Studies are centered on the physicochemical and immunochemical analysis of the group A streptococcal M protein, a surface antigen of the organism. This protein is intimately associated with streptococcal virulence through its property of inhibiting phagocytosis of the organism. Although there are a large number of serologically distinct M proteins among the many types of group A streptococci, they share the common biological property of the antiphagocytic effect. At present, two serologically unrelated M proteins have been purified and partially sequenced. Physiocochemical and sequence data indicate that the M molecules have a close structure relationship with mammalian tropomyosin.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI011822-12
Application #
3125027
Study Section
Allergy and Immunology Study Section (ALY)
Project Start
1977-01-01
Project End
1987-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
12
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Rockefeller University
Department
Type
Graduate Schools
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065
Fischetti, Vincent A (2018) Development of Phage Lysins as Novel Therapeutics: A Historical Perspective. Viruses 10:
Schuch, Raymond; Khan, Babar K; Raz, Assaf et al. (2017) Bacteriophage Lysin CF-301, a Potent Antistaphylococcal Biofilm Agent. Antimicrob Agents Chemother 61:
Euler, Chad W; Juncosa, Barbara; Ryan, Patricia A et al. (2016) Targeted Curing of All Lysogenic Bacteriophage from Streptococcus pyogenes Using a Novel Counter-selection Technique. PLoS One 11:e0146408
Shen, Yang; Barros, Marilia; Vennemann, Tarek et al. (2016) A bacteriophage endolysin that eliminates intracellular streptococci. Elife 5:
Hendrickson, Christina; Euler, Chad W; Nguyen, Scott V et al. (2015) Elimination of Chromosomal Island SpyCIM1 from Streptococcus pyogenes Strain SF370 Reverses the Mutator Phenotype and Alters Global Transcription. PLoS One 10:e0145884
Lood, Rolf; Raz, Assaf; Molina, Henrik et al. (2014) A highly active and negatively charged Streptococcus pyogenes lysin with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia. Antimicrob Agents Chemother 58:3073-84
Gilmer, Daniel B; Schmitz, Jonathan E; Euler, Chad W et al. (2013) Novel bacteriophage lysin with broad lytic activity protects against mixed infection by Streptococcus pyogenes and methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 57:2743-50
McGowan, Sheena; Buckle, Ashley M; Mitchell, Michael S et al. (2012) X-ray crystal structure of the streptococcal specific phage lysin PlyC. Proc Natl Acad Sci U S A 109:12752-7
Raz, Assaf; Talay, Susanne R; Fischetti, Vincent A (2012) Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes. Mol Microbiol 84:631-47
Aksyuk, Anastasia A; Bowman, Valorie D; Kaufmann, Barbel et al. (2012) Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry. Proc Natl Acad Sci U S A 109:14001-6

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