Cargando…
EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity
BACKGROUND: The endoglycosidase EndoS and the cysteine proteinase SpeB from the human pathogen Streptococcus pyogenes are functionally related in that they both hydrolyze IgG leading to impairment of opsonizing antibodies and thus enhance bacterial survival in human blood. In this study, we further...
Autores principales: | Allhorn, Maria, Olsén, Arne, Collin, Mattias |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2266755/ https://www.ncbi.nlm.nih.gov/pubmed/18182097 http://dx.doi.org/10.1186/1471-2180-8-3 |
Ejemplares similares
-
EndoS and EndoS2 hydrolyze Fc-glycans on therapeutic antibodies with different glycoform selectivity and can be used for rapid quantification of high-mannose glycans
por: Sjögren, Jonathan, et al.
Publicado: (2015) -
SpeB of Streptococcus pyogenes Differentially Modulates Antibacterial and Receptor Activating Properties of Human Chemokines
por: Egesten, Arne, et al.
Publicado: (2009) -
EndoE from Enterococcus faecalis Hydrolyzes the Glycans of the Biofilm Inhibiting Protein Lactoferrin and Mediates Growth
por: Garbe, Julia, et al.
Publicado: (2014) -
Neutrophil-derived reactive agents induce a transient SpeB negative phenotype in Streptococcus pyogenes
por: Shumba, Patience, et al.
Publicado: (2023) -
Molecular Cloning and Docking of speB Gene Encoding Cysteine Protease With Antibiotic Interaction in Streptococcus pyogenes NBMKU12 From the Clinical Isolates
por: Balasubramanian, Natesan, et al.
Publicado: (2018)