منابع مشابه
Properties of an inducible extracellular neuraminidase from an Arthrobacter isolate.
The elective isolation of a soil microorganism, tentatively assigned to the genus Arthrobacter, which produced an extracellular neuraminidase is described. The secretion of neuraminidase from washed cells in minimal medium required the presence of sialo-containing glycoproteins, whereas free N-acetyl-neuraminic asid of N-acetylmannosamine were poor inducers. No enzyme could be dected in the ind...
متن کاملInfluenza neuraminidase
Influenza neuraminidase is the target of two licensed antivirals that have been very successful, with several more in development. However, neuraminidase has been largely ignored as a vaccine target despite evidence that inclusion of neuraminidase in the subunit vaccine gives increased protection. This article describes current knowledge on the structure, enzyme activity, and antigenic signific...
متن کاملEffect of streptococcal extracellular nuclease on the carrier activity of RNA for streptolysin S.
Upon digestion with a streptococcal extracellular nuclease, yeast RNA yielded acid-insoluble core having increased carrier activity for streptolysin S. The carrier activity was found in minor fractions of the core which were eluted from a DEAE-cellulose column at higher salt concentrations. Upon gel filtration through a Sephadex G-75 column, the effective component (Fr. I) was eluted earlier th...
متن کاملDiphosphopyridine Nucleotidase as an Extracellular Product of Streptococcal Growth and Its Possible Relationship to Leukotoxicity
Among 170 streptococcal strains, there were encountered 98 that yielded culture supernates which caused splitting of diphosphopyridine nucleotide (DPN). All of the latter belonged to Group A, C, or G. Release of DPNase accompanied the growth of diverse antigenic types of Group A streptococci, and data on the frequency of DPNase-producing strains for certain types are given. In contrast, culture...
متن کاملM1 protein allows Group A streptococcal survival in phagocyte extracellular traps through cathelicidin inhibition.
M1 protein contributes to Group A Streptococcus (GAS) systemic virulence by interfering with phagocytosis and through proinflammatory activities when released from the cell surface. Here we identify a novel role of M1 protein in the stimulation of neutrophil and mast cell extracellular trap formation, yet also subsequent survival of the pathogen within these DNA-based innate defense structures....
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1968
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.95.4.1491-1492.1968