M-Protein-derived Conformational Peptide Epitope Vaccine Candidate against Group A Streptococcus

2013 ◽  
Vol 10 (1) ◽  
pp. 39-45 ◽  
Author(s):  
Mariusz Skwarczynski ◽  
Khairul A. Kamaruzaman ◽  
Saranya Srinivasan ◽  
Mehfuz Zaman ◽  
I-Chun Lin ◽  
...  
Keyword(s):  
Vaccine Candidate ◽  
Group A Streptococcus ◽  
M Protein ◽  
Epitope Vaccine ◽  
Peptide Epitope ◽  
Group A

FbaA- and M protein-based multi-epitope vaccine elicits strong protective immune responses against group A streptococcus in mouse model

2014 ◽  
Vol 16 (5) ◽  
pp. 409-418 ◽  
Author(s):  
Cuiqing Ma ◽  
Zheng Liu ◽  
Wenjian Li ◽  
Xuesong Qian ◽  
Song Zhang ◽  
...  
Keyword(s):  
Mouse Model ◽  
Immune Responses ◽  
Group A Streptococcus ◽  
M Protein ◽  
Epitope Vaccine ◽  
Group A

scholarly journals Longitudinal Analysis of Group A Streptococcus emm Types and emm Clusters in a High-Prevalence Setting: Relationship between Past and Future Infections

2019 ◽  
Vol 221 (9) ◽  
pp. 1429-1437 ◽  
Author(s):  
Patricia Therese Campbell ◽  
Steven Y C Tong ◽  
Nicholas Geard ◽  
Mark R Davies ◽  
Kate A Worthing ◽  
...  
Keyword(s):  
Vaccine Candidate ◽  
Group A Streptococcus ◽  
Dominant Mode ◽  
Classification Systems ◽  
M Protein ◽  
Ecological Niches ◽  
Population Immunity ◽  
High Prevalence ◽  
Group A ◽  
The Relationship

Abstract Group A Streptococcus is a pathogen of global importance, but despite the ubiquity of group A Streptococcus infections, the relationship between infection, colonization, and immunity is still not completely understood. The M protein, encoded by the emm gene, is a major virulence factor and vaccine candidate and forms the basis of a number of classification systems. Longitudinal patterns of emm types collected from 457 Fijian schoolchildren over a 10-month period were analyzed. No evidence of tissue tropism was observed, and there was no apparent selective pressure or constraint of emm types. Patterns of emm type acquisition suggest limited, if any, modification of future infection based on infection history. Where impetigo is the dominant mode of transmission, circulating emm types either may not be constrained by ecological niches or population immunity to the M protein, or they may require several infections over a longer period of time to induce such immunity.

scholarly journals Host Pathways of Hemostasis that Regulate Group A Streptococcus pyogenes Pathogenicity

2020 ◽  
Vol 21 (2) ◽  
pp. 193-201
Author(s):  
Victoria A. Ploplis ◽  
Francis J. Castellino
Keyword(s):  
Streptococcus Pyogenes ◽  
Inflammatory Responses ◽  
Group A Streptococcus ◽  
Protein A ◽  
M Protein ◽  
Severe Group ◽  
Group A ◽  
Flow Through ◽  
Hallmark Feature ◽  
Major Target

A hallmark feature of severe Group A Streptococcus pyogenes (GAS) infection is dysregulated hemostasis. Hemostasis is the primary pathway for regulating blood flow through events that contribute towards clot formation and its dissolution. However, a number of studies have identified components of hemostasis in regulating survival and dissemination of GAS. Several proteins have been identified on the surface of GAS and they serve to either facilitate invasion to host distal sites or regulate inflammatory responses to the pathogen. GAS M-protein, a surface-exposed virulence factor, appears to be a major target for interactions with host hemostasis proteins. These interactions mediate biochemical events both on the surface of GAS and in the solution when M-protein is released into the surrounding environment through shedding or regulated proteolytic processes that dictate the fate of this pathogen. A thorough understanding of the mechanisms associated with these interactions could lead to novel approaches for altering the course of GAS pathogenicity.

scholarly journals Erratum: Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein

2017 ◽  
Vol 2 (7) ◽  
Author(s):  
Cosmo Z. Buffalo ◽  
Adrian J. Bahn-Suh ◽  
Sophia P. Hirakis ◽  
Tapan Biswas ◽  
Rommie E. Amaro ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Binding Protein ◽  
M Protein ◽  
Group A

scholarly journals Evaluation of safety and immunogenicity of a group A streptococcus vaccine candidate (MJ8VAX) in a randomized clinical trial

PLoS ONE ◽  
2018 ◽  
Vol 13 (7) ◽  
pp. e0198658 ◽  
Author(s):  
Silvana Sekuloski ◽  
Michael R. Batzloff ◽  
Paul Griffin ◽  
William Parsonage ◽  
Suzanne Elliott ◽  
...  
Keyword(s):  
Clinical Trial ◽  
Randomized Clinical Trial ◽  
Vaccine Candidate ◽  
Group A Streptococcus ◽  
Group A

scholarly journals Conversion of an M- group A streptococcus to M+ by transfer of a plasmid containing an M6 gene.

1986 ◽  
Vol 164 (5) ◽  
pp. 1641-1651 ◽  
Author(s):  
J R Scott ◽  
P C Guenthner ◽  
L M Malone ◽  
V A Fischetti
Keyword(s):  
Structural Gene ◽  
Human Blood ◽  
Group A Streptococcus ◽  
M Protein ◽  
Gene Encoding ◽  
Hyperimmune Serum ◽  
Amino Terminal ◽  
Group A ◽  
Hyperimmune Rabbit ◽  
Streptococcal Strain

An M28-derived group A streptococcal strain deleted for the gene encoding M protein was converted to M+ by introduction of a plasmid carrying emm6, the structural gene for type 6 M protein from strain D471. The reconstituted M+ strain, JRS2, resists phagocytosis in human blood and is opsonized by anti-M6 hyperimmune serum, but not by anti-M28 serum. Immunofluorescent microscopy and ELISA demonstrate the presence of M protein on its surface. In addition, JRS2 removes opsonic antibodies from hyperimmune rabbit sera generated by immunization with purified ColiM6 protein and with a synthetic amino-terminal peptide derived from M6. Immunization of rabbits with JRS2 generates opsonic anti-M6 antibodies. These results indicate that the cloned emm6 gene contains the information necessary to convert a phagocytosis-sensitive streptococcus to phagocytosis resistance. Furthermore, it also contains the determinants for M type specificity and those required to elicit opsonic antibodies. It thus appears to determine all the traits associated with M protein.

scholarly journals Protective immunity induced by an intranasal multivalent vaccine comprising 10 Lactococcus lactis strains expressing highly prevalent M-protein antigens derived from Group A Streptococcus

2018 ◽  
Vol 62 (6) ◽  
pp. 395-404 ◽  
Author(s):  
Aniela Wozniak ◽  
Natalia Scioscia ◽  
Patricia C. García ◽  
James B. Dale ◽  
Braulio A. Paillavil ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Protective Immunity ◽  
Group A Streptococcus ◽  
M Protein ◽  
Protein Antigens ◽  
Multivalent Vaccine ◽  
Group A

scholarly journals Structure-based group A streptococcal vaccine design: Helical wheel homology predicts antibody cross-reactivity among streptococcal M protein–derived peptides

2020 ◽  
Vol 295 (12) ◽  
pp. 3826-3836 ◽  
Author(s):  
Michelle P. Aranha ◽  
Thomas A. Penfound ◽  
Jay A. Spencer ◽  
Rupesh Agarwal ◽  
Jerome Baudry ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Coiled Coil ◽  
Cross Reactivity ◽  
M Protein ◽  
High Sequence Identity ◽  
Sequence Identity ◽  
Streptococcal M Protein ◽  
Helical Wheel ◽  
Group A ◽  
Immunological Assays

Group A streptococcus (Strep A) surface M protein, an α-helical coiled-coil dimer, is a vaccine target and a major determinant of streptococcal virulence. The sequence-variable N-terminal region of the M protein defines the M type and also contains epitopes that promote opsonophagocytic killing of streptococci. Recent reports have reported considerable cross-reactivity among different M types, suggesting the prospect of identifying cross-protective epitopes that would constitute a broadly protective multivalent vaccine against Strep A isolates. Here, we have used a combination of immunological assays, structural biology, and cheminformatics to construct a recombinant M protein–based vaccine that included six Strep A M peptides that were predicted to elicit antisera that would cross-react with an additional 15 nonvaccine M types of Strep A. Rabbit antisera against this recombinant vaccine cross-reacted with 10 of the 15 nonvaccine M peptides. Two of the five nonvaccine M peptides that did not cross-react shared high sequence identity (≥50%) with the vaccine peptides, implying that high sequence identity alone was insufficient for cross-reactivity among the M peptides. Additional structural analyses revealed that the sequence identity at corresponding polar helical-wheel heptad sites between vaccine and nonvaccine peptides accurately distinguishes cross-reactive from non–cross-reactive peptides. On the basis of these observations, we developed a scoring algorithm based on the sequence identity at polar heptad sites. When applied to all epidemiologically important M types, this algorithm should enable the selection of a minimal number of M peptide–based vaccine candidates that elicit broadly protective immunity against Strep A.

scholarly journals Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein

2016 ◽  
Vol 1 (11) ◽  
Author(s):  
Cosmo Z. Buffalo ◽  
Adrian J. Bahn-Suh ◽  
Sophia P. Hirakis ◽  
Tapan Biswas ◽  
Rommie E. Amaro ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Binding Protein ◽  
M Protein ◽  
Group A
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