Smidt M.,Intercell |
Battig P.,Karolinska Institutet |
Verhaegh S.J.C.,Erasmus University Rotterdam |
Niebisch A.,Intercell |
And 12 more authors.
PLoS ONE | Year: 2013
Moraxella catarrhalis is one of the three most common causative bacterial pathogens of otitis media, however no effective vaccine against M. catarrhalis has been developed so far. To identify M. catarrhalis vaccine candidate antigens, we used carefully selected sera from children with otitis media and healthy individuals to screen small-fragment genomic libraries that are expressed to display frame-selected peptides on a bacterial cell surface. This ANTIGENome technology led to the identification of 214 antigens, 23 of which were selected by in vitro or in vivo studies for additional characterization. Eight of the 23 candidates were tested in a Moraxella mouse pulmonary clearance model, and 3 of these antigens induced significantly faster bacterial clearance compared to adjuvant or to the previously characterized antigen OmpCD. The most significant protection data were obtained with the antigen MCR_1416 (Msp22), which was further investigated for its biological function by in vitro studies suggesting that Msp22 is a heme binding protein. This study comprises one of the most exhaustive studies to identify potential vaccine candidate antigens against the bacterial pathogen M. catarrhalis. © 2013 Smidt et al. Source
Eucodis Bioscience Gmbh | Date: 2013-06-12
The present invention relates to the use of a secreted fungal catalase, for hydrogen-peroxide neutralization in growth media for the detection of microorganisms as well as to a method for detecting microorganisms in hydrogen peroxide-bearing aerosol or on a hydrogen peroxide bearing surface, said method comprising contacting said aerosol or surface with a growth medium comprising a secreted fungal catalase, and detecting growth of microorganisms in said medium.
O'Neill M.,Biocatalysis Group |
Beecher D.,Biocatalysis Group |
Mangan D.,Biocatalysis Group |
Rowan A.S.,Biocatalysis Group |
And 5 more authors.
Tetrahedron Asymmetry | Year: 2012
A novel, commercially available lipase enzyme panel performing kinetic bioresolutions of a number of secondary alcohols is reported. The secondary alcohols that have been chosen are known from the literature to be particularly challenging substrates to resolve. Following initial screening, four co-solvents were investigated for each lead enzyme in an effort to assess their tolerance to common organic solvents. The superiority of these novel enzymes over lipase B from Candida antarctica (CALB) has been demonstrated. © 2012 Elsevier Ltd. All rights reserved. Source