Monoclonal antibodies that specifically bind the F1 antigen of Yersinia pestis with high affinity are described. Use of the monoclonal antibodies for the detection of Y. pestis infection and the diagnosis of plague are also described. Immunoconjugates of the monoclonal antibodies and a radionuclide can also be used for the treatment of a Y. pestis infection.

The present invention provides a component having effects in vivo of improving or optimizing the intestinal environment, suppressing intestinal putrefaction, or suppressing alternation of intestinal bacterial growth and/or pathological changes of intestinal bacterial growth in gut microbiota. The invention also provides an active ingredient suitably used for treating intestinal diseases. The invention provides a monoclonal IgA antibody that binds to amino acids 11 to 333 of serine hydroxymethyltransferase.

The invention provides for an isolated antibody that specifically recognizes a galactan-III epitope of the lipopolysaccharide (LPS) O-antigen structure of Klebsiella pneumoniae, which epitope is incorporated in galactan-III repeating units, wherein the galactan-III repeating unit is a branched galactose homopolymer of Formula (I). The invention further provides for a pharmaceutical or diagnostic preparation comprising said antibody, and a method of producing said antibody.

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Embodiments of the present invention provide methods for the treatment or prevention of infection-related immune conditions using compositions comprising IgM.

The present disclosure provides binding proteins (e.g., antibodies or antigen binding fragments thereof) that specifically bind to Klebsiella pneumoniae O2 and induce opsonophagocytic killing of Klebsiella (e.g., Klebsiella pneumoniae) and/or protects mice from a lethal Klebsiella challenge. The present disclosure also provides methods of reducing Klebsiella (e.g., Klebsiella pneumoniae) or treating or preventing Klebsiella (e.g., Klebsiella pneumoniae) infection in a subject comprising administering the Klebsiella pneumoniae O2 binding proteins, (e.g., antibodies or antigen-binding fragments thereof) to the subject.

The invention provides for an isolated antibody that specifically recognizes a galactan-III epitope of the lipopolysaccharide (LPS) O-antigen structure of Klebsiella pneumoniae, which epitope is incorporated in galactan-III repeating units, wherein the galactan-III repeating unit is a branched galactose homopolymer of Formula (I). The invention further provides for a pharmaceutical or diagnostic preparation comprising said antibody, and a method of producing said antibody. ##STR00001##

The present disclosure provides binding proteins (e.g., antibodies or antigen binding fragments thereof) that specifically bind to Klebsiella pneumoniae O1 and induce opsonophagocytic killing of Klebsiella (e.g., Klebsiella pneumoniae). The present disclosure also provides methods of reducing Klebsiella (e.g., Klebsiella pneumoniae) or treating or preventing Klebsiella (e.g., Klebsiella pneumoniae) infection in a subject comprising administering the Klebsiella pneumoniae O1 binding proteins, (e.g., antibodies or antigen-binding fragments thereof) to the subject.

The present invention provides isolated polypeptides isolatable from a Yersinia spp. Also provided by the present invention are compositions that include one or more of the polypeptides, and methods for making and methods for using the polypeptides.

The present invention relates generally to the field of nutrition, health and wellness. In particular the present invention relates to probiotics and ways to increase their effectiveness. One embodiment of the present invention relates to a combination of probiotics with SIgA and possible uses of this combination. For example a use of a composition comprising SIgA and at least one probiotic for the preparation of a product to treat or prevent inflammation is disclosed.

In general, the invention features a novel CBM32-derived affinity scaffold. In certain embodiments, the scaffold comprises two types of regions: constant regions (CRs) and variable loop regions (VLRs) as depicted in the structure in FIG. 1. We have discovered that the CRs provide structural features that enable overall conformational stability while the intervening sequences corresponding to VLRs tolerate amino acid sequence randomization.