A method for determining whether a test sample contains a phytopathogenic fungus, which includes (a) putting the test sample on a front surface of a substrate having a through hole; the substrate having a cellulose film on the back surface thereof; the through hole has a cross-sectional area of not less than 7.065 square micrometers and not more than 19.625 square micrometers; and the cellulose film has a thickness of not less than 0.5 micrometers and not more than 3.7 micrometers; (b) leaving the test sample at rest after the step (a); (c) irradiating the cellulose film with ultraviolet light after the step (b); (d) bringing a back surface of the cellulose film into contact with a fungus color reaction reagent after the step (c); and (e) determining that the test sample contains the phytopathogenic fungus, if a color is given to the fungus color reaction reagent.

The present application discloses proteins or peptides and methods of using such proteins or peptides to evaluate the immune status of a patient. In one embodiment, proteins or peptides may be used to detect endogenous calnexin specific CD4 T cells. In one preferred embodiment, the proteins or peptides may comprise peptide-MHCII tetramers (pMHC tetramers).

Velvet disease infestation is detected using rmAbs that are cross-reactive with one or more A. ocellatum or P. pillulare antigens. The analysis may be performed shipboard, dockside, in an aquaculture or aquarium setting, otherwise in situ at the point of sample collection or elsewhere. The results may be used to monitor health and disease of captured or cultured fish species or the safety of water to be introduced into an aquaculture facility.

The present invention relates to: a method for screening an antifungal agent, the method measuring the amount or activity of proteins involved in passage through the brain-blood barrier; a biomarker composition for diagnosing meningoencephalitis or cryptococcosis; a diagnostic kit including said composition; and a therapeutic pharmaceutical composition including an inhibitor for the protein.

A biorecognition element for rapid detection of fuel biocontamination. The biorecognition element is a biorecognition element selected from SEQ. ID No. 2 through SEQ. ID No. 24, SEQ. ID No. 22 through SEQ. ID No. 44, SEQ. ID No. 46 through SEQ. ID No. 57, SEQ. ID No. 59 through SEQ. ID No. 196 or SEQ. ID No. 198 through SEQ. ID No. 332.

In a first step, when a β-1,6-branched β-1,3-glucan is contained in a test specimen, an active reporter protein comprising one and the other of split reporter proteins is formed by binding the β-1,6-branched β-1,3-glucan to a first fusion protein and a second fusion protein, and when a β-1,3-glucan is contained in the test specimen, the active reporter protein comprising one and the other of the split reporter proteins is formed by binding the β-1,3-glucan to the first fusion protein and a third fusion protein, and in a second step, the active reporter protein formed in the first step is detected and quantified.

Described herein are engineered microbe-targeting or microbe-binding molecules, kits comprising the same and uses thereof. Some particular embodiments of the microbe-targeting or microbe-binding molecules comprise a carbohydrate recognition domain of mannose-binding lectin, or a fragment thereof, linked to a portion of a Fc region. In some embodiments, the microbe-targeting molecules or microbe-binding molecules can be conjugated to a substrate, e.g., a magnetic microbead, forming a microbe-targeting substrate (e.g., a microbe-targeting magnetic microbead). Such microbe-targeting molecules and/or substrates and the kits comprising the same can bind and/or capture of a microbe and/or microbial matter thereof, and can thus be used in various applications, e.g., diagnosis and/or treatment of an infection caused by microbes such as sepsis in a subject or any environmental surface. Microbe-targeting molecules and/or substrates can be regenerated after use by washing with a low pH buffer or buffer in which calcium is insoluble.

Antibody-based binding agents derived from human and camelid immunoglobulins are described, as well as strains of yeast engineered to secrete the binding agents, and methods of treating and preventing Clostridium difficile infections using the engineered strains of yeast. These binding agents recognize and bind with specificity to Clostridium difficile toxin A and/or toxin B and in some cases exhibit toxin neutralizing activity. The binding agents include camelid V.sub.HH peptide monomers, linked groups of V.sub.HH peptide monomers, V.sub.HH peptide monomers joined to antibody Fc domains, and V.sub.HH peptide monomers joined to IgG antibodies.

The present application provides a fungal (1,3)-Beta-D glucan-directed monoclonal antibody, coding genes thereof, expression thereof and application thereof and belongs to the technical area of medicine & biomedical detection. The antibody contains complementarity determining regions of a light chain variable region and its amino acid sequences contain: VL-CDR1 shown by SEQ ID NO:1, VL-CDR2 shown by SEQ ID NO:2 and VL-CDR3 shown by SEQ ID NO:3; the antibody also contains cornplementarity determining regions of a heavy chain variable region and its amino acid sequences contain: VH-CDR1 shown by SEQ ID NO:4, VH-CDR2 shown by SEQ ID NO:5 and VH-CDR3 shown by SEQ ID NO:6. This antibody specifically binds with the fungal (1,3)-Beta-D glucan, has strong antibody affinity and does not trigger cross reaction with interference substances.

The present disclosure belongs to the technical field of biosensors and particularly provides a construction method for a photocathode indirect competition sensor and an evaluation method. The construction method includes: using Z-type Bi.sub.2O.sub.3/CuBi.sub.2O.sub.4 as a sensing platform; calculating a photoinduced electron Z-type transfer path and an energy band structure of Bi.sub.2O.sub.3 and CuBi.sub.2O.sub.4 using a density functional theory (DFT); and constructing a Bi.sub.2O.sub.3/CuBi.sub.2O.sub.4-based biosensor. A photoelectrochemical (PEC) photocathode biosensor based on a Bi.sub.2O.sub.3/CuBi.sub.2O.sub.4 heterojunction prepared through the solution has good repeatability, reproducibility, stability, and specificity for detecting a target. The PEC biosensor constructed in the solution of the present disclosure has a broad application prospect in the fields of healthcare, environment, and food.