Researchers from St. Jude and the University of Utah identified extracellular matrix adhesion (Ema) regions of genomic DNA unique to virulent GBS strains. Proteins translated from these regions have a role in mediating adhesion to and invasion of GBS to human epithelial cells. Members of the Ema locus are ubiquitous in GBS and therefore have a role in the prevention of infection by multiple serotypes of GBS. Antibody against these antigens may prevent initial steps in infection and a vaccine that contains Ema and other proteins that prevent colonization of pregnant women and other individuals at increased risk of invasive GBS infection would eliminate most infections.
The human pathogen group B Streptococcus (GBS) produces pilus-like structures encoded in genomic islands with similar organization to pathogenicity islands. 3 different types have been identified in GBS, at least 1 of which is present in all isolates; and the researchers demonstrated that recombinant pilus proteins protect mice with GBS and are potential vaccine candidates.
Patents covering EmaA DNA, proteins and antibodies and EmaE proteins, and their uses are available for licensing.
Extracellular Matrix Adhesin, EmaA, EmaE, Group B Streptococcus, Vaccine.
Granted Patents or Published Applications
US Patents 7,128,919; 7,645,577; 7,892,552; 8,529,912.
Related Scientific References
Maione et al., "Identification of a Universal Group B Streptococcus Vaccine by Multiple Genome Screen," Science 2005 309:148-150 and Supporting Online Material.
Patti et al., "Critical Residues in the Ligand-binding Site of the Staphylococcus aureus Collagen-binding Adhesion (MSCRAMM)," J. Biol. Chem. 1995 270(20):12005-12011
Rich et al., "Ace Is a Collagen-binding MSCRAMM from Enterococcus faecalis," J. Biol. Chem. 1999 274(38):26939-26945
Yeung M K and Cisar J O, Sequence homology between the subunits of two immunologically and functionally distinct types of fimbrae of Actinomyces spp. The Journal of Bacteriology 172:2462-8, 1990.
Li T, Johansson I, Hay D I and Stromberg N. Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins. Infection and Immunity 67:2053-2059, 1999.
Jaffe J, Natanson-Yaron S, Caparon M G and Hanski E. Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains Molecular Microbiology 21:2720-728, 1996.
Rocha C L and Fischetti V A. Identification and characterization of a novel fibronectin-binding protein on the surface of Group A streptococci. Infection and Immunity 66:1482-1491, 1999.
Schneewind O, Jones K F and Fischetti V A. Sequence and structural characteristics of the trypsin-resistant T6 protein of group A streptococci. The Journal of Bacteriology 172:3310-7, 1990.
If you are interested in licensing this technology in one of these or any other fields, please contact us. Contact: email@example.com
Contact the Office of Technology Licensing (Phone: 901-595-2342, Fax: 901-595-3148) for more information.