A stimuli-responsive surface (3) comprising a substrate (20) on which is located a switchable molecule (2) which has a functional moiety (22) associated therewith, wherein the switchable molecule (2) has a first equilibrium state (2A) in which access to the functional moiety (22) is inhibited and a second stimulated state (2B), in which access to the functional moiety (22) is permitted.

Disclosed herein are methods of detecting microbial infection in mammalian subjects comprising treatment of a sample and detection of galactofuranose (galF)-containing antigenic components utilizing monoclonal antibodies. The methods disclosed provide for pretreatment of biological samples, such as urine samples, to maximize detection of galF antigens and improvement of sensitivity of galF antigen detection assays. The methods include minimizing intelectin-1 binding to galF antigens and improvement of monoclonal antibody binding. The detection methods are useful for identifying the presence of microbial antigens related to bacterial, fungal, and parasitic pathogens, including Streptococcus pneumoniae, Aspergillus species, Fusarium species, Coccidioides species, Cryptococcus species, Histoplasma species, and Leishmania species.

The present disclosure relates to a method of diagnosing Lyme disease in a subject comprising measuring the level of B. burgdorferi peptidoglycan or the level of an antibody that specifically binds to B. burgdorferi peptidoglycan (“anti-peptidoglycan agent”). The present disclosure also relates to a method of treating a Lyme disease in a subject in need thereof comprising administering to the subject an antagonist against B. burgdorferi peptidoglycan (e.g., an anti-peptidoglycan antibody or a peptidoglycan-specific hydrolase). Antagonists (e.g., anti-peptidoglycan antibodies) suitable for the present methods are also disclosed.

The invention relates to carbohydrate ligands presenting the minimal Human Natural Killer-1 (HNK-1) epitope that bind to anti-MAG (myelin-associated glycoprotein) IgM antibodies, and their use in diagnosis as well as for the treatment of anti-MAG neuropathy. In particular, the invention relates to disaccharides of formula (I) and (II) wherein Z is optionally substituted phenyl, heteroaryl, arylcarbonyl, or heteroarylmethyl, and to therapeutically acceptable polymers comprising a multitude of substituents of formula (I) and/or formula (II), wherein Z is a bifunctional linker connecting the disaccharides to the polymer backbone. ##STR00001##

Antibody molecules that specifically bind to APRIL are disclosed. The antibody molecules can be used to treat, prevent, and/or diagnose disorders, such as IgA nephropathy.

Compositions and methods related to transgenic glyphosate tolerant Brassica plants are provided. Specifically, the present invention provides Brassica plants having a DP-073496-4 event which imparts tolerance to glyphosate. The Brassica plant harboring the DP-073496-4 event at the recited chromosomal location comprises genomic/transgene junctions within SEQ ID NO: 2 or with genomic/transgene junctions as set forth in SEQ ID NO: 12 and/or 13. The characterization of the genomic insertion site of the event provides for an enhanced breeding efficiency and enables the use of molecular markers to track the transgene insert in the breeding populations and progeny thereof. Various methods and compositions for the identification, detection, and use of the event are provided.

In alternative embodiments, the invention provides vaccines, pharmaceutical compounds and formulations for diagnosing, preventing, treating or ameliorating Group A Streptococcus (GAS), Group C Streptococcus (GCS), or Group A Streptococcus (GGS), infections, or other pathogenic Streptococcus infections. In alternative embodiments, the invention provides compositions such as diagnostic tests, assays, immunoassays and test strips, and methods, for detecting or diagnosing the presence of a Streptococcal infection, e.g., Group A Streptococcus (GAS), Group C Streptococcus (GCS), or Group A Streptococcus (GGS), infections, or other pathogenic Streptococcus infections.

The present document describes an antibody or an antigen-binding fragment that bind to O-glycan mucin-type glycoprotein MUC16 comprising three variable heavy domain complementarity determining regions (CDR)(CDR H1, H2 and H3), and three variable lighy domain CDR (CDR L1, L2 and L3). The present invention also relates to pharmaceutical compositions, nucleic acid vectors, cells comprising the nucleic acid vectors, and methods of inhibiting tumor growth of a tumor expressing O-glycan mucin-type glycoprotein MUC16.

The invention provides antibodies that specifically bind to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine expressed by a cancer cell or an inflammatory cell. Also provided are compositions including these antibodies, as well as polynucleotides, vectors, host cells, and methods useful for production thereof. Further provided are methods and kits for treating or preventing cancer in an individual by administering to the individual an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine, optionally in combination with another anti-cancer agent. Still further provided are methods and kits for treating or preventing gastrointestinal disease in an individual by administering to the individual an antibody that specifically binds to an epitope containing N-acetylglucosamine or N-acetyl-galactosamine. Yet further provided are methods and kits for detecting the presence of cancer cells in an individual including an antibody that specifically binds to an epitope containing N-acetylglucosamine and/or N-acetyl-galactosamine.

There is provided a method for measuring an antigen, comprising: providing a solution containing an antigen; providing a first antibody that specifically recognizes the antigen and is bound to a magnetic carrier; providing a second antibody that specifically recognizes the antigen and is modified with an oxidase; providing (a substrate liquid including) a substrate which reacts with the oxidase; allowing the first antibody to recognize the antigen; allowing the second antibody to recognize the antigen; using a magnetic field to capture an antigen-antibody complex of the antigen recognized by the first antibody and the second antibody in the magnetic field; washing the antigen-antibody complex while it is captured in the magnetic field; reacting the substrate with the antigen-antibody complex to produce hydrogen peroxide; and measuring the hydrogen peroxide.