Phycoerythrin (PE) and peptide:MHCII (p:MHCII) reactive monoclonal antibodies; methods to generate monoclonal antibodies including, for example, peptide:MHC (p:MHC) reactive monoclonal antibodies; compositions including monoclonal antibodies; and uses thereof.

The present invention relates to a variant of a parent polypeptide comprising an Fc fragment, wherein the variant exhibits an increased affinity for at least one of the Fc (FcR) fragment receptors selected from among FcγRIIIa (CD16a), FcγRIIa (CD32a), and FcγRIIb (CD32b) receptors, relative to that of the parent polypeptide, characterized in that it comprises at least one mutation chosen from among K290G, Y296W, V240H, V240I, V240M, V240N, V240S, F241H, F241Y, L242A, L242F, L242G, L242H, L242I, L242K, L242P, L242S, L242T, L242V, F243L, F243S, E258G, E258I, E258R, E258M, E258Q, E258Y, V259C, V259I, V259L, T260A, T260H, T260I, T260M, T260N, T260R, T260S, T260W, V262A, V262S, V263T, V264L, V264S, V264T, V266L, V266M, S267A, S267Q, S267V, K290D, K290E, K290H, K290L, K290N, K290Q, K290R, K290S, K290Y, P291G, P291Q, P291R, R292I, R292L, E293A, E293D, E293G, E293M, E293Q, E293S, E293T, E294A, E294G, E294P, E294Q, E294R, E294T, E294V, Q295I, Q295M, Y296H, S298A, S298R, Y300I, Y300V, Y300W, R301A, R301M, R301P, R301S, V302A, V302F, V302L, V302M, V302R, V302S, V303S, V303Y, S304T, V305A, V305F, V305I, V305L, V305R and V305S of the Fc fragment, wherein the numbering is that of the EU index or equivalent in Kabat.

The present invention relates to a variant of a parent polypeptide comprising an Fc fragment, wherein the variant exhibits an increased affinity for at least one of the Fc (FcR) fragment receptors selected from among FcγRIIIa (CD16a), FcγRIIa (CD32a), and FcγRIIb (CD32b) receptors, relative to that of the parent polypeptide, characterized in that it comprises at least one mutation chosen from among K290G, Y296W, V240H, V240I, V240M, V240N, V240S, F241H, F241Y, L242A, L242F, L242G, L242H, L242I, L242K, L242P, L242S, L242T, L242V, F243L, F243S, E258G, E258I, E258R, E258M, E258Q, E258Y, V259C, V259I, V259L, T260A, T260H, T260I, T260M, T260N, T260R, T260S, T260W, V262A, V262S, V263T, V264L, V264S, V264T, V266L, V266M, S267A, S267Q, S267V, K290D, K290E, K290H, K290L, K290N, K290Q, K290R, K290S, K290Y, P291G, P291Q, P291R, R292I, R292L, E293A, E293D, E293G, E293M, E293Q, E293S, E293T, E294A, E294G, E294P, E294Q, E294R, E294T, E294V, Q295I, Q295M, Y296H, S298A, S298R, Y300I, Y300V, Y300W, R301A, R301M, R301P, R301S, V302A, V302F, V302L, V302M, V302R, V302S, V303S, V303Y, S304T, V305A, V305F, V305I, V305L, V305R and V305S of the Fc fragment, wherein the numbering is that of the EU index or equivalent in Kabat.

Amatoxins (AMAs) are lethal toxins found in a variety of mushroom species. Detection methods are needed to determine the occurrence of AMAs in mushroom species, often suspected in mushroom poisonings. Provided herein are novel, sensitive monoclonal antibodies (mAbs) detection and purification techniques utilizing the mAbs that show selectivity for α-amanitin (α-AMA), β-amanitin (β-AMA) and γ-amanitin (γ-AMA).

Amatoxins (AMAs) are lethal toxins found in a variety of mushroom species. Detection methods are needed to determine the occurrence of AMAs in mushroom species, often suspected in mushroom poisonings. Provided herein are novel, sensitive monoclonal antibodies (mAbs) detection and purification techniques utilizing the mAbs that show selectivity for α-amanitin (α-AMA), β-amanitin (β-AMA) and γ-amanitin (γ-AMA).

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 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 invention relates to the composition and method of preparing an immunogen designated as I-spga consisting of a complex antigen prepared from 18 to 26 species of pathogenic microorganisms isolated from patients, inactivated with binary ethyleneamine (BEI) and formalin, diluted in a SPGA immunopotentiator mixed with QS-21 adjuvant. By inoculating the hens with the I-spga immunogen, hyperimmune eggs (Immunospga) are obtained which contain immunologically active proteins specific to the 18-26 antigens used for immunization. The immune response of the hens is specific to the used antigens by amplification of the antigenic signal by the SPGA immunopotentiator and due to a special immunization program that allows the immune system to act complex and intense: The I-spga complex antigen contains 18-26 microorganisms isolated from patients, bacterial bodies, components from bodies obtained by ultrasonography, cilia, exotoxins, endotoxins, spores, viruses, fungi or yeasts. This pathogenic material is inactivated with BEI and formalin. The I-spga antigen is of three types. The standard I-spga antigen is composed of 18 to 24 antibiotic-resistant bacterial species isolated from patients in Romania. The specific I-spga complex antigen is composed of the I-spga complex antigen containing a mixture of 7-9 strains from a single species of bacteria, fungi or yeasts isolated from patients in Romania mixed with SPGA and QS-21, used for inoculation of hens previously immunized with standard I-spga antigen. The personalized I-spga antigen is composed of patient-derived pathological material containing cellular debris and pathogenic germs inactivated with BEI and formalin and mixed with SPGA and QS-21 and is used to immunize hens previously immunized with the standard I-spga antigen. This now patented technology encompasses a new generation of biological products in which the immune response of the hens to different groups of parenterally inoculated antigens at different time intervals is overlapping. Chicken response is uniform and additional administration of immunogens and SPGA as an immunopotentiator amplifies the antigenic signal and immune response. The I-spga immunogen as well as the immune response contain two markers, G and A, which identify the I-spga antigen used for immunization against the antigens used to produce the Imunoinstant group bio-preparations or similar products. The I-spga immunogen is used to immunize the hens for obtaining immunologically active proteins that can be used to treat immune deficiencies, psoriasis, epidermolysis bullosa, other dermatitises, nosocomial infections, antibiotic-resistant infections in the urinary system of children

The present invention is directed to antibodies binding to and neutralizing Candida and methods for use thereof.

The present invention is directed to antibodies binding to and neutralizing Candida and methods for use thereof.