments, RNA fragments, nucleic acids, dyes, and ligands. In some embodiments, the binding agent includes one or more of the following: lectins, glycoproteins, oligosaccharides, and glycoconjugates.

[0016] The binder may include lectins, which may be one or more of the following: AIA / Jacalin, RPbAI, AAL, ABL, ACA, AMA, BPA, CAA, Calsepa, CCA, ConA, CPA, DBA, DSA, ECA, EEA, GHA, GNA, GSL-I-B4, GSL-II, HHA, HPA, Lch-A, Lch-B, LEL, LTA, MAA, MOA, MPA, NPA, PA-I, PCA, PHA-E, PHA-L, PNA, PSA, RCA-I / 120, SBA, SJA, SNA-I, SNA-II, STA, UEA-I, VRA, VVA-B4, WFA, and WGA. Suitablely, the lectin can be one or more of VRA, Lch-B, EEA, PA-I, PNA, CAA, GSL-I-B4, AMA, RCA-I / 120, and GNA.

[0017] In some embodiments, the binding agent comprises a glycoprotein, which may be one or more of the following: Tamm-Horsfall protein, fetoglobulin, asialofetuin, convertase, fibrinogen, α-1-antitrypsin, α-crystallin, ceruloplasmin, α-1-acidic glycoprotein, ribonuclease B, transferrin, β-lactoglobulin, C-lactalbumin, albumin, β-casein, C-casein, K-casein, lactoferrin, ovalbumin, ovomucoid, ovotransferrin, and derived glycomacropeptide. Typically, the glycoprotein may be one or more of the following: fetoglobulin, asialofetuin, and α-crystallin.

[0018] In some embodiments, the binder is a glycoconjugate or a novel glycoconjugate. The glycoconjugate or novel glycoconjugate can be A-BSA blood type, B-HSA blood type, Fuc-α-4AP-BSA, Fuc-β-4AP-BSA, 2... Fucosyl lactose-BSA, difucosyl-p-lact-N-hexasaccharide-APD-HSA (Lea / Lex), tri-fucosyl-Ley-heptasaccharide-APE-HSA, monofucosyl, monosialic acid-N-neohexose-APD-HSA, Gal-β-4AP-BSA, Galα1,3Gal-BSA, Gal-α-1,3Galb1, Gal-β-1,4Gal-BSA, Gal-α-1,2Gal-BSA, 4GlcNAc-HSA, Gal-α-PITC-BSA, Gal-β-ITC-BSA, Glc-β -4AP-BSA, Glc-β-ITC-BSA, GlcNAc-BSA, Globotriose-HSA, Globo-N-tetraose-APD-HSA, Globotriose-APD-HSA, GM1-pentasaccharide -APD-HSA, Asialo-GM1-tetrasaccharide-APD-HSA, Globo-N-tetraose-APD-HSA, Globotriose-APD-HSA, H-type II-APE-BSA, H-type 2-APE-HSA, Man-α-1,3(Man-α-1,6), Man-BSA, Man-α-ITC-BSA, Man-b-4AP-BSA, LacNAc-BSA, LacNAc-α-4AP-BSA, LacNAc-β-4AP-BSA, Lac-β-4AP-BSA, Lacto-N-tetraose-APD-HSA, Lacto-N-fucopentaose I-BSA (Lacto-N-fucopentaose I-BSA), lacto-N-neotetraose-APD-HSA, lactose-N-fucopentose II-BSA, lacto-N-fucopentose III-BSA, Lacto-N-difucohexaose I-BSA (Lacto-N-difucohexaose I-BSA), Lewis a-BSA, Lewis x-BSA, Lewis y-tetraose-APE-HSA (Lewis y-tetrasaccharide-APE-HSA), LNDI-BSA / Lewis b-BSA, Di-Lex-APE-BSA, Di-Lewisx-APE-HSA, Tri-Lex-APE-HSA, L-rhamnose-Sp14-BSA, 3'-sialyl-lactose-APD-HSA, 3'-sialyl-3-fucosyllactose-BSA, 6'-sialyl-lactose-APD-HSA, Xyl-α-4AP-BSA, Xyl-β-4AP-BSA, 3'-sialyl Lewis x-BSA, 3'-sialyl Lewis a-BSA It contains one or more of the following: Lewisa-BSA, 6-Sulfo Lewis x-BSA, 6-Sulfo Lewis a-BSA, 3-Sulfo Lewis a-BSA, 3-Sulfo Lewis x-BSA, sialyl-LNF V-APD-HSA, and sialyl-LNnT-penta-APD-HSA.

[0019] When the binder is a glycoconjugate, a neoglycoconjugate, or a glycoprotein, it may have terminal sugar residues comprising one or more of mannose, N-acetylglucosamine, N-acetylgalactosamine, N-acetylneuraminic acid and N-hydroxyacetylneuraminic acid (sialic acid), galactose, glucose, and fucose moieties.

[0020] The carrier material may also include antimicrobial substances, which may be one or more of preservatives, antibiotics, and detergents. Antimicrobial substances may be silver, copper, or EDTA.

[0021] In any implementation, the carrier material of the device may be in the form of cloth, wiping material, wound dressing, swab, filter, pad, blanket, mat, mask, or coating.

[0022] In a second aspect, the present invention provides a method for removing biotoxins, viruses, microorganisms and / or microbial components from a surface, the method comprising providing an apparatus according to any embodiment described herein and bringing the surface into contact with the apparatus.

[0023] In a third aspect, the present invention provides a method for removing biotoxins, viruses, microorganisms and / or microbial components from a gas or liquid, the method comprising providing an apparatus according to any embodiment described herein and passing the gas or liquid through the apparatus.

[0024] In any of the above-described embodiments, the binder may bind to the biotoxin, virus, microorganism, and / or microbial component to be removed. The virus, microorganism, and / or microbial component to be removed may be spores.

[0025] In another aspect, the present invention provides a method of manufacturing an apparatus, the method comprising providing a carrier material comprising at least one carbohydrate-based polymer, treating the carrier with an oxidant to generate acid and / or aldehyde groups, and contacting the treated carrier with a binder comprising one or more of lectins, glycoproteins, and glycoconjugates, such that the binder is linked to the carbohydrate-based polymer via one or more covalent bonds. The oxidant may be periodate, preferably sodium periodate. The oxidant may be selected from 2,2,6,6-tetramethylpiperidin-1-oxy (TEMPO), sodium nitrate, or sodium nitrate in phosphoric acid; toluenesulfonyl chloride, an activator in the presence of an organic solvent and a base; and combinations thereof.

[0026] Further possible features discussed in conjunction with embodiments of the apparatus according to the invention are considered equally applicable to apparatus manufactured by the above-described process.

[0027] In one particular aspect, an apparatus is provided comprising: a carrier material comprising cellulose; and a binding agent comprising a glycoprotein selected from one or more of the following: Tamm-Horsfall protein, fetoglobulin, asialofetuin, convertase, fibrinogen, α-1-antitrypsin, α-crystallin, ceruloplasmin, α-1-acid glycoprotein, ribonuclease B, transferrin, β-lactoglobulin, C-lactalbumin, albumin, β-casein, C-casein, K-casein, lactoferrin, ovalbumin, ovomucoid, ovotransferrin, and derived glycomacropeptide. The binding agent is linked to the cellulose via one or more covalent bonds, and the binding agent is capable of binding to a target, which is one or more of a biotoxin, virus, microorganism, and microbial components. Attached Figure Description

[0028] The invention will be further described with reference to the accompanying drawings, in which:

[0029] Figures 1A to 1C The following are illustrated: removal of Tula Francisella bacteria from various surfaces using apparatus according to various embodiments of the present invention. Francisella tularensis The results of efficacy tests.

[0030] Figures 2A to 2D The following are illustrated: removal of botulinum toxin from various surfaces using apparatus according to various embodiments of the present invention. Clostridium botulinum The results of efficacy tests.

[0031] Figure 3A and Figure 3B The invention illustrates the removal of Bacillus anthracis in cellular (3A) or spore (3B) form from various surfaces using devices according to various embodiments of the invention. Bacillus anthracis The results of efficacy tests.

[0032] Figures 4A to 4C Results of efficacy tests for removing influenza viruses from various surfaces using devices according to various embodiments of the present invention are shown.

[0033] Figure 5A and Figure 5B The following are illustrated: removal of EHEC (Escherichia coli) from various surfaces using apparatus according to various embodiments of the present invention. Escherichia coli , E. coli O157:H7 and Enterobacter cloacae ( Enterobacter cloacae The results of efficacy tests.

[0034] Figure 6 The following diagram illustrates the removal of Propionibacterium acnes from plastic surfaces using a device according to various embodiments of the invention. Propionibacterium acnesThe results of efficacy tests.

[0035] Figure 7 The removal of Candida albicans from plastic surfaces at various pH levels using a device according to an embodiment of the present invention is illustrated. Candida albicans The results of efficacy tests.

[0036] Figure 8 A method for characterizing skin models inoculated with various microorganisms is shown using a testing apparatus according to an embodiment of the present invention.

[0037] Figure 9A and Figure 9B The results of an efficacy test for removing Escherichia coli from pig skin slices using the apparatus according to an embodiment of the present invention are shown.

[0038] Figure 10 The results of an efficacy test for removing Candida albicans from pig skin slices using the apparatus according to an embodiment of the present invention are shown.

[0039] Figure 11 The removal of Aspergillus fumigatus from pig skin slices using an apparatus according to an embodiment of the invention is shown. Aspergillus fumigatus The efficacy test results of ). Detailed Implementation

[0040] All references cited herein are incorporated herein by reference in their entirety. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains.

[0041] Before further elaborating on the present invention, several definitions are provided to help understand the present invention.

[0042] As used herein, the term "target" refers to an article that needs to be removed from a surface or otherwise delivered or secured into / on the device according to the invention. Typically, a target is a biotoxin, virus, microorganism, or microbial component, and may also be a pathogen. In some cases, a target may be an allergen or a microscopic component produced by non-microbial life, such as plant pollen, fungal spores, dust mite feces and other components, potential allergens from food such as nuts and shellfish, animal or plant venoms or toxins, and animal products (such as dander).

[0043] As used herein, the term “microorganism” refers to microorganisms, particularly bacteria, fungi, so-called “protozoa”, or any other prokaryotic or eukaryotic organism with microscopic characteristics.

[0044] As used herein, the terms “microbial component,” “microbial product,” or “microbial substance” refer to the product of microorganisms that are desired to be removed from a surface or otherwise inhaled or immobilized within / on the device according to the invention. Microbial components can be toxins, i.e., substances harmful to the body, such as protein-based or non-protein-based bacterial toxins, such as lipopolysaccharides (endotoxins), or enterotoxins, such as enterotoxins produced by Vibrio cholerae.

[0045] As used herein, the term "toxin" or "biotoxin" refers to a substance that is harmful to the body and is derived from biological sources. As mentioned above, biotoxins can be produced by microorganisms or derived from other sources, such as plants or animals.

[0046] As used in this article, the term "pathogen" refers to a virus or microorganism that can cause disease.

[0047] As used herein, the term "carbohydrate-based polymer" refers to a polymer that comprises monosaccharide units (simple sugar molecules) as the main or sole component of its repeating polymeric units. Carbohydrate-based polymers include, but are not limited to, polysaccharides, dextran, starch, glycogen, fungal β-glucan, chitin, chitosan, cellulose and cellulose derivatives (e.g., cellulose acetate, celluloid, and nitrocellulose), kelp polysaccharides, golden kelp polysaccharides, xylan, arabinoxylan, mannan, fucoidan, and galactomannan. While many such polymers consist solely of monosaccharide units and their derivatives, copolymers containing monosaccharides and other units exist, such as glycopeptide hybrid copolymers. Furthermore, certain carbohydrate-based polymers, particularly those that, in a non-fibrous form, can be dissolved, suspended, dispersed, emulsified, or carried in fluid carriers such as liquids or gases via spray, sol aerosol, emulsion, or other means.

[0048] As used herein, the term "polysaccharide" refers to a carbohydrate-based polymer composed of chains of monosaccharide units (simple sugar molecules), where the chains can be linear or branched. Polysaccharides are commonly used to store sugars for later use, such as starch, glycogen, and kelp polysaccharides. Other polysaccharides can be used for structural purposes, including cellulose, fungal β-glucan, chitin, pectin, xylan, arabinoxylan, etc. Bacteria often produce and secrete polysaccharides, for example, to help adhere to surfaces or evade the host's immune system.

[0049] As used herein, the term "cellulose" refers to a biogenic carbohydrate polymer composed of β(1→4)-linked D-glucose unit chains. Cellulose is produced by green plants used for cell walls, as well as by other species including several algae and some bacteria. Micronized cellulose or nanocellulose can be non-fibrous and therefore can be dissolved, suspended, dispersed, emulsified, or carried in fluid carriers such as liquids or gases in the form of sprays, sol aerosols, emulsions, or other methods.

[0050] As used herein, the term "binding agent" refers to a biomolecule capable of binding to a biotoxin, virus, microorganism, or microbial component. Such molecules may include one or more of the following: antithrombotic agents, anti-inflammatory agents, antibodies, antigens, adhesins, immunoglobulins, enzymes, hormones, neurotransmitters, cytokines, proteins, globular proteins, cell attachment proteins, peptides, cell attachment peptides, proteoglycans, toxins, polysaccharides, carbohydrates, fatty acids, drugs, vitamins, DNA fragments, RNA fragments, nucleic acids, dyes, and ligands. Typically, the binding agents discussed herein are one or more of the following: glycoproteins, oligosaccharides, lectins, glycoconjugates, and their derivatives.

[0051] As used herein, the term "glycoprotein" refers to a protein having one or more oligosaccharide groups or glycans attached to it. Many secretory proteins are "glycosylated" in this way, and transmembrane proteins with extracellular domains typically have glycosyl groups attached to these domains.

[0052] As used herein, the term "glycoconjugate" refers to a protein or lipid having one or more glycan oligosaccharide groups attached thereto. Examples include glycoproteins, glycolipids, glycosphingolipids, proteoglycans, and glycosaminoglycans of natural or synthetic origin. "Novel glycoconjugate," or NGC, refers to an artificial or synthetic glycoconjugate, particularly glycoproteins and glycolipids, in which the protein or lipid backbone is chemically conjugated to one or more sugar residues. In most cases, proteins such as bovine serum albumin (BSA) and human serum albumin (HSA) are used to prepare novel glycoconjugates.

[0053] As used herein, the term "lectin" refers to a carbohydrate-binding protein (the terms carbohydrate-binding protein or CBP are used interchangeably). Lectins are specific to carbohydrate moieties, such as those found on glycoproteins, glycolipids, or oligosaccharides. Some lectins are also called "agglutinins" because they are able to agglutinate the particles they bind to. However, the term lectin can be applied to any substance that allows such agglutination, such as antibodies.

[0054] As used herein, the term "adhesin" refers to cell surface components involved in cell-to-cell or cell-to-surface adhesion. These are common in pathogenic, parasitic, or symbiotic microorganisms because they are used to adhere to host surfaces.

[0055] As used herein, the term "preservative" refers to a chemical substance that has antimicrobial properties, particularly by killing, denaturing, or destroying microorganisms, or preventing their growth or reproduction. Generally, preservatives are safe for use on skin or living tissue (including the mouth), but are typically not used in the body for efficacy or safety reasons. Some, but not all, preservatives can effectively denature or destroy viruses. Many types of preservatives exist, including alcohols (such as phenol), low-concentration disinfectant chemicals (such as bleach or peroxides), iodine, and certain specific chemicals (such as chlorhexidine gluconate and quaternary ammonium compounds).

[0056] As used in this article, the term "antibiotic" refers to a chemical substance that has antimicrobial activity and is used or can be used in the body. These substances typically interfere with bacterial processes, causing microbial cell death or lysis, but are generally ineffective against viruses or bacterial products. Antibiotics are known to come in many types, such as penicillins, cephalosporins, tetracyclines, and salinomycins.

[0057] This invention describes apparatus and methods related to the collection, purification / sterilization, preservation, and delivery of biotoxins, viruses, microorganisms, and microbial-derived components (proteins, peptides, and carbohydrates) for downstream diagnostic and forensic applications. This method targets the natural binding sites of viruses, microorganisms, and / or their components or biotoxins, and provides a non-toxic, environmentally friendly alternative for the biodecontamination of physical surfaces and for the biodecontamination of human and animal skin and mucous membrane epithelial surfaces. The method is designed to have broad specificity, i.e., to be used for multiple purposes in multiple forms against a variety of pathogens.

[0058] The interaction between cell surface proteins and carbohydrates is essential for cell-to-cell adhesion. This also applies to the adhesion of certain biotoxins, viruses, microorganisms, and microbial-derived proteins to other surfaces, such as the cells of host organisms.

[0059] The mechanisms by which microorganisms and viruses bind to cells, particularly commensal, symbiotic, or parasitic microorganisms, are bound to host cells, is a particularly important area of ​​evolution. For example, host-bacterial interactions can be mediated by bacterial adhesins and their homoglycan receptor epitopes on the surface of host cells. Most adhesins on Gram-negative and Gram-positive bacteria recognize suitable hosts through glycan markers on the surface of the host organism's epithelial cells (Kline et al., Cell Host and Microbe, 2009). Table 1 lists exemplary bacterial species and their respective adhesins, target ligands, and tissues. Especially in the case of pathogens, the interaction between pathogen surface markers and host surface markers is crucial for strong adhesion to the host, immune system evasion, and (in the case of intracellular pathogens and toxins) entry into the cell. In fact, the ability of a particular bacterium to specifically adhere to a host cell (often by possessing specific surface proteins or other molecules) can represent virulence factors, thus distinguishing pathogenic and non-pathogenic strains. In nature, pathogens are constantly bound to, retained, and removed from the surface of human and animal cells before they can multiply or enter cells to cause infection.

[0060] Table 1

[0061] Utilizing a similar principle to carbohydrate-protein binding technology, current devices achieve a unique approach by leveraging natural and modified protein and carbohydrate epitopes chemically linked to a carrier in various forms. These devices provide a variety of "hooks" capable of binding to biotoxins, viruses, microorganisms, and / or their components, competing with host attachment surfaces to effectively remove or capture these targets.

[0062] Therefore, in order to remove microorganisms and proteins (bacteria, viruses, bacteriophage particles, fungi, and proteins) of microbial origin, carbohydrates, proteins, and protein fragments immobilized on physical materials can be used to collect samples of biotoxins, viruses, microorganisms, and / or their components, and to reduce the microbial load on surfaces, purify / disinfect surfaces, and preserve samples collected on the device for diagnostic and forensic purposes.

[0063] carrier material

[0064] The carrier material provides a surface for the binder to which it is to be attached, and a matrix therein to immobilize viruses, microorganisms, microbial-derived components, and / or biotoxins. Suitablely, the carrier material is capable of forming covalent bonds with the binder, enabling the formation of a strong and appropriately irreversible connection.

[0065] Typically, the carrier can comprise a carbohydrate-based polymer, preferably a polysaccharide such as starch, glycogen, chitin, cellulose, chitosan, pectin, fungal β-glucan, xylan, or arabinoxylan. The carrier may suitably contain cellulose. For example, the carrier can comprise cellulose, hemicellulose, or lignocellulose. The carrier itself may contain cellulose, for example, plant-derived materials such as paper, cotton, viscose fiber, or flax, or the material may be blended or coated with cellulose from another source. The carrier may also comprise a mixture of materials, such as a mixture of cellulose-containing materials and synthetic materials, such as a 50% mixture of cotton and polyester. Cellulose can also be produced by microorganisms such as bacteria. In particular, *Acetobacter* spp. (…) Acetobacter ), Octococcus spp. Sarcina ventriculi ) and Agrobacterium spp. Agrobacterium Bacteria have been used to produce bacterial cellulose.

[0066] Non-fibrous cellulose materials and carbohydrate-based polymers can be used as carriers. In particular, micronized cellulose and nanocellulose can be used in this way as non-fibrous cellulose. Such non-fibrous cellulose or carbohydrate-based polymers can be dissolved, suspended, dispersed, emulsified, or otherwise supported in fluid carriers such as liquids or gases. Therefore, when coupled with the binders described herein, such formulations can be applied to, for example, receptor materials in a non-solid form (such as a spray or paint).

[0067] This non-solid form of the carbohydrate-based polymer linked to the binder allows for a range of applications that would otherwise be impossible. For example, this suspended or soluble form of the product / device can be sprayed or otherwise applied to a recipient material, such as textiles, to impart protective qualities to the material depending on the characteristics of the applied product. After use, the recipient material can be washed or treated, for example, with a detergent or under low pH conditions, to remove the previously used product. The recipient material can then be retreated with fresh product to restore protective qualities before the next use or exposure. This method can be used, for example, to treat personal protective equipment such as face masks to impart protective qualities against one or more targets—biotoxins, viruses, microorganisms, and / or microbial components, as appropriate for specific applications.

[0068] Other potential applications of the non-solid form of carbohydrate-based polymers linked to binders include their use as cleaning compositions that can be sprayed or otherwise applied to the recipient material to be cleaned, and then removed along with any target biotoxins, viruses, microorganisms, and / or microbial components bound to them. Specific applications of this approach include cleaning large shipping containers, transportation hubs, and hospitals, as well as sterilizing aseptic equipment, such as in hospital or space environments.

[0069] More generally, for all considered forms where it is desired to permanently kill, denature, or otherwise destroy biotoxins, viruses, microorganisms, and / or microbial components inhaled by the device of the present invention, the carrier or device may further include an agent suitable for performing this operation. For example, the carrier may be impregnated or mixed with antimicrobial or antiviral chemicals such as antibiotics, preservatives, bleaching agents (possibly including hypochlorites, peroxides, and percarbonates), and other materials with inherent antimicrobial properties (such as silver or copper), other suitable metal ions, and metal chelating agents (such as EDTA), which have been shown to have antimicrobial efficacy (Finnegan and Percival, Wound Healing Society, 2014). Other possibilities include benzoic acid, benzalkonium chloride, and other quaternary ammonium cations. Different other substances may be selected depending on the proposed use of the device; for example, if the device is intended for use on the skin, a bactericide safe for that purpose may be selected. Stabilizers and / or preservatives may also be used, examples of which are known in the art.

[0070] In some cases, it may be necessary to retain the target biotoxin, virus, microorganism, and / or microbial components for subsequent analysis for research, diagnostic, or forensic purposes. In such cases, the vector may be substantially free of antimicrobial substances and may even be treated to increase the likelihood of intact survival of the target biotoxin, virus, microorganism, and / or microbial components for subsequent analysis, for example, by including buffers or other solutions, or specific pH levels, to support the immobilized target. Buffers or other solutions may also be included to aid in the binding of the binder to the desired target, as most interactions depend on the aqueous environment, specific pH levels, etc.

[0071] It is envisioned that various forms of carriers be prepared. For example, carrier materials can be prepared into wipes, cloths, wound dressings, filters, pads, coatings, blankets, mats, masks, and other articles. In particular, the use of wiping forms similar to paper towels, towels, or napkins is considered, as this provides a convenient form for wiping surfaces to be cleaned and for subsequent treatment. The devices according to the invention are also contemplated for use in removing target biotoxins, viruses, microorganisms, and / or microbial components from gases or liquids, such as removing airborne or atomized viral particles from the air. In this case, the carrier is designed to allow the gas or liquid to pass through so that the target can be removed. As mentioned above, certain carrier materials are also contemplated to be coupled with binders and dissolved, suspended, dispersed, emulsified, or otherwise carried in fluids; thus, fluids containing these carrier materials are examples of devices according to the invention.

[0072] It may also be desirable for the device of the present invention to be adapted for general cleaning on living or non-living surfaces such as skin. Therefore, the carrier is contemplated to contain other components suitable for the intended use, such as cleansers, moisturizers, deodorants, or chemicals for makeup removal (e.g., when used for skin cleansing), and / or detergents, fragrances, or cleansers for removing dust, dirt, metal rust, etc., from non-living surfaces. In this way, the device described herein can be used for therapeutic purposes, such as removing or killing bacteria from physical surfaces and from the skin (e.g., treating acne, diaper rash, and other skin conditions). In non-therapeutic uses, such as cosmetic uses, the device can be used for cleansing or moisturizing skin, baby care, hand washing, makeup removal, or applying deodorants.

[0073] Incontinence pads that incorporate or include the device according to the invention may also be considered, and the construction may be selected to provide protection against infectious agents that promote urethral diseases.

[0074] Pads and / or wipes designed for breastfeeding and / or nipple soothing are also under consideration, and can be designed to provide effective protection against infectious agents that cause mastitis.

[0075] binder

[0076] A binder capable of binding to a target biotoxin, virus, microorganism, and / or microbial component is attached to a carrier material. Any bio-derived molecule capable of binding to a biotoxin, virus, microorganism, or microbial component can be used in the device of the present invention. Such molecules may include one or more of the following: antithrombotic agents, anti-inflammatory agents, antibodies, antigens, adhesins, immunoglobulins, enzymes, hormones, neurotransmitters, cytokines, proteins, globular proteins, cell adhesion proteins, peptides, cell adhesion peptides, proteoglycans, toxins, polysaccharides, carbohydrates, fatty acids, drugs, vitamins, DNA fragments, RNA fragments, nucleic acids, dyes, and ligands. Suitably, the binder includes one or more of the following: glycoproteins, oligosaccharides, lectins, and glycoconjugates.

[0077] The binders suitable for use in this invention have a variety of sources, many of which can be derived from naturally occurring solutions, such as emulsions, urine, mucus, saliva, eggs, fungi, algae, and plant extracts. The binders can also be synthesized (e.g., through in vitro translation), engineered (e.g., through recombinant engineering), or naturally occurring binders can be processed or modified to prepare specific peptides, glycopeptides, fragments, polysaccharides, or the like, for example, representing only the binding portion of a specific larger molecule.

[0078] Another advantage of the various binders discussed in this article is that they are non-toxic and environmentally friendly compared to commonly used antimicrobial or antiviral agents. For example, polyguanidine compounds, commonly used as biocides, are classified as FDA-restricted compounds due to their toxicity to humans and environmental damage. Another example of a guanidine drug is chlorhexidine gluconate, which is planned to be restricted to prescription use only in the future. Similarly, quaternary ammonium compounds, such as polyionenes, are commonly used in wipes and hand sanitizers, but their use is also being restricted by the FDA.

[0079] While some potential binders are expected to bind very specifically to only one target (particularly antibodies), many more binders have a broader range of potential binding targets and can be used to remove more than one target biotoxin, virus, microorganism, and / or microbial component. However, to increase the number of potential targets and thereby improve the use of the device, more than one type of binder can be used in the device, which can be derived from molecules of the same class (e.g., multiple glycoproteins) or molecules of different classes (e.g., glycoproteins and lectins). Therefore, depending on the desired application, the device of the present invention can be designed to have highly specific binding targets, such as in scientific or forensic settings, or for more commonly used purposes due to its suitability for home or field settings.

[0080] Many interactions between biotoxins, viruses, microorganisms, and / or microbial components and host cells or their adhesion surfaces are driven by carbohydrates, glycoproteins, and lectins (carbohydrate-binding proteins or CBPs, glycan-binding proteins or GBPs) and their fragments (such as peptides). For example, the type 1 fimbriae FimH adhesins possessed by certain bacteria, such as certain strains of Escherichia coli, can bind to host cell surface markers such as CD48, TLR4, or more commonly, mannose residues via their lectin (carbohydrate-binding) domains.

[0081] Therefore, it is considered to use glycoconjugates (including glycoproteins, glycolipids, glycosphingolipids, proteoglycans, and glycosaminoglycans) of natural or synthetic origin to provide binding sites for the adhesion of target biotoxins, viruses, microorganisms, and / or microbial components to the device. The glycoconjugates used in the device of the present invention may have terminal residues comprising one or more of mannose, N-acetylglucosamine, N-acetylgalactosamine, N-acetylneuraminic acid and N-hydroxyacetylneuraminic acid (sialic acid), galactose, glucose, and fucose moieties.

[0082] Suitable glycoconjugates and novel glycoconjugates applicable to the apparatus of the present invention include A-BSA blood type, B-HSA blood type, Fuc-α-4AP-BSA, Fuc-β-4AP-BSA, 2'-fucosyllactose-BSA, difucosyl-p-lact-N-hexasaccharide-APD-HSA (Lea / Lex), tri-fucosyl-Ley-heptasaccharide-APE-HSA, monofucosyl, monosialic acid-N-neohexose-APD-HSA, Gal-b-4AP-BSA, Galα1,3Gal-BSA, Gal-α-1,3Galb1, Gallb1,4Gal-BSA, Galα1,2Gal-BSA, 4GlcNAc-HSA, Gal-α-PITC-BSA, Gal-β-ITC-BSA, and Glc-b-4 AP-BSA, Glc-β-ITC-BSA, GlcNAc-BSA, Globotriose-HSA, Globo-N-tetraose-APD-HSA, Globotriose-APD-HSA, GM1-pentasaccharide- APD-HSA, Asialo-GM1-tetrasaccharide-APD-HSA, Globo-N-tetraose-APD-HSA, Globotriose-APD-HSA, H-type II-APE-BSA, H-type 2-APE-HSA, Manα1,3(Manα1,6), Man-BSA, Man-α-ITC-BSA, Man-b-4AP-BSA, LacNAc-BSA, LacNAc-α-4AP-BSA, LacNAc-β-4AP-BSA, Lac-β-4AP-BSA, Lacto-N-tetraose-APD-HSA, Lacto-N-fucopentaose I-BSA (Lacto-N-fucopentaose I-BSA), lacto-N-neotetraose-APD-HSA, lacto-N-fucopentose II-BSA, lacto-N-fucopentose III-BSA, Lacto-N-difucohexaose I-BSA (Lacto-N-difucohexaose I-BSA), Lewis a-BSA, Lewis x-BSA, Lewis y-tetra-APE-HSA (Lewis y-tetrasaccharide-APE-HSA), LNDI-BSA / Lewis b-BSA, Di-Lex-APE-BSA, Di-Lewisx-APE-HSA, Tri-Lex-APE-HSA, L-rhamnose-Sp14-BSA, 3'-sialyl-lactose-APD-HSA, 3'-sialyl-3-fucosyllactose-BSA, 6'-sialyl-lactose-APD-HSA, Xyl-α-4AP-BSA, Xyl-β-4AP-BSA, 3'-sialyl Lewis x-BSA, 3'-sialyl Lewis a-BSA α-BSA, 6-SulfoLewis x-BSA, 6-SulfoLewis α-BSA, 3-SulfoLewis α-BSA, 3-SulfoLewis x-BSA, sialyl-LNF V-APD-HSA, and sialyl-LNnT-penta-APD-HSA.

[0083] Suitable glycoproteins for use in the device of the present invention may have terminal residues comprising one or more of the following: mannose, N-acetylglucosamine, N-acetylgalactosamine, N-acetylneuraminic acid and N-hydroxyacetylneuraminic acid (sialic acid), galactose, glucose and fucose moieties. Such glycoproteins and oligosaccharides may be derived from naturally occurring solutions, such as emulsions, urine, mucus, saliva, eggs, fungi, algae and plant extracts. Specific glycoproteins suitable for use in the device of the present invention include Tamm-Horsfall protein, fetoglobulin, asialofetuin, invertase, fibrinogen, α-1-antitrypsin, α-crystallin, ceruloplasmin, α-1-acidic glycoprotein, RNAse B, transferrin, β-lactoglobulin, C-lactalbumin, albumin, β-casein, C-casein, K-casein, lactoferrin, ovalbumin, oval mucin, ovotransferrin and derived glycomacropeptides. Mucins (highly glycosylated, high-molecular-weight proteins) and other glycoproteins found in mucus can also be used. These components of mucus are thought to reduce the risk of infection by interfering with microbial adhesion and preventing biofilm formation (Caldara et al., Current Biology, 2012).

[0084] Lectins, or carbohydrate-binding proteins, are commonly involved in the binding of bacteria and viruses to their intended targets for intercellular interactions and in innate and adaptive immune responses. Lectins are present in all organisms and play a variety of roles in cell adhesion, immune recognition, microbial recognition (such as pathogens and symbionts), host recognition, toxin activity, and plant protection. In research contexts, many lectins can be efficiently isolated from plant and fungal species and can be engineered to alter their specificity. Lectins are used to purify and characterize glycoconjugates, and lectin-histochemistry is used for staining cells, tissues, and organs to understand the differences in glycosylation of biological samples under different conditions.

[0085] The lectins intended for use in this invention and their sources include, but are not limited to, the following substances: AIA, Jacalin (jackfruit lectin), (jackfruit) Artocarpus integrifolia ), jackfruit lectin; RPbAI (black locust, Robinia pseudoacacia ), locust agglutinin; AAL (Auricularia auricula-judae), Aleuria aurantia ), Orange-yellow Coccidioidomyces lectin; ABL (Agaricus bisporus), (Button mushroom) Agaricus bisporus ), edible fungi lectins; ACA (Amaranthus genus), Amaranthus caudatus Amaranth red lectin; AMA (Arisaema variegata) Arum maculatum ), spotted aromatin; BPA, (Bauhinia flower) Bauhinia purpurea Camels foot tree lectin; CAA (Caragana arboreum) Caragana arborescens ), pea tree lectin; Calsepa (a type of flowering plant) Calystegia sepium ), Convolvulella fuciformis; CCA (Zodiac Crab) Cancer antennarius California crab; ConA, (canana, Canavalia ensiformis ), sword bean lectin; CPA, (Chickpea) Cicer arietinum ), chickpea lectin; DBA (Double-flowered Lentil), Dolichos biflorus ), horse bean lectin; DSA (Mandala) Datura stramonium ), Datura condensate; ECA (Erythrina crista-galli) Erythrina cristagalli Cockscomb / Erythrina lectin; EEA (Euonymus japonicus) Euonymous europaeus ), Euonymus agglutinin; GHA (Money Peppermint) Glechoma hederacea ), peperomia lectin; GNA, (Snow Drop Flower, Galanthus nivalis Snowdrop agglutinin; GSL-I-B4, (Ghana seed, Griffonia simplicifolia ), Ghana seed / Ghana lectin-I; GSL-II (Ghana seed), Griffonia simplicifolia ), Ghana seed / Ghana lectin-II; HHA, (Amaryllis macrocarpa) Hippeastrum hybrid Amaryllis agglutinin; HPA (Roman snail) Helix pomatia ), snail lectin; Lch-A, (Soldier Bean, Lens culinaris ), lentil lectin A; Lch-B, (Soldier Bean, Lens culinaris ), lentil lectin B; LEL, (Tomato) Lycopersicum eculentum ), tomato lectin; LTA (European Bud Root) Lotus tetragonolobus ), lotus condensate; MAA, (Korean locust tree) Maackia amurensis ), saddle tree lectins; MOA (Small leather umbrella with stiff handle) Marasmius oreades ), hard-stemmed small bark umbrella agglutinin; MPA (Maclura pomifera), a lectin from the mulberry tree; NPA, (Nymphoides) Narcissus pseudonarcissus ), Narcissus agglutinin; PA-I (Pseudomonas aeruginosa) Pseudomonas aeruginosa ), Pseudomonas aeruginosa agglutinin; PCA (Polygonum multiflorum) Phaseolus coccineus ), red bean lectin; PHA-E, (from kidney beans, Phaseolus vulgaris ), bean erythropoietin; PHA-L, (bean, Phaseolus vulgaris ), bean leukocyte lectin; PNA (peanut, Arachis hypogaea ), peanut lectin; PSA (peas, Pisum sativum ), pea lectin; RCA-I / 120, (castor bean, Ricinus communis ), Ricin I; SBA, (soy, Glycine max ), soybean lectin; SJA (locust flower) Sophora japonica ), Sophora japonica lectin; SNA-I (Black Elderberry) Sambucus nigra ), elderberry lectin-I; SNA-II (Black Elderberry) Sambucus nigra ), elderberry lectin-II; STA (Potato) Solanum tuberosum ), potato lectin; UEA-I, (Gorgon bean, Ulex europaeus ), Vitex lectin-I; VRA (mung bean sprouts) Vigna radiate ), mung bean lectin; VVA-B4, (Glossy-leaved Purple Vetch, Vicia villosa ), hairy vetch lectin; WFA (Wisteria florida) Wisteria floribunda ), Japanese wisteria lectin; and WGA, (cultivated wheat, Triticum vulgaris ), wheat germ lectin.

[0086] preparation

[0087] While theoretically, the binder can be relatively easily impregnated into the carrier material, for example by immersing the carrier material in an aqueous solution containing the binder, allowing it to be absorbed or adsorbed onto or into the carrier, proper bonding between the binder and the carrier material can create chemical bonds, particularly covalent bonds, between them. This relatively strong and permanent bond is advantageous because the binder is not lost over time, and target biotoxins, viruses, microorganisms, and microbial components will be more firmly retained on the device / carrier material and are less likely to be transferred to subsequent surfaces. Not wanting to be bound by theory, it is also considered that the stronger the adhesion between the binder and the carrier material, the more likely the target is to be absorbed and adhered to the carrier, rather than the binder itself being removed from the carrier. Therefore, by forming covalent bonds between the binder and the carrier material, the safety, effectiveness, stability, and lifespan of the device are improved.

[0088] One or more binders to be attached to the carrier material can be provided or formulated in any suitable manner. For example, the binder can be formulated in a buffer solution with a diluent and / or excipients or stabilizers. The binder may alternatively or additionally be provided in the form of a pharmaceutically acceptable carrier, which may include one or more of solutions, rinses, shampoos, sprays, lotions, gels, foams, lubricants, creams, ointments, soaps, non-soap bars, and powders.

[0089] To facilitate the formation of covalent bonds between the binder and the carrier material, it may be practical to chemically treat the carrier material to provide attachment sites for the binder. For example, in the case of carrier materials comprising cellulose, cellulose can be treated to generate acidic and / or aldehyde functional groups, which can react with the amino groups of proteins to form bonds. In the reaction treating these carriers, the carbohydrate rings in the cellulose are disrupted by an oxidizing agent. In particular, the oxidizing agents used are thought to be perhalates, such as periodate or perchlorate, percarbonate, permanganate, hypochlorite, perborate, or peroxides. Other oxidation methods may include cellulose oxidation mediated by TEMPO (2,2,6,6-tetramethylpiperidin-1-oxy); oxidation in phosphoric acid with sodium nitrate and / or sodium nitrite; and / or treatment with the activator toluene sulfonyl chloride in the presence of an organic solvent (such as acetone / dioxane) and a base (such as pyridine or triethylamine). For example, the exemplary methods discussed in US5,516,673; Cumpstey I. Chemical modification of polysaccharides. ISRN Org Chem. 2013 Sep 10;2013:417672; Saito T, Isogai A. TEMPO-mediated oxidation of native cellulose; The effect of oxidation conditions on chemical and crystal structures of the water-insoluble fractions. Biomacromolecules. 2004;5(5):1983-1989; and Kim UJ et al., Periodate oxidation of crystalline cellulose. Biomacromolecules. 2000;1(3):488-492.

[0090] The purpose of this treatment is to introduce reactive groups into the cellulose molecule, which can be one or more of, for example, aldehydes, ketones, N-hydroxysuccinimides, epoxides, imide esters, acid anhydrides, or carbonate groups. Reactions 1 and 2 illustrate an exemplary reaction in which sodium periodate is used to generate an active aldehyde group (reaction 1) by ring-opening of D-glucose units linked via cellulose β(1-4), followed by attachment of proteins such as lectins, glycoproteins, or neoglycoconjugates (reaction 2). This reaction can be carried out in a buffer solution at pH 5-9. Figure 7 ). [Reaction 1] [Reaction 2]

[0091] In the example given below, a "Schiff base" (-CH=NH-) is formed between the cellulose unit and the attached protein. Optionally, this double bond can be reduced to a single bond to improve the persistence of the bond. This can be achieved by using a reducing agent, such as sodium cyanoborohydride. This reaction will also reduce the exposed CH=O portion to CH2OH.

[0092] Such reactions form irreversible and highly stable bonds, allowing the desired carbohydrates and proteins to be embedded within cellulose materials. Similar reactions can be used to link glycopolymers, multimeric proteins, and other biopolymers, where amide or carboxylic acid bonds are used for conjugation. Given that these reactions target glycomonomers, it is understandable that similar methods could be used to attach binders to other glycocarriers, such as polysaccharides, including starch, glycogen, kelp polysaccharides, fungal β-glucan, chitin, pectin, xylan, arabinoxylan, dextran, or amylose. For example, dextran has been oxidized and subsequently bound to soybean peptides (Wang and Xiong, J Food Sci Technol, 2016). Other glycopolymers, such as peptidoglycans (found in bacterial cell walls), can also be substrates for binder attachment.

[0093] It is also understandable that oxidation methods, such as those described, which involve subsequently binding cellulose with a binding agent, are superior to methods that involve modifying the reagent to be bound itself, because such treatments can disrupt or destroy the binding potential of those reagents. In contrast, the methods described herein preserve the carbohydrate (or other) chemistry of the binding agent while ensuring that it is firmly bound to the carrier material. Similarly, the lifetime of covalent bonds is superior to the retention time of chemicals bound to the carrier material by electrostatic attraction or other forces, as such bonds degrade over time.

[0094] To promote the long-term stability and sterility of the device of the present invention, the carrier material, carrier solution, preparation material and / or packaging material may be treated before, during or after the above preparation steps by a combination of filtration, heating, chemicals, radiation and high pressure; for example by pasteurization, high pressure sterilization, gamma radiation, ultraviolet radiation, electron beam (eBeam radiation), gas vapor sterilization (ozone, chlorine dioxide, ethylene oxide, nitrogen oxides) or similar methods.

[0095] Similarly, buffer solutions can be used to promote the long-term stability and sterility of devices, such as borate, Tris, and citrate buffers, which have the added advantage of being safe for ophthalmic applications. Target biotoxins, viruses, microorganisms and microbial components

[0096] The device according to the invention can target biotoxins, viruses, microorganisms, and / or microbial components associated with biological threats, i.e., potential hazards from biological weapons, synthetic biological products, and / or weaponized microorganisms, such as in the case of bioterrorism, or potential epidemic agents, such as influenza variants, SARS, MERS, Hantavirus, Nipah virus, Ebola virus, Zika virus, etc. Devices targeting such targets include wipes and filters that can be used to protect against or eliminate these hazards. However, the device according to the invention can also be used for defensive research against such agents, for example, for routine research or the production of vaccines or antitoxins. Therefore, the device can be used for biomonitoring environments, such as capturing or screening persistent biological threat agents after anticipated release or during natural outbreaks, or for preventing epidemic agents and foodborne agents. Since the active identification of these agents for forensic, biosurveillance, or other purposes is often crucial, it is advantageous that the primary purpose of the device of the invention is not to destroy the target but to remove one of them. Examples of such biothreats and species believed to cause them include bacteria such as *Francisella* (tularemia), *Bacillus anthracis* (anthrax), *Clostridium botulinum* (botulism), *Burkholderia melioides* (melioidosis), and *Burkholderia pseudomelioides* (melioidosis); viruses such as influenza virus, Ebola virus, Marburg virus, smallpox virus (smallpox), foot-and-mouth disease virus (oral sores virus), SARS-related coronaviruses, and Chapare / Lujo virus (Q fever caused by *Coxiella*, a family of arenaviridae); and toxins such as botulinum neurotoxin, ricin, abrin, and Shiga-like toxin. In particular, severe acute respiratory syndrome coronavirus 2 (novel coronavirus, SARS-CoV-2) is considered a biothreat and can be a target of embodiments of the present invention. Alternative strains are species similar to biothreat agents in one or more aspects and can be used as mimics to study various strategies for combating biothreats. Examples of species that can serve as such alternatives and can also be targeted by the device described herein include Bacillus species (Bacillus subtilis, Bacillus atrophus, Bacillus mycosis fungoides); Clostridium sporogenes and *Holarcctica holarctica* LVS subspecies (… Francisella tularensis subsp. holarctica LVS).

[0097] The target bacteria may also be pathogens causing hospital-acquired infections (HAI), healthcare-associated infections (HCAI), or nosocomial infections, and / or antibiotic-resistant bacteria that resist destruction by common antibiotics. Examples of such bacteria include Clostridium difficile, methicillin-resistant Staphylococcus aureus (MRSA), vancomycin-resistant Staphylococcus aureus (VRSA), Escherichia coli (STEC, VTEC, EHEC), Clostridium difficile, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, Enterococcus faecalis, nontuberculous mycobacteria, occasional mycobacteria, Proteus mirabilis, etc. The advantage of this invention against such bacteria is that adhesion is not affected by the mechanisms these bacteria use to destroy or evade antibiotics.

[0098] Another advantage of this invention is its effectiveness in removing bacterial spores. As previously mentioned, spores produced by certain microorganisms are highly resistant to heat, or chemical, pharmaceutical, and ultraviolet radiation, making them difficult to destroy. However, the adhesion method used in this invention has proven effective in removing these targets because it eliminates the need to attempt to directly destroy the spores.

[0099] Targets may include biotoxins, viruses, microorganisms, and microbial components associated with foodborne illnesses. Many such targets are bacteria, such as Campylobacter, Clostridium, Escherichia coli, Listeria, Salmonella, Shigella, Staphylococcus, Vibrio, and Helicobacter pylori. Targets may also be viruses such as norovirus, rotavirus, and foot-and-mouth disease virus. In such cases, the device according to the invention can be used for cleaning food preparation surfaces and utensils, or can be used as mats, napkins, etc.

[0100] Microbial components, such as bacterial toxins, can also be anticipated as targets of the device of the present invention. Such toxins include, for example, cholera toxin, botulinum toxin, pertussis toxin, enterotoxin, tetanus toxin, and staphylococcal enterotoxin. Similarly, plant- or animal-derived biotoxins, such as tetrodotoxin, ricin, and abrin, are considered targets of the device of the present invention. For example, the highly toxic ricin is a heterodimer; the A chain acts as an N-glycoside hydrolase, which is the basis of its toxicity, and the B chain is a lectin that can bind to galactose residues on the surface of target cells, thereby enabling cell entry. Using the device of the present invention with a specific binding agent that can interact with the B-chain lectin can effectively remove or otherwise capture these proteins. Other toxic proteins, such as abrin, have similar lectin components and can also serve as targets. In this case, the present invention is advantageous compared to existing antimicrobial methods because toxins cannot be killed like microorganisms and are often resistant to denaturation by chemical or other means. The adhesive method of the present invention can remove toxins without these problems.

[0101] Tables 2 and 3 show the various bacterial toxins and their top ten known specific interactions with lectins (Table 2), and the glycoprotein / neoglycosidic conjugates identified based on binding assays (Table 3). These analyses were performed using glycan microarrays to evaluate selected toxins against various lectins and glycoprotein / neoglycosidic conjugates. These techniques represent a tool for in vitro assessment of protein-carbohydrate interactions, allowing for an increased number of possible experiments with limited sample sizes and facilitating analysis or method screening prior to subsequent focused studies. (Kilcoyne, Gerlach, Kane, and Joshi, Analytical Methods, 2012).

[0102] Table 2 Table 3

[0103] application

[0104] The device of the present invention is intended for a variety of applications, such as prevention, treatment, and topical application. Possible uses include purification, cleaning, sample collection, sample retention, sample concentration, forensic analysis of samples, wound care and healing, prevention of disease transmission and spread, prevention of secondary contamination, prevention of biofilm formation, personal hygiene, and / or reduction of stress and fear associated with risks related to transmission agents.

[0105] Methods for treating or preventing certain conditions and diseases using the device of the present invention are also provided. These diseases include human, animal, and plant diseases that can be mediated by bacteria, fungi, viruses, or toxic agents, or by eukaryotic microorganisms (such as malaria parasites), trypanosomes (such as Leishmania), and sleep-related parasites. For example, target microorganisms or microbial components may cause skin diseases and conditions.

[0106] Examples of skin diseases and conditions caused by fungal factors, and species considered causative, include candidiasis (Candida albicans), pityriasis versicolor (Malassezia furfur or Malassezia furfur), seborrheic dermatitis (Malassezia spp.), and tinea pedis (athlete's foot, possibly caused by fungal species including Trichophyton spp., Epidermophyton spp., and Microsporum spp.). Other infections and factors considered to cause or be involved in these infections include acne vulgaris (Propionibacterium acnes, Propionibacterium granulosum, and Pseudomonas aeruginosa), staphylococcal scalded skin syndrome, impetigo, leg ulcers, folliculitis, boils, pyoderma (Staphylococcus aureus, Streptococcus pyogenes, and Pseudomonas aeruginosa), and common body odor (Propionibacterium acnes). Treatment of breast tissue inflammation (mastitis), such as inflammation mediated by Staphylococcus aureus, Streptococcus agalactiae, Streptococcus bovis, Escherichia coli, Pseudomonas aeruginosa, Streptococcus lactis, and Staphylococcus chromogenicus, is also considered. Devices designed to remove these factors from the skin as an adjunct to treatment, or devices designed to remove these factors from the surface to reduce transmission, can be manufactured. These conditions can be treated or prevented by applying the device according to the invention to infected or at-risk skin to remove target biotoxins, viruses, microorganisms, or components thereof. Methods for preventing wound infection are also considered; by removing target viruses, microorganisms, or microbial agents from the skin on or around the wound, or from the site of a future wound (e.g., in surgery), opportunistic infectious agents can be prevented from colonizing the wound.

[0107] It is also anticipated that the target of the device may be those present in body cavities that may cause oral dysbiosis, disease, or condition, such as gingivitis, periodontitis, dental caries, or halitosis (bad breath), such as target biotoxins, viruses, microorganisms, or microbial components. Target biotoxins, viruses, microorganisms, or microbial components may cause vaginal infections. The device of the present invention can be applied in or around such cavities to treat or prevent infections.

[0108] Factors involved in causing sexually transmitted diseases that can be targeted by the device of the present invention include Neisseria gonorrhoeae, Chlamydia trachomatis, Treponema pallidum, Ureaplasma urealyticum, and Haemophilus ducreyi.

[0109] Factors that can be targeted by the device of the present invention and that cause eye infections include Staphylococcus, Neisseria gonorrhoeae, and Chlamydia trachomatis.

[0110] Factors that can be targeted by the device of the present invention and that cause upper respiratory tract infections include Aspergillus, Streptococcus pneumoniae and other Streptococcus species, Pseudomonas aeruginosa, Bordetella pertussis, Moraxella catarrhalis, Mycoplasma pneumoniae, Mycobacterium tuberculosis, Coxsella bebenzna, Klebsiella pneumoniae, Staphylococcus aureus, Legionella pneumophila and Proteus (such as Escherichia coli, Proteus and Serratia), Haemophilus influenzae, influenza virus, rhinovirus and coronaviruses such as SARS, MERS and the pandemic novel coronavirus.

[0111] The apparatus of the present invention is also intended for removing biofilms, i.e., aggregates of microorganisms that adhere to each other and to the surface, from a target surface. Such biofilms are difficult to remove by conventional methods due to the large number of organisms and the presence of extracellular factors that protect them from attack.

[0112] Devices as described above are also considered for the delivery of beneficial, symbiotic, probiotic, non-harmful, and symbiotic bacterial and / or microbial components and / or controlled doses of biotoxins between surfaces (including skin) for therapeutic and cosmetic purposes. In this case, a binder capable of binding probiotic targets is attached to a carrier material and used to bind multiple layers of probiotic microorganisms or microbial components for release onto selected surfaces. In this manner, the device can be used to collect and / or concentrate beneficial microorganisms (e.g., symbiotic and probiotic bacteria) and transfer, transplant, and / or deliver them to another site or surface, including internal delivery, such as delivery to the gastrointestinal tract. While the transferred microorganisms themselves can bind to the device of the present invention via the binder, replication may still occur, and subsequently generated microorganisms may not be bound and can be freely transferred to the target surface. Similar methods can allow for the collection and / or storage of beneficial bacteria for later use. For this or other purposes (such as forensic analysis or laboratory use), the bound biotoxins, viruses, microorganisms, or microbial components can even be isolated from the device, for example, by changing the pH or ionic strength using a buffer solution, or by using a weak acid. Monosaccharide or disaccharide solutions can also be used to disrupt sugar-protein interactions, thereby releasing bound biotoxins, viruses, microorganisms, or microbial components.

[0113] Furthermore, the device of the present invention can also be used to capture or remove targets that are not strictly speaking biotoxins, viruses, microorganisms, or microbial components, if they can be bound by the binders considered herein. For example, allergens and other microscopic components produced by non-microbial life may have surface components, such as lectins or glycoconjugates, which may be bound by the aforementioned binders. Examples include potential allergens in foods such as plant pollen, fungal spores, dust mite feces and other components, nuts and shellfish, animal or plant venoms or toxins, and animal products such as dander. Such targets can be harmful to humans or animals by causing allergic reactions or otherwise. Since allergic reactions are typically mediated by cell surface interactions, and some allergens contain or are composed of glycoconjugates, the device of the present invention can effectively bind such targets. Advantageously, this can allow the removal of such targets from surfaces, liquids or gases, or the face or skin of a subject. For example, a device prepared to provide binding sites for plant pollen can be used to remove pollen from surfaces or the eyes or skin of humans or animals.

[0114] In the context of an epidemic or outbreak, the present invention can be used in a variety of ways, including but not limited to: purifying exposed skin to reduce the risk of transmission during the removal of personal protective equipment (PPE); sampling and cleaning of the PPE itself; and collecting samples from the public (e.g., during screening in transport hubs / vehicles) to aid future decision-making (implementing lockdowns, excluding public access routes and transport units, etc.).

[0115] Devices for delivering inhibitory compounds / anti-adhesion molecules (such as antibacterial agents, antiviral agents, antifungal agents, and antitoxins) are also considered.

[0116] Another possible use of embodiments of the present invention in laboratory settings or elsewhere is in purifying fractions during biopharmaceutical and pharmaceutical manufacturing processes to capture components containing glycans and lectins. For example, this might involve removing LPS / endotoxins, microbial residues, and contaminants or non-product fractions generated during the manufacturing process. This can also be applied to recombinant protein / vaccine production to remove host components and enrich the desired product.

[0117] The apparatus and method of the present invention can also be used in conjunction with surgical gloves or other surgical or medical devices, for example, by adding the apparatus of the present invention to the surface of a surgical glove. This helps reduce the likelihood of infection transmission during surgery or other care, as infection is a major source of biocontamination of implanted devices during surgery. One example is the use of surgical gloves during catheter implantation. Example

[0118] The following non-limiting examples illustrate some implementations of the present invention.

[0119] Example 1 – Device Preparation

[0120] To generate active aldehyde groups for subsequent attachment of binders to the cellulose chain, a periodate oxidation reaction was performed. A cellulose backbone of 33 g / m³ of 100% cotton material was immersed in a 0.1 M acetate buffer (1:50, w / v) containing 5.0 mg / ml sodium periodate, and chemically treated with sodium periodate (Sigma-Aldrich 311448). The mixture was kept in darkness for efficient reaction, gently shaken at 50 rpm for 6 hours at room temperature. The reaction is thought to occur between the C2-C3 bonds of the glucopyranoside ring, resulting in the formation of two aldehyde groups at the C2 and C3 positions. The resulting compound is 2,3-dialdehyde cellulose (DAC).

[0121] The material was then thoroughly washed with ice-cold distilled water (3 washes, 10 times the absorbent volume each time) to remove periodate oxidants from the treated material. For the addition of a binding agent (lectin, glycoprotein, glycoconjugate, or neoglycoconjugate) after chemical treatment, it is believed that the active ingredient chemically binds to the DAC residues of the cellulose backbone. A binding agent solution (1 mg / ml) was prepared by dissolving the agent in PBS at pH 7.4. The treated cotton material was then immersed in the protein solution at a ratio of 1:25 (w / v). The material was incubated at 4°C for 16 h, and then washed 3 times with 10 times the absorbent volume in PBS at pH 7.4.

[0122] Example 2 - Biological Threat Factors

[0123] Biothalassemia bacteria (Tulafrancsis, Clostridium botulinum, and Bacillus anthracis (cells and spores)) were recovered, grown to a stationary phase, and stained to target the biothalassemia. After careful analysis of the binding data generated by the glycan microarray as described above, and based on comparisons with model organisms, glycoprotein / glycoconjugates and lectins were recommended for the preparation of antimicrobial cellulose-based devices. The efficacy of the active cellulose wiping material (prepared according to Example 1) was tested on plastic / metal / glass surfaces contaminated with the aforementioned biothalassemia agents, comparing it to dry wiping materials and wiping materials treated with relevant buffers (dH2O, PBS).

[0124] From OD stained with 0.5% crystal violet 600Contaminants were prepared in overnight cultures of 2.0 μL. 100 µL of each contaminant was placed in each selected test area with a diameter of 5 cm and dried for 60 min. For each of the following experiments, the swab was placed in the center of the contaminated area and left to stand for 10 minutes without movement. After removing the swab, the “residual contaminants” on each surface were recovered by washing with 0.5 ml of PBS (pH 7.4) and analyzed using a series of quantitative methods to count the remaining bacteria on the surface (measurement of optical density, colony count, PCR).

[0125] For Tulafrancsis ( Figure 1A-1C As described above, it uses a protein containing fetal glycoprotein ( Figure 1A ), desialyl glycoprotein ( Figure 1B ) or lectin GNA ( Figure 1C Efficacy testing was performed on the active wipes. The recovery solution was tested by adding an appropriate buffer solution and then at 600 nm (OD). 600 Residual contaminants were monitored by measuring absorbance / density. Raw values ​​without surface adjustment are shown. An asterisk indicates a statistically significant data point (p < 0.05) compared to the "unwiped" case, based on a Student's t-test. The error bar represents the standard deviation of three replicates. It can be seen that, in all cases, using "active" wipes treated with glycoproteins or lectins resulted in a significant reduction in residual bacteria.

[0126] For botulinum toxin ( Figure 2A-2D ), using a protein containing fetal glycoprotein ( Figure 2A ), desialyl glycoprotein ( Figure 2B ) or lectin GNA ( Figure 2C Efficacy testing was performed on the active wipes. The recovery solution was tested by adding an appropriate buffer solution and then at 600 nm (OD). 600 Residual contaminants were monitored by measuring absorbance / density. Raw values ​​without surface adjustment are shown. An asterisk indicates a statistically significant data point (p < 0.05) compared to the "unwiped" case, based on a Student's t-test. The error bar represents the standard deviation of three replicates. It can be seen that, in all but one case, using an "active" wipe treated with glycoproteins or lectins resulted in a significant reduction in residual bacteria. Figure 2D The image shows residual bacteria on the surface after wiping treatment; control group: 7.32 × 10⁻⁶. 8 The recovery rate of standard stock strains at cfu / ml was measured by colony-forming units (cfu). For this purpose, the recovered contaminants were serially diluted, and 100 µl of each contaminant was spread onto agar plates for bacterial incubation. Plates with colony counts of 30–300 were considered a suitable counting range.

[0127] Targeting anthrax cells ( Figure 3A ) or spores ( Figure 3B Using active swabs containing fetal glycoprotein, desialyl glycoprotein, GNA lectin, GSL-I-B4 lectin, PA-I lectin, AMA lectin, or RCA-1 lectin to treat Bacillus anthracis ( Figures 3A-3B (and Table 4) Efficacy test. Residual contaminants after wiping treatment, control 1.21 × 10 7 CFU / ml (trophic cells) or 1.31 × 10⁻⁶ 7 Standard stock strains at cfu / ml (spores) were recovered by colony-forming units (cfu). Recovered contaminants were serially diluted, and 100 µl of each contaminant was spread onto agar plates for bacterial incubation. Plates with colony counts of 30–300 were considered a suitable counting range. Raw values ​​without surface adjustment are shown. An asterisk indicates a statistically significant data point (p < 0.05) compared to the unwiped condition, based on a Student's t-test. Error bars represent the standard deviation of three replicates. These data are also shown in Table 4, which shows the percentage of residual contaminants found compared to surfaces treated with dry wiping (FET-fetoglobulin, ASF-desialanofetoglobulin).

[0128] Table 4 Residual contaminants after use of control and active swabs - Anthrax nutrient cells Residual contaminants after use of control and active swabs - Anthrax nutrient cells

[0129] The device of this invention is also used to resist influenza virus contamination on glass, plastic, and metal surfaces. Briefly, the surface is contaminated with 500 μl of virus solution, the supernatant is applied to the surface, and it is allowed to dry for 3 hours. A swab conjugated with a fetal glycoprotein or an attached desialylate glycoprotein is used. All surfaces are contaminated three times with different types of swabs. For the swab test, the swab is placed in the center of the contaminated area (without moving). The swabs are allowed to interact for 10 minutes. After incubation, the swabs are removed, and the recovery rate of residue from the contaminated area is assessed. Each surface is washed with 1 ml of PBS, and the recovered solution is transferred to a sterile Eppendorf tube for viral RNA isolation and for cleaning of glass (…). Figure 4A ),plastic( Figure 4B ) and metals ( Figure 4CThe residues were quantified. The figure shows the amount of virus isolated from the surface, relative to the amount found after using only dry swabs. Error bars represent standard deviations, in triplicate. The results showed that while swabs with attached fetoglobulin appeared to reduce residual virus, leaving only 2-28% of viral particles after static capture (see Table 5), swabs with attached desialylated fetoglobulin appeared to have no effect compared to PBS-treated swabs.

[0130] Table 5

[0131] Example 3 - Foodborne Disease Factors:

[0132] The device of the present invention (prepared according to Example 1) is also used to combat bacteria associated with foodborne illnesses on glass, plastic, and metal surfaces. Table 6 shows the bacteria tested (EHEC Escherichia coli O157:H7 and Enterobacter cloacae), and the lectins bound to the carrier material in each case.

[0133] Table 6

[0134] Figure 5A and 5B The results of tests for the efficacy of these bacteria are shown. As in the previous examples, contaminants were prepared from overnight cultures stained with crystal violet. 100 µl of each contaminant was placed in each selected test area and allowed to dry for 60 minutes. For each of the following experiments, the swab was placed in the center of the contaminated area and left to stand for 10 minutes without movement. Residual contaminants were monitored by measuring fluorescence after SYTO82 staining. Figure 5A , 5B The original values ​​are shown without surface adjustment. Error bars represent the standard deviation of three replicate experiments. An unwiped contaminated surface was used as a control. Based on the measurement of residual fluorescence after 10 min of static testing, the active swab using WGA lectin left only 1% of *E. coli* O157:H7, while the active swab using GSI-B4 left 4% of *Enterobacter cloacae*. Table 7 also shows the results demonstrating the efficacy of the control and active swabs.

[0135] Table 7 – Contamination Rate Compared to Unwiped Surfaces

[0136] Example 4 - Other skin disease factors (bacteria / fungi):

[0137] Other microorganisms known to colonize the skin are potential targets of the device of the present invention. These include Propionibacterium, Malassezia (formerly known as Pityriasis alba), Candida, Aspergillus, Staphylococcus, Streptococcus, Pseudomonas, and Haemophilus influenzae. For illustration, the device of the examples (prepared according to Example 1) is also used to combat the bacteria Propionibacterium acnes and the fungus Candida albicans associated with skin diseases and conditions.

[0138] Wipes conjugated with the glycoprotein desialized fetoglobulin (ASF) or the lectin WGA are used to clean plastic surfaces contaminated with Propionibacterium acnes, as described in the examples above. Figure 6 After a static wiping test for 10 minutes, the same treatment as in the above examples was performed again. It was observed that 33% of the contaminants remained on the PBS swabs, 15.8% on the ASF swabs, and only 9.5% on the WGA swabs. This indicates that the WGA swabs can capture 90.5% of the contaminants simply through contact (without movement).

[0139] Combating Candida albicans contamination on plastic surfaces using swabs conjugated with lectin ConA ( Figure 7 The contamination and wiping tests were as described previously. To compare capture efficacy at different pH levels, swabs were prepared using buffer solutions with or without the active ingredient (ConA) at pH 5, 7, and 9 and a standard pH of 7.4. The capture efficacy of the active ingredient was observed to be similar across a wide pH range from 5 to 9. Therefore, the swabs exhibited comparable efficacy under the selected conditions, and pH changes did not affect the ability of the active ingredient to capture.

[0140] Example 5 - Wound Cleaning and Care

[0141] To evaluate the device and its efficacy in capturing nutrients from biological surfaces, a porcine skin model was used. Porcine skin has been a primary human skin model for research on human dermatology for the past 20 years. This is due to the similarity in anatomical structure between the two species compared to any other laboratory animal. For example, porcine dermal collagen is more similar to that of humans than that of any other common laboratory animal. The application of porcine skin in wound care and infection research in human diseases has been well-established and studied. The epidermal thickness and structure of porcine skin are highly similar to those of human skin. Vascular features are highly correlated with hair follicle type. *Escherichia coli* and *Candida albicans* strains were used as target organisms.

[0142] Methods such as Figure 8As shown. In short, to remove natural contaminants from pigskin, the sliced ​​samples were placed in water at 60°C for 30 seconds. 100 µl of Escherichia coli (OD 2.0) (stained with crystal violet) or Candida albicans (stained with trypan blue) culture was pipetted onto each pigskin sample, and the samples were air-dried for 30 minutes. As previously described, a swab capture test was performed using the device prepared according to Example 1 by static contact for 10 minutes, then 1 ml of LB or yeast culture medium was added to each pigskin sample, and the contaminant mixture was recovered. The growth of this mixture was monitored to assess the remaining Escherichia coli (…). Figure 9A and B) and Candida albicans ( Figure 10 Quantitative. Figure 9A and 9B E. coli recovered from pigskin after a capture assay using cotton-based swabs containing WGA agglutinin was shown, as measured by absorbance at 595 nm. Figure 9A ) or by colony-forming units ( Figure 9B )Measurement. Figure 10 The image shows Candida albicans DSM 6659 recovered from pigskin after treatment with a cotton-based swab containing ConA or GNA lectin, as measured by absorbance after a 15-hour growth period.

[0143] Swabs conjugated with lectin ConA were used to combat pig skin sections contaminated with Aspergillus fumigatus. The contamination protocol and swab test were as described previously. Aspergillus fumigatus was recovered from pig skin after treatment with a cotton-based swab capture test. The active swabs containing ConA lectin were then inoculated onto potato dextrose agar after serial dilutions of the remaining contaminant at a 1:10 ratio, and colony formation units were measured. Figure 11 Colony counting analysis was performed after incubation at 30°C for 24 hours. Figure 11 The image shows Aspergillus fumigatus strain 819 recovered from pigskin after treatment with a cotton-based swab capture test, in which the active swab contained ConA lectin.

Claims

1. An apparatus for capturing and retaining a target, comprising: Carrier materials for polymers containing carbohydrates; and A binder, the binder comprising: i) A glycoprotein selected from one or more of the following: urinary regulatory protein, fetoglobulin, desialylated fetoglobulin, invertase, α-1-antitrypsin, α-crystallin, ceruloplasmin, α-1-acidic glycoprotein, ribonuclease B, transferrin, β-lactoglobulin, C-lactalbumin, β-casein, C-casein, K-casein, lactoferrin, and ovotransferrin; and ii) A lectin selected from one or more of the following: jackfruit lectin, RPbAI, AAL, ABL, ACA, AMA, BPA, CAA, Calsepa, CCA, ConA, CPA, DBA, DSA, ECA, EEA, GHA, GNA, GSL-I-B4, GSL-II, HHA, HPA, Lch-A, Lch-B, LEL, LTA, MAA, MOA, MPA, NPA, PA-I, PCA, PHA-E, PHA-L, PNA, PSA, RCA-I, SBA, SJA, SNA-I, SNA-II, STA, UEA-I, VRA, VVA-B4, WFA, and WGA; in: The binder is connected to the carrier material via one or more covalent bonds; and The binder can bind to a target, which is one or more of a biotoxin, virus, allergen, microorganism, and microbial components, thereby capturing and retaining the target during use.

2. The apparatus according to claim 1, wherein: i) The carrier material includes cellulose; and / or ii) The carrier material comprises one or more of cotton and paper, and / or ii) The carrier material is in the form of cloth, wiping material, wound dressing, swab, filter, pad, blanket, mat, mask, or coating; and / or iv) The carrier material also contains a buffer solution.

3. The apparatus according to claim 1 or 2, wherein the apparatus comprises a fluid, and wherein the carrier material is carried in the fluid by means of dissolution, suspension, dispersion or emulsification.

4. The apparatus of claim 2 or 3, wherein the carrier material comprises cellulose, and the binder is connected to the cellulose via one or more covalent bonds.

5. The device according to any one of claims 1 to 4, wherein the binder further comprises one or more of the following: antithrombotic agent, anti-inflammatory agent, antibody, antigen, adhesin, immunoglobulin, enzyme, hormone, neurotransmitter, cytokine, protein, globular protein, cell attachment protein, peptide, cell attachment peptide, proteoglycan, toxin, polysaccharide, carbohydrate, fatty acid, drug, vitamin, DNA fragment, RNA fragment, nucleic acid, dye, and ligand.

6. The apparatus according to any one of claims 1 to 5, wherein the glycoprotein is one or more of lactoferrin, fetoglobulin, desialylated fetoglobulin, and α-crystallin.

7. The apparatus according to any one of claims 1 to 6, wherein the binder further comprises a glycoconjugate or a novel glycoconjugate, said glycoconjugate or novel glycoconjugate being selected from A-BSA blood type, B-HSA blood type, Fuc-α-4AP-BSA, Fuc-β-4AP-BSA, 2'-fucosyllactose-BSA, difucosyl-p-lact-N-hexasaccharide-APD-HSA, tri-fucosyl-Ley-heptasaccharide-APE-HSA, monofucosyl, monosialic acid-N-neohexose-APD-HSA, Gal-β-4AP-BSA, Galα1,3Gal-BSA, Gal-α-1,3Galb1, Gal-β-1,4Gal-BSA, Gal-α-1,2Gal-BSA, 4GlcNAc-HSA, Gal-α-PITC-BSA, Ga l-β-ITC-BSA, Glc-β-4AP-BSA, Glc-β-ITC-BSA, GlcNAc-BSA, erythrocyte trisaccharide-HSA, Globo-N-tetrasaccharide-APD-HSA, erythrocyte trisaccharide-APD-HSA, GM1-pentasaccharide-APD-HSA, Asialo-GM1-tetrasaccharide-APD-HSA, Globo-N-tetrasaccharide-APD-HSA, erythrocyte trisaccharide-APD-HSA, H-type II-APE-BSA, H-type 2-APE-HSA, Man-α-1,3. Man-BSA, Man-α-ITC-BSA, Man-b-4AP-BSA, LacNAc-BSA, LacNAc-α-4AP-BSA, LacNAc-β-4AP-BSA, Lac-β-4AP-BSA, Lactose-N-tetrasaccharide-APD-HSA, Lactose-N-fucopentose I-BSA, Lactose-N-neotetrasaccharide-APD-HSA, Lactose-N-fucopentose II-BSA, Lactose-N-fucopentose III-BSA, Lactose-N-difucopentose hexasaccharide I-BSA, Lewis α-BSA, Lewis x-BSA, Lewis y-tetrasaccharide-APE-HSA, Lewis One or more of the following: b-BSA, Di-Lex-APE-BSA, Di-Lewisx-APE-HSA, Tri-Lex-APE-HSA, L-rhamnose-Sp14-BSA, 3'-sialyl-lactose-APD-HSA, 3'-sialyl-3-fucolactose-BSA, 6'-sialyl-lactose-APD-HSA, Xyl-α-4AP-BSA, Xyl-β-4AP-BSA, 3'-sialic acid Lewis x-BSA, 3'-sialic acid Lewis a-BSA, 6-sulfonyl Lewis x-BSA, 6-sulfonyl Lewis a-BSA, 3-sulfonyl Lewis a-BSA, 3-sulfonyl Lewis x-BSA, sialic acid-LNF V-APD-HSA, and sialic acid-LNnT-penta-APD-HSA.

8. The apparatus of claim 7, wherein when the binder is a glycoconjugate, a neoglycoconjugate, or a glycoprotein, the binder has terminal residues comprising one or more of mannose, N-acetylglucosamine, N-acetylgalactosamine, N-acetylneuraminic acid and N-hydroxyacetylneuraminic acid, galactose, glucose, and fucose moieties.

9. The apparatus according to any one of claims 1 to 8, wherein the apparatus further comprises an antimicrobial substance.

10. The apparatus of claim 9, wherein the antimicrobial substance is one or more of a preservative, an antibiotic, or a detergent, or the antimicrobial substance is silver, copper, or EDTA.

11. A method for removing biotoxins, viruses, allergens, microorganisms and / or microbial components from a surface, gas or liquid, the method comprising: Provide an apparatus according to any one of claims 1 to 10; and To bring the surface into contact with the device, or to allow gas or liquid to pass through the device.

12. The method according to claim 11, wherein: i) The binder binds to the biotoxins, viruses, allergens, microorganisms and / or microbial components to be removed; and / or ii) The biotoxins, viruses, allergens, microorganisms and / or microbial components are spores.

13. A method of manufacturing an apparatus for capturing and retaining a target, the method comprising: Provide carrier materials containing carbohydrate-based polymers; The carrier is treated with an oxidant to generate acid and / or aldehyde groups; and The treated carrier is contacted with a binder, such that the binder is linked to a carbohydrate-based polymer via one or more covalent bonds, wherein the binder comprises: i) A glycoprotein selected from one or more of the following: urinary regulatory protein, fetoglobulin, desialylated fetoglobulin, invertase, α-1-antitrypsin, α-crystallin, ceruloplasmin, α-1-acidic glycoprotein, ribonuclease B, transferrin, β-lactoglobulin, C-lactalbumin, β-casein, C-casein, K-casein, lactoferrin, and ovotransferrin; and ii) A lectin selected from one or more of the following: jackfruit lectin, RPbAI, AAL, ABL, ACA, AMA, BPA, CAA, Calsepa, CCA, ConA, CPA, DBA, DSA, ECA, EEA, GHA, GNA, GSL-I-B4, GSL-II, HHA, HPA, Lch-A, Lch-B, LEL, LTA, MAA, MOA, MPA, NPA, PA-I, PCA, PHA-E, PHA-L, PNA, PSA, RCA-I, SBA, SJA, SNA-I, SNA-II, STA, UEA-I, VRA, VVA-B4, WFA, and WGA; Furthermore, the binder can bind to a target, which is one or more of a biotoxin, virus, allergen, microorganism, and microbial components, thereby capturing and retaining the target during use.

14. The method of claim 13, wherein the oxidant is i) periodate; or ii) the oxidant is selected from: 2,2,6,6-Tetramethylpiperidine-1-oxy radical; Sodium nitrate or sodium nitrate in phosphoric acid; Toluenesulfonyl chloride, an activator in the presence of organic solvents and bases; And their combinations.

15. The method of claim 14, wherein the periodate is sodium periodate.

16. The method according to claim 13 or 14, wherein after the above steps, the apparatus is treated by pasteurization, autoclaving, gamma radiation, ultraviolet radiation, electron beam and / or gas vapor sterilization.

17. The method of claim 16, wherein the gas vapor sterilization uses one or more gases selected from ozone, chlorine dioxide, ethylene oxide, and nitrogen oxides.

18. The method according to any one of claims 13 to 17, wherein: i) The carrier material comprises cellulose; and / or ii) The carrier material comprises one or more of cotton and paper; and / or iii) The carrier material is in the form of cloth, wiping material, wound dressing, swab, filter, pad, blanket, mat, mask, or coating; and / or iv) The carrier material also contains a buffer solution.

19. The method according to any one of claims 13 to 18, wherein the apparatus comprises a fluid, wherein the carrier material is carried in the fluid in a manner of dissolution, suspension, dispersion or emulsification.

20. The method according to any one of claims 13 to 19, wherein the glycoprotein is one or more of lactoferrin, fetoglobulin, desialylated fetoglobulin, and α-crystallin.

21. The method according to any one of claims 13 to 20, wherein the treated carrier is further contacted with a binder comprising a glycoconjugate or a novel glycoconjugate, said glycoconjugate or novel glycoconjugate being selected from A-BSA blood type, B-HSA blood type, Fuc-α-4AP-BSA, Fuc-β-4AP-BSA, 2'-fucosyllactose-BSA, difucosyl-p-lact-N-hexasaccharide-APD-HSA, tri-fucosyl-Ley-heptasaccharide-APE-HSA, monofucosyl, monosialic acid-N-neohexose-APD-HSA, Gal-β-4AP-BSA, Galα1,3Gal-BSA, Gal-α-1,3Galb1, Gal-β-1,4Gal-BSA, Gal-α-1,2Gal-BSA, 4GlcNAc-HSA, Gal-α-PITC-BSA, Gal-β- ITC-BSA, Glc-β-4AP-BSA, Glc-β-ITC-BSA, GlcNAc-BSA, Erythrocyte Trisaccharide-HSA, Globo-N-Tetrasaccharide-APD-HSA, Erythrocyte Trisaccharide-APD-HSA, GM1-Pentasaccharide-APD-HSA, Asialo-GM1-Tetrasaccharide-APD-HSA, Globo-N-Tetrasaccharide-APD-HSA, Erythrocyte Trisaccharide-APD-HSA, H-type II-APE-BSA, H-type 2-APE-HSA, Man-α-1,3. Man-BSA, Man-α-ITC-BSA, Man-b-4AP-BSA, LacNAc-BSA, LacNAc-α-4AP-BSA, LacNAc-β-4AP-BSA, Lac-β-4AP-BSA, Lactose-N-tetrasaccharide-APD-HSA, Lactose-N-fucopentose I-BSA, Lactose-N-neotetrasaccharide-APD-HSA, Lactose-N-fucopentose II-BSA, Lactose-N-fucopentose III-BSA, Lactose-N-difucopentose hexasaccharide I-BSA, Lewis α-BSA, Lewis x-BSA, Lewis y-tetrasaccharide-APE-HSA, Lewis One or more of the following: b-BSA, Di-Lex-APE-BSA, Di-Lewisx-APE-HSA, Tri-Lex-APE-HSA, L-rhamnose-Sp14-BSA, 3'-sialyl-lactose-APD-HSA, 3'-sialyl-3-fucolactose-BSA, 6'-sialyl-lactose-APD-HSA, Xyl-α-4AP-BSA, Xyl-β-4AP-BSA, 3'-sialic acid Lewis x-BSA, 3'-sialic acid Lewis a-BSA, 6-sulfonyl Lewis x-BSA, 6-sulfonyl Lewis a-BSA, 3-sulfonyl Lewis a-BSA, 3-sulfonyl Lewis x-BSA, sialic acid-LNF V-APD-HSA, and sialic acid-LNnT-penta-APD-HSA.

22. The method of claim 21, wherein when the binding agent is a glycoconjugate, a neoglycoconjugate, or a glycoprotein, the binding agent has terminal residues comprising one or more of mannose, N-acetylglucosamine, N-acetylgalactosamine, N-acetylneuraminic acid and N-hydroxyacetylneuraminic acid, galactose, glucose, and fucose moieties.

23. The method according to any one of claims 13 to 22, wherein the device further contacts one or more antimicrobial substances.

24. The method of claim 23, wherein the one or more antimicrobial substances are selected from preservatives, antibiotics, detergents, silver, copper or EDTA.

25. The method according to any one of claims 13 to 24, wherein the binder further comprises one or more of the following: an antithrombotic agent, an anti-inflammatory agent, an antibody, an antigen, an adhesin, an immunoglobulin, an enzyme, a hormone, a neurotransmitter, a cytokine, a protein, a globular protein, a cell attachment protein, a peptide, a cell attachment peptide, a proteoglycan, a toxin, a polysaccharide, a carbohydrate, a fatty acid, a drug, a vitamin, a DNA fragment, an RNA fragment, a nucleic acid, a dye, and a ligand.

26. A method for capturing or screening one or more biological threat agents, the method comprising contacting the device according to any one of claims 1 to 10 with one or more biological threat agents.

27. The method of claim 26, wherein the one or more bio-threat agents are not destroyed during capture or screening.

28. The method according to claim 26 or 27, wherein the biological threat factor is: (i) Selected from one or more bacteria, including Francisella, Bacillus anthracis, Clostridium botulinum, Burkholderia melioides, and Burkholderia pseudomelioides; (ii) One or more viruses selected from influenza virus, Ebola virus, Marburg virus, smallpox virus, foot-and-mouth disease virus, SARS-related coronavirus, Chapare virus, and Lujo virus; (iii) One or more toxins selected from botulinum neurotoxin, ricin, absinthecin, and shiga-like toxin; and / or (iv) Bacterial spores.

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