Conserved anchorless surface proteins as group A streptococcal vaccine candidates.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Gillen, Christine M
Cole, Jason N
Cork, Amanda J
Djordjevic, Steven P
Cordwell, Stuart J
Sriprakash, Kabada S
Chhatwal, G S
Margarit, Immaculada Y R
Batzloff, Michael R
Walker, Mark J
MetadataShow full item record
AbstractStreptococcus pyogenes (group A Streptococcus (GAS)) causes ∼700 million human infections each year, resulting in over 500,000 deaths. The development of a commercial GAS vaccine is hampered by the occurrence of many unique GAS serotypes, antigenic variation within the same serotype, differences in serotype geographical distribution, and the production of antibodies cross-reactive with human tissue that may lead to autoimmune disease. Several independent studies have documented a number of GAS cell wall-associated or secreted metabolic enzymes that contain neither N-terminal leader sequences nor C-terminal cell wall anchors. Here, we applied a proteomic analysis of serotype M1T1 GAS cell wall extracts for the purpose of vaccine development. This approach catalogued several anchorless proteins and identified two protective vaccine candidates, arginine deiminase and trigger factor. These surface-exposed enzymes are expressed across multiple GAS serotypes exhibiting ≥99% amino acid sequence identity. Vaccine safety concerns are alleviated by the observation that these vaccine candidates lack human homologs, while sera from human populations suffering repeated GAS infections and high levels of autoimmune complications do not recognize these enzymes. Our study demonstrates anchorless cell surface antigens as promising vaccine candidates for the prevention of GAS disease.
CitationConserved anchorless surface proteins as group A streptococcal vaccine candidates. 2012, 90 (10):1197-207 J. Mol. Med.
AffiliationSchool of Biological Sciences, University of Wollongong, Wollongong, NSW, 2522, Australia.
The following license files are associated with this item:
- Structure-informed design of an enzymatically inactive vaccine component for group A Streptococcus.
- Authors: Henningham A, Ericsson DJ, Langer K, Casey LW, Jovcevski B, Chhatwal GS, Aquilina JA, Batzloff MR, Kobe B, Walker MJ
- Issue date: 2013 Aug 6
- Group a streptococcal vaccine candidates: potential for the development of a human vaccine.
- Authors: Henningham A, Gillen CM, Walker MJ
- Issue date: 2013
- Sortase A induces Th17-mediated and antibody-independent immunity to heterologous serotypes of group A streptococci.
- Authors: Fan X, Wang X, Li N, Cui H, Hou B, Gao B, Cleary PP, Wang B
- Issue date: 2014
- Differing Efficacies of Lead Group A Streptococcal Vaccine Candidates and Full-Length M Protein in Cutaneous and Invasive Disease Models.
- Authors: Rivera-Hernandez T, Pandey M, Henningham A, Cole J, Choudhury B, Cork AJ, Gillen CM, Ghaffar KA, West NP, Silvestri G, Good MF, Moyle PM, Toth I, Nizet V, Batzloff MR, Walker MJ
- Issue date: 2016 Jun 14
- Immunization with a streptococcal multiple-epitope recombinant protein protects mice against invasive group A streptococcal infection.
- Authors: Kuo CF, Tsao N, Hsieh IC, Lin YS, Wu JJ, Hung YT
- Issue date: 2017