Abstract: The invention provides BASB021 polypeptides and polynucleotides encoding BASB021 polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are diagnostic, prophylactic and therapeutic uses.

Abstract: The invention provides BASB010 polypeptides and polynucleotides encoding BASB010 polypeptides and methods for producing such polypeptides by recombinant techniques. Also provided are diagnostic, prophylactic and therapeutic uses.

Abstract: Provided are BASB011 polypeptides and polynucleotides encoding BASB011 polypeptide from Moraxella catarrhalis. Also provided are immunogenic uses.

Abstract: The invention discloses the Moraxella catarrhalis outer membrane protein-106 (OMP106) polypeptide, polypeptides derived therefrom (OMP106-derived polypeptides), nucleotide sequences encoding said polypeptides, and antibodies that specifically bind the OMP106 polypeptide and/or OMP106-derived polypeptides. Also disclosed are immunogenic, prophylactic or therapeutic compositions, including vaccines, comprising OMP106 polypeptide and/or OMP106-derived polypeptides. The invention additionally discloses methods of inducing immune responses to M. catarrhalis and M. catarrhalis OMP106 polypeptides and OMP106-derived polypeptides in animals.

Abstract: A protein from the M. catarrhalis designated the 74 kD protein is isolated and purified. The 74 kD protein has an amino-terminal amino acid sequence which is conserved among various strains of M. catarrhalis. The protein has a molecular weight of approximately 74,9 kD as measured on a 10% SDS-PAGE gel, while its molecular weight as measured by mass spectrometry is approximately 74 kD. The 74 kD protein is used to prepare a vaccine composition which elicits a protective immune response in a mammalian host to protect the host again disease caused by M. catarrhalis.

Abstract: An isolated and purified outer membrane protein of a Moraxella strain, particularly M. catarrhalis, having a molecular mass of about 200 kDa, is provided. The about 200 kDa outer membrane protein as well as nucleic acid molecules encoding the same are useful in diagnostic applications and immunogenic compositions, particularly for in vivo administration to a host to confer protection against disease caused by a bacterial pathogen that produces the about 200 kDa outer membrane protein or produces a protein capable of inducing antibodies in a host specifically reactive with the about 200 kDa outer membrane protein.

Abstract: An isolated and purified outer membrane protein of a Moraxella strain, particularly M. catarrhalis, has a molecular mass of about 200 kDa. The about 200 kDa outer membrane protein as well as nucleic acid molecules encoding the same are useful in diagnostic applications and immunogenic compositions, particularly for in vivo administration to a host to confer protection against disease caused by a bacterial pathogen that produces the about 200 kDa outer membrane protein or produces a protein capable of inducing antibodies in a host specifically reactive with the about 200 kDa outer membrane protein.

Abstract: An isolated and purified outer membrane protein of a Moraxella strain, particularly M. catarrhalis, having a molecular mass of about 200 kDa, is provided. The about 200 kDa outer membrane protein as well as nucleic acid molecules encoding the same are useful in diagnostic applications and immunogenic compositions, particularly for in vivo administration to a host to confer protection against disease caused by a bacterial pathogen that produces the about 200 kDa outer membrane protein or produces a protein capable of inducing antibodies in a host specifically reactive with the about 200 kDa outer membrane protein.

Abstract: A multi-valent immunogenic composition confers protection on an immunized host against infection caused by both Haemophilus influenzae and Moraxella catarrhalis. Such composition comprises at least four antigens comprising at least one antigen from Haemophilus influenzae, and at least one antigen from Moraxella catarrhalis. Three of the antigens are adhesins. High molecular weight (HMW) proteins and Haemophilus influenzae adhesin (Hia) proteins of non-typeable Haemophilus and a 200 kDa outer membrane protein of Moraxella catarrhalis comprise the adhesin components while the other antigen is a non-proteolytic analog of Hin47 protein. Each component does not impair the immunogenicity of the others. The multi-valent immunogenic composition may be combined with DTP component vaccines, which may also include non-virulent poliovirus and PRP-T, to provide a component vaccine without impairment of the immunogenic properties of the other antigens.

Abstract: Described herein is a method for removing toxic lipooligosaccharide (LOS) from outer membranes of Gram-negative cocci, such as Neisseria meningitidis. LOS-depleted outer membranes and LOS-depleted soluble outer membrane proteins can be prepared, which are able to elicit bactericidal antibodies against homologous strains of bacteria. Vaccines and other uses of the preparations are further described.

Abstract: An isolated and purified lactoferrin receptor protein is isolated and purified from bacterial pathogens, including Moraxella and Neisseria, and has a molecular weight of between about 70,000 and about 90,000, as determined by SDS-PAGE. Such lactoferrin receptor protein may be provided in combination with a lactoferrin receptor protein from the bacterial pathogen of a molecular weight of about 100,000 to about 105,000 daltons. The lactoferrin receptor protein may be produced by providing a solubilized membrane preparation from the bacterial pathogen containing lactoferrin receptor proteins, non-lactoferrin receptor proteins and other contaminants, complexing the lactoferrin receptor proteins with lactoferrin and purifying the resulting complexes substantially free from the non-lactoferrin receptor proteins and the other contaminants, and separating the novel lactoferrin receptor protein from the complexes.

Abstract: An isolated and purified lactoferrin receptor protein is isolated and purified from bacterial pathogens, including Moraxella and Neisseria, and has a molecular weight of between about 70,000 and about 90,000, as determined by SDS-PAGE. Such lactoferrin receptor protein may be provided in combination with a lactoferrin receptor protein from the bacterial pathogen of a molecular weight of about 100,000 to about 105,000 daltons. The lactoferrin receptor protein may be produced by providing a solubilized membrane preparation from the bacterial pathogen containing lactoferrin receptor proteins, non-lactoferrin receptor proteins and other contaminants, complexing the lactoferrin receptor proteins with lactoferrin and purifying the resulting complexes substantially free from the non-lactoferrin receptor proteins and the other contaminants, and separating the novel lactoferrin receptor protein from the complexes.

Abstract: An isolated and purified outer membrane protein of a Moraxella strain, particularly M. catarrhalis, has a molecular mass of about 200 kDa. The about 200 kDa outer membrane protein as well as nucleic acid molecules encoding the same are useful in diagnostic applications and immunogenic compositions, particularly for in vivo administration to a host to confer protection against disease caused by a bacterial pathogen that produces the about 200 kDa outer membrane protein or produces a protein capable of inducing antibodies in a host specifically reactive with the about 200 kDa outer membrane protein.

Abstract: An isolated and purified non-denatured transferrin receptor protein of a Moraxella strain, particularly M. catarrhalis, has an apparent molecular mass of about 80 to about 90 kDa, as determined by SDS-PAGE. The transferrin receptor protein or a fragment analog thereof is useful in diagnostic applications and immunogenic compositions, particularly for in vivo administration to a host to confer protection against disease caused by a strain of Moraxella.

Abstract: An isolated and purified non-denatured transferrin receptor protein of a Moraxella strain, particularly M. catarrhalis, has an apparent molecular mass of about 80 to about 90 kDa, as determined by SDS-PAGE. The transferrin receptor protein or a fragment analog thereof is useful in diagnostic applications and immunogenic compositions, particularly for in vivo administration to a host to confer protection against disease caused by a strain of Moraxella. The transferrin receptor protein is isolated from strains of Moraxella catarrhalis by a procedure including extraction of agent soluble proteins of a cell mass produced by cultivating the strain under iron-starved conditions. The transferrin receptor protein is selectively solubilized from the extracted cell mass and purified.

Abstract: Purified and isolated nucleic acid molecules are provided which encode lactoferrin receptor proteins of Moraxella, such as M. catarrhalis, or a fragment or an analog of the lactoferrin receptor protein. The nucleic acid sequence may be used to produce recombinant lactoferrin receptor proteins Lbp1, Lbp2 and ORF3 of the strain of Moraxella free of other proteins of the Moraxella strain for purposes of diagnostics and medical treatment. Furthermore, the nucleic acid molecule may be used in the diagnosis of infection.