The present specification discloses SNAP-25 compositions, methods of making α-SNAP-25 antibodies that bind an epitope comprising a carboxyl-terminus at the P.sub.1 residue from the BoNT/A cleavage site scissile bond from a SNAP-25 cleavage product, α-SNAP-25 antibodies that bind an epitope comprising a carboxyl-terminus at the P.sub.1 residue from the BoNT/A cleavage site scissile bond from a SNAP-25 cleavage product, methods of detecting BoNT/A activity, and methods of detecting neutralizing α-BoNT/A antibodies.

The present invention relates to a novel endoprotease, mutants thereof having binding but lacking or having reduced hydrolyzing activity, and use in methods of studying and isolating O-linked glycoproteins.

The present invention provides a method for detecting and assaying Clostridium neurotoxins and identification of serotypes of botulinum neurotoxins in various food matrices and clinical samples. This method is also used for detection of BoNT inside the neuronal and epithelial cells. The method comprises detecting and assaying the presence of a Clostridium neurotoxin in a sample by: exposing the sample containing a Clostridium neurotoxin to a sample comprising a novel SNAMPXIN/SNAMP universal recombinant substrate fusion protein capable of producing a detectable FRET, following cleavage; detecting and assaying the presence of the Clostridium neurotoxin by measuring a change in the energy transfer or the luminescence signal; and detecting and assaying an electrophoretic mobility pattern of one or more cleaved protein bands or a degraded protein, using a high throughput automated system to identify the different serotypes of the Clostridium neurotoxin. SNAMPXIN/SNAMP is formed from parts of BoNT substrates SNAP-25 and VAMP.

The present invention relates to a novel endoprotease, mutants thereof having binding but lacking or having reduced hydrolyzing activity, and use in methods of studying and isolating O-linked glycoproteins.

Disclosed herein is a method for identifying and treating a Streptococcus pyogenes (group A Streptococcus, GAS) infection in a subject. The method mainly includes determining the presence of endopeptidase O (PepO) protein in the biological sample; and administering an effective amount of an anti-infective agent to the subject to ameliorate symptoms associated with the GAS infection if the PepO protein is present in the biological sample.

Provided herein is a large immuno-sorbent surface area assay (ALISSA) for the rapid and sensitive detection of botulinum neurotoxins (BoNTs) and anthrax toxin. This assay is designed to capture a low number of toxin molecules and to measure their intrinsic protease activity via conversion of a fluorogenic or luminescent substrate. Also provided herein are novel peptides that can be specifically cleaved by BoNT and novel peptides that are resistant to cleavage by BoNT. The combination of these cleavable and control peptides can be used for implementation of an exemplary ALISSA used to specifically detect BoNT enzymatic activity. Furthermore, the ALISSA as described herein may also be used in a column based format for use in a high-throughput system for testing large quantities of samples.

A method for making a population of cells that are highly sensitive to clostridial neurotoxin, the method comprising: (a) contacting recombinant cells that express an indicator protein with clostridial neurotoxin; and (b) following such contact, selecting the cells that exhibit cleavage of the indicator protein. A cell from the population produced using the aforementioned method. An assay for determining the activity of a modified or recombinant neurotoxin comprising contacting such a cell with the modified or recombinant neurotoxin under conditions and for a period of time sufficient to allow the protease domain of a wild-type clostridial neurotoxin to cleave the indicator protein in the cell and determining the presence of product resulting from the cleavage of the indicator protein.

Compositions and methods are disclosed that provide a rapid, sensitive, and accurate cell-based assay for enzyme activity, particularly for enzyme activities associated with botulinum toxins. A cell is provided that expresses a construct that includes an anchor region, a cleavage site, and a reporting region having two or more identical reporter peptides. Enzymatic activity at the cleavage site releases the reporter region into the cytosol, where multiple degradation events occur. The observed change in the signal is proportional to the enzymatic activity.

Methods, compositions and kits are provided for treating a subject exposed to or at risk for exposure to a disease agent, methods, compositions and kits having a pharmaceutical composition including at least one recombinant binding protein or a source of expression of the binding protein, wherein the binding protein neutralizes at least one or a plurality of disease agents that are toxins, for example at least one of a Botulinum toxin or an Anthrax toxin.

The present specification discloses SNAP-25 compositions, methods of making α-SNAP-25 antibodies that bind an epitope comprising a carboxyl-terminus at the P.sub.1 residue from the BoNT/A cleavage site scissile bond from a SNAP-25 cleavage product, α-SNAP-25 antibodies that bind an epitope comprising a carboxyl-terminus at the P.sub.1 residue from the BoNT/A cleavage site scissile bond from a SNAP-25 cleavage product, methods of detecting BoNT/A activity, and methods of detecting neutralizing α-BoNT/A antibodies.