Abstract: Herein are provided anti-EGFR single domain antibodies (sdAb) prepared by immunizing a llama with recombinant human EGFRvIII. VHH antibodies specific to EGFR were isolated. The example antibodies initially produced comprise CDR1, CDR2, and CDR3 sequences corresponding, respectively to SEQ NOs: 1-3, 4-6, 7-9, 10-12, 13-15, 16-18, 19-21, 22-24, 25-27, 28-30, 31-33, 34-36, 37-39, 40-42, 43-45, and 46-48; and related sequences, including humanized variants. Also provided are multivalent antibodies comprising any one of the sdAbs, including bispecific T-cell engagers, bispecific killer cell engagers (BiKEs), and trispecific killer cell engagers (TriKEs). Also described are chimeric antigen receptors (CARs) for CAR-T therapy comprising any one of the aforementioned sdAbs. Uses of these molecules in the treatment of cancer are also described, in particularly EGFR-high cancers. Hinge lengths may be selected to achieve desired activities, such as high activity or high selectivity for target vs. non-target cells.

Abstract: The present document describes an antibody or an antigen-binding fragment that bind to serum albumin comprising three complementarity determining regions (CDR1, CDR2 and CDR3), for half-life extension of biologics. The present invention also relates to pharmaceutical compositions, nucleic acid vectors, cells comprising the nucleic acid vectors, and methods of removing molecules from serum.

Abstract: A chimeric antigen receptor (CAR) that binds to CEACAM6, an epitope or fragment thereof, or a variant thereof.

Abstract: Polypeptides with biophysical properties such as solubility, stability, high expression, monomericity, binding specificity or non-aggregation, including monomeric human heavy and light chain variable domains (VHs and VLs), are identified using a high throughput method for screening polypeptides, comprising the steps of obtaining a phage display library, allowing infection of a bacterial lawn by the library phage, and identifying phage which form larger than average plaques on the bacterial lawn. Sequences of monomeric human VHs and VLs are identified, which may be useful for immunotherapy or as diagnostic agents. Multimer complexes of human VHs and VLs are also identified. The VHs and VLs identified may be used to create further libraries for identifying additional polypeptides. Further, the VHs and VLs may be subjected to DNA shuffling to select for improved biophysical properties.

Abstract: The present document describes an antibody or an antigen-binding fragment that bind to serum albumin comprising three complementarity determining regions (CDR1, CDR2 and CDR3), for half-life extension of biologics. The present invention also relates to pharmaceutical compositions, nucleic acid vectors, cells comprising the nucleic acid vectors, and methods of removing molecules from serum.

Abstract: Polypeptides with biophysical properties such as solubility, stability, high expression, monomericity, binding specificity or non-aggregation, including monomeric human heavy and light chain variable domains (VHs and VLs), are identified using a high throughput method for screening polypeptides, comprising the steps of obtaining a phage display library, allowing infection of a bacterial lawn by the library phage, and identifying phage which form larger than average plaques on the bacterial lawn. Sequences of monomeric human VHs and VLs are identified, which may be useful for immunotherapy or as diagnostic agents. Multimer complexes of human VHs and VLs are also identified. The VHs and VLs identified may be used to create further libraries for identifying additional polypeptides. Further, the VHS and VLs may be subjected to DNA shuffling to select for improved biophysical properties.

Abstract: The present invention is directed to Clostridium difficile toxin-specific antibodies, compositions, and uses thereof. The anti-toxin antibodies may be specific for TcdA. The invention also includes methods of treating a Clostridium difficile infection, methods of capturing Clostridium difficile toxins, and methods of detecting Clostridium difficile toxins.

Abstract: The present invention provides a single domain antibody (sdAb) scaffold comprising one or more than one non-canonical disulfide bond in the framework region (FR). The one or more than one non-canonical disulfide bond may be formed between cysteines introduced by mutations in FR2 and FR3. In the case where the sdAb scaffold is a VH, the Cys may be introduced at any one of positions 47-49 and any one of positions 67-71, based on Kabat numbering; in one example, the Cys may be introduced at positions 49 and 69, based on Kabat numbering. In the case where the sdAb scaffold is a VL, the Cys residues may be introduced at any one of positions 46-49 and any one of positions 62-66, based on Kabat numbering; in one example, the Cys residues may be introduced at positions 48 and 64, based on Kabat numbering.

Abstract: Campylobacter jejuni is a leading cause of bacterial food-borne diseases in humans, ranging from acute diarrheal disease to neurological disorders. An isolated or purified antibody or fragment thereof specific to C. jejuni is described. The antibody or fragment thereof binds to a flagellar protein and reduces motility of C. jejuni. The antibody or fragment thereof is derived from a heavy chain IgG variable domain fragment (VHH) of a camelid animal immunized with C. jejuni flagellar protein. A multivalent form, as well as a phage format, of the antibody or fragment thereof is described. Methods of reducing presence of C. jejuni in an animal or an animal environment, methods and formulations for treating C. jejuni infection, and method of detecting C. jejuni are also described.

Abstract: Polypeptides with desirable biophysical properties such as solubility, stability, high expression, monomericity, binding specificity or non-aggregation, including monomeric human VHs and VLs, are identified using a high throughput method for screening polypeptides, comprising the steps of obtaining a phage display library, allowing infection of a bacterial lawn by the library phage, and identifying phage which form larger than average plaques on the bacterial lawn. Sequences of monomeric human VHs and VLs are identified, which may be useful for immunotherapy or as diagnostic agents. Multimer complexes of human VHs and VLs are also identified. The VHs and VLs identified may be used to create further libraries for identifying additional polypeptides. Further, the VHs and VLs may be subjected to DNA shuffling to select for improved biophysical properties.

Abstract: Polypeptides with desirable biophysical properties such as solubility, stability, high expression, monomericity, binding specificity or non-aggregation, including monomeric human VHs and VLs, are identified using a high throughput method for screening polypeptides, comprising the steps of obtaining a phage display library, allowing infection of a bacterial lawn by the library phage, and identifying phage which form larger than average plaques on the bacterial lawn. Sequences of monomeric human VHs and VLs are identified, which may be useful for immunotherapy or as diagnostic agents. Multimer complexes of human VHs and VLs are also identified. The VHs and VLs identified may be used to create further libraries for identifying additional polypeptides. Further, the VHs and VLs may be subjected to DNA shuffling to select for improved biophysical properties.

Abstract: Campylobacter jejuni is a leading cause of bacterial food-borne diseases in humans, ranging from acute diarrheal disease to neurological disorders. An isolated or purified antibody or fragment thereof specific to C. jejuni is described. The antibody or fragment thereof binds to a flagellar protein and reduces motility of C. jejuni. The antibody or fragment thereof is derived from a heavy chain IgG variable domain fragment (VHH) of a camelid animal immunized with C. jejuni flagellar protein. A multivalent form, as well as a phage format, of the antibody or fragment thereof is described. Methods of reducing presence of C. jejuni in an animal or an animal environment, methods and formulations for treating C. jejuni infection, and method of detecting C. jejuni are also described.

Abstract: The present invention is directed to Clostridium difficile toxin-specific antibodies, compositions, and uses thereof. The anti-toxin antibodies may be specific for either TcdA or TcdB. The invention also includes methods of treating a Clostridium difficile infection, methods of capturing Clostridium difficile toxins, and methods of detecting Clostridium difficile toxins.

Abstract: Campylobacter jejuni is a leading cause of bacterial food-borne diseases in humans, ranging from acute diarrheal disease to neurological disorders. An isolated or purified antibody or fragment thereof specific to C. jejuni is described. The antibody or fragment thereof binds to a flagellar protein and reduces motility of C. jejuni. The antibody or fragment thereof is derived from a heavy chain IgG variable domain fragment (VHH) of a camelid animal immunized with C. jejuni flagellar protein. A multivalent form, as well as a phage format, of the antibody or fragment thereof is described. Methods of reducing presence of C. jejuni in an animal or an animal environment, methods and formulations for treating C. jejuni infection, and method of detecting C. jejuni are also described.

Abstract: A chimeric antigen receptor (CAR) that binds to CEACAM6, an epitope or fragment thereof, or a variant thereof.

Abstract: The present invention is directed to Clostridium difficile toxin-specific antibodies, compositions, and uses thereof. The anti-toxin antibodies may be specific for either TcdA or TcdB. The invention also includes methods of treating a Clostridium difficile infection, methods of capturing Clostridium difficile toxins, and methods of detecting Clostridium difficile toxins.

Abstract: The present invention provides a single domain antibody (sdAb) scaffold comprising one or more than one non-canonical disulfide bond in the framework region (FR). The one or more than one non-canonical disulfide bond may be formed between cysteines introduced by mutations in FR2 and FR3. In the case where the sdAb scaffold is a VH, the Cys may be introduced at any one of positions 47-49 and any one of positions 67-71, based on Kabat numbering; in one example, the Cys may be introduced at positions 49 and 69, based on Kabat numbering. In the case where the sdAb scaffold is a VL, the Cys residues may be introduced at any one of positions 46-49 and any one of positions 62-66, based on Kabat numbering; in one example, the Cys residues may be introduced at positions 48 and 64, based on Kabat numbering.

Abstract: The present invention provides a single domain antibody (sdAb) scaffold comprising one or more than one non-canonical disulfide bond in the framework region (FR). The one or more than one non-canonical disulfide bond may be formed between cysteines introduced by mutations in FR2 and FR3. In the case where the sdAb scaffold is a VH, the Cys may be introduced at any one of positions (47-49) and any one of positions (67-71), based on Kabat numbering; in one example, the Cys may be introduced at positions (49) and (69), based on Kabat numbering. In the case where the sdAb scaffold is a VL, the Cys residues may be introduced at any one of positions 46-49 and any one of positions (62-66), based on Kabat numbering; in one example, the Cys residues may be introduced at positions (48 and 64), based on Kabat numbering.

Abstract: Polypeptides with desirable biophysical properties such as solubility, stability, high expression, monomericity, binding specificity or non-aggregation, including monomeric human VHs and VLs, are identified using a high throughput method for screening polypeptides, comprising the steps of obtaining a phage display library, allowing infection of a bacterial lawn by the library phage, and identifying phage which form larger than average plaques on the bacterial lawn. Sequences of monomeric human VHs and VLs are identified, which may be useful for immunotherapy or as diagnostic agents. Multimer complexes of human VHs and VLs are also identified. The VHs and VLs identified may be used to create further libraries for identifying additional polypeptides. Further, the VHs and VLs may be subjected to DNA shuffling to select for improved biophysical properties.

Abstract: Campylobacter jejuni is a leading cause of bacterial food-borne diseases in humans, ranging from acute diarrheal disease to neurological disorders. An isolated or purified antibody or fragment thereof specific to C. jejuni is described. The antibody or fragment thereof binds to a flagellar protein and reduces motility of C. jejuni. The antibody or fragment thereof is derived from a heavy chain IgG variable domain fragment (VHH) of a camelid animal immunized with C. jejuni flagellar protein. A multivalent form, as well as a phage format, of the antibody or fragment thereof is described. Methods of reducing presence of C. jejuni in an animal or an animal environment, methods and formulations for treating C. jejuni infection, and method of detecting C. jejuni are also described.