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Outer membrane protein B1 of Moraxella catarrhalis
| Details |
Inventors: Campagnari, Anthony A.;
Assignee: The Research Foundation of the State University of New York (Amherst, NY)
Primary Examiner: Housel; James C.
Assistant Examiner: Ryan; V.
Attorney, Agent or Firm: Hodgson, Russ, Andrews, Woods & Goodyear, LLP
An isolated and purified outer membrane protein B1, and peptides formed therefrom, of Moraxella catarrhalis are described. A method for the isolation and purification of outer membrane protein B1 from a bacterial strain that produces B1 protein, e.g. Moraxella catarrhalis, comprises growing the bacteria in culture in iron-depleted medium to enhance the expression of the B1 protein, harvesting the bacteria from the culture, extracting from the harvested bacteria a preparation substantially comprising an outer membrane protein preparation, contacting the outer membrane preparation with an affinity matrix containing immobilized transferrin wherein B1 protein binds to the transferrin, and eluting the bound B1 protein from the transferrin. Disclosed are the uses of the B1 protein as an immunogen for vaccine formulations, and as antigens in diagnostic immunoassays. |
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DETAILED DESCRIPTION OF THE INVENTION Definitions By the terms "OMP B1", and "B1 protein" are meant, for the purposes of the specification and claims, to refer to a protein having the following distinguishing and functional characteristics: (a) the protein is substantially expressed by a bacterial strain that produces B1 protein, e.
g.
, M.
catarrhalis, and is detectable in the outer membrane of the bacterial strain, under iron-limiting conditions, i.
e.
, when the organism is growing in an iron-limited environment; (b) expression of the protein appears to become repressed when the bacterial strain is grown in an iron-rich environment; (c) the protein has an apparent molecular mass of approximately 81 to 84 kDa as determined by SDS-PAGE; (d) the protein, in its native conformation in the outer membrane, contains surface-exposed epitopes; and (e) the protein binds human transferrin, particularly iron-saturated transferrin.
Additionally, in the N-terminal portion of the amino acid sequence of the protein may be the nine amino acids in sequence LeuGlnGlyGlyPheTyrGlyProLys (SEQ ID NO:1).
A peptide with this sequence may be synthesized using any of the methods known to those skilled in the art for synthesizing peptides.
By the terms "isolated and purified" and "substantially free from other outer membrane proteins and components" is meant, for the purposes of the specification and claims, to refer to a B1 protein preparation that appears to be at least approximately 80% pure, and may be up to approximately 99% pure, as, for example, determined by SDS-PAGE.
By the term "individual" is meant, for the purposes of the specification and claims to refer to any mammal, especially humans.
By the term "iron-repressible proteins" is meant, for the purposes of the specification and claims to refer to outer membrane proteins which are expressed in detectable amounts when M.
catarrhalis is grown in iron-depleted or iron-limiting conditions, but which detectable expression is repressed by placing the iron-starved bacteria into an iron-replete environment
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