Literature DB >> 12770717

Novel protein vaccine candidates against Group B streptococcal infection identified using alkaline phosphatase fusions.

Martin J G Hughes1, Rebecca Wilson, Joanne C Moore, Jonathan D Lane, Richard J Dobson, Phillip Muckett, Zabin Younes, Philippa Pribul, Andrew Topping, Robert G Feldman, Joseph D Santangelo.   

Abstract

Using an alkaline phosphatase-based genetic screening method, we identified a number of proteins that are potentially located on the outer surface of Group B streptococcus (Streptococcus agalactiae). In an enzyme-linked immunosorbent assay, antisera raised against two of the proteins, the streptococcal yutD homologue and a subunit of an ABC transporter, recognised clinically important serotypes of Group B streptococcus. In a neonatal rat model, purified IgG from the sera conferred significant levels of protection against a lethal challenge infection. The proteins identified show potential as protein subunit candidates for vaccines against Group B streptococcal disease in neonates.

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Year:  2003        PMID: 12770717     DOI: 10.1016/S0378-1097(03)00310-0

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  3 in total

Review 1.  ATP-binding cassette transporters are targets for the development of antibacterial vaccines and therapies.

Authors:  Helen S Garmory; Richard W Titball
Journal:  Infect Immun       Date:  2004-12       Impact factor: 3.441

Review 2.  Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens.

Authors:  Gunnar Lindahl; Margaretha Stålhammar-Carlemalm; Thomas Areschoug
Journal:  Clin Microbiol Rev       Date:  2005-01       Impact factor: 26.132

Review 3.  How Zinc-Binding Systems, Expressed by Human Pathogens, Acquire Zinc from the Colonized Host Environment: A Critical Review on Zincophores.

Authors:  Denise Bellotti; Magdalena Rowińska-Żyrek; Maurizio Remelli
Journal:  Curr Med Chem       Date:  2021       Impact factor: 4.740

  3 in total

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