• SpeB, the most abundant streptococcal extracellular protein, is a cysteine protease. (wikipedia.org)
  • The maturation and proteolytic activity of streptococcal cysteine protease (SpeB), an important virulence factor in GAS, has been reported to be abrogated by zinc and copper. (bvsalud.org)
  • Since the host pathogenicity of the SpeB-deficient strain was significantly reduced, maintenance of intracellular manganese and zinc levels in the GAS via MntE and CzcD may not only confer metal resistance to the bacterium, but may also play an essential role in its virulence. (bvsalud.org)
  • It was originally studied as two separate toxins, streptococcal pyrogenic exotoxin B and streptococcal cysteine proteinase, until it was shown that both proteins were encoded by the speB gene and that the attributed pyrogenic activities were due to contamination by SpeA and SpeC. (wikipedia.org)
  • SpeB is known as streptococcal pyrogenic exotoxin B, streptopain and streptococcal cysteine proteinase as a result of its original misidentification as two separate toxins, and is neither an exotoxin nor pyrogenic. (wikipedia.org)
  • All superantigenic streptococcal pyrogenic exotoxins contain two major conserved protein domains that are linked by an α-helix, which consist of an amino-terminal oligosoccharide/oligonucleotide binding fold and a carboxy-terminal β-grasp domain, as well as dodecapeptide binding region. (wikipedia.org)
  • French, J. B. , Cen, Y. , Sauve, A. A. , and Ealick, S. E. (2010) High-resolution crystal structures of Streptococcus pneumoniae nicotinamidase with trapped intermediates provide insights into the catalytic mechanism and inhibition by aldehydes . (cornell.edu)
  • SpeB is a 28 kDa protein with three major forms, mSpeB1, mSpeB2 and mSpeB3, which are categorized by variations the primary amino acid sequence. (wikipedia.org)
  • TIM barrel domain, Glyoxalase/fosfomycin resistance/dioxygenase domain, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily [InterProScan]. (ntu.edu.sg)
  • Finally cystine-192 and histidine-340 form a catalytic dyad. (wikipedia.org)
  • Cystathionine-ß-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. (bvsalud.org)