Abstract
Safe recombinant vaccines, based on a small number of antigenic proteins, are emerging as the most attractive, cost-effective solution against infectious diseases. In the present work, we confirmed previous data from our laboratory showing that whole viable bacterial cell treatment with proteases followed by the identification of released peptides by mass spectrometry is the method of choice for the rapid and reliable identification of vaccine candidates in Gram-positive bacteria. When applied to the Group B Streptococcus COH1 strain, 43 surface-associated proteins were identified, including all the protective antigens described in the literature as well as a new protective antigen, the cell wall-anchored protein SAN_1485 belonging to the serine-rich repeat protein family. This strategy overcomes the difficulties so far encountered in the identification of novel vaccine candidates and speeds up the entire vaccine discovery process by reducing the number of recombinant proteins to be tested in the animal model.
Highlights
When applied to the Group B Streptococcus COH1 strain, 43 surface-associated proteins were identified, including all the protective antigens described in the literature as well as a new protective antigen, the cell wall-anchored protein SAN_1485 belonging to the serine-rich repeat protein family
We have recently proposed a novel proteomics-based approach, which has allowed the identification of Group A Streptococcus (GAS)1 proteins having domains protruding out of the bacterial surface [7]
As in the case of GAS [7], the proteins identified comprise all protective antigens so far described in the literature [6, 17,18,19,20,21,22,23,24,25,26] as well as a new antigen, SAN_1485, which appears to be highly protective in the active maternal immunization mouse model
Summary
IDENTIFICATION OF A NOVEL PROTECTIVE ANTIGEN FOR GROUP B STREPTOCOCCUS HYPERVIRULENT STRAIN COH1□S. As in the case of GAS [7], the proteins identified comprise all protective antigens so far described in the literature [6, 17,18,19,20,21,22,23,24,25,26] as well as a new antigen, SAN_1485, which appears to be highly protective in the active maternal immunization mouse model These data confirm the effectiveness of protease digestion coupled to mass spectrometry for the identification of surface-exposed antigens in Gram-positive bacteria and demonstrate the power of this technology for the rapid discovery of new vaccines
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