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  • sialyltransferase  (1)
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  • 1
    ISSN: 1572-9699
    Keywords: Neisseria genorrhoeae ; complement killing ; CMP-NANA ; serum resistance ; sialyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Freshly isolated gonococci upon subculture are readily lysed by normal human serum although a few strains remain inherently resistant to the complement activity. The sensitive gonococci can be converted to serum resistance by incubation with a host derived factor referred to as cytidine 5′-monophospho-N-acetylneuraminic acid (CMP-NANA). These gonococci resist complement mediated killing due to their sialylation of an epitope structure on a component of lipo-oligosaccharide (LOS). In the present study, the kinetics of conversion to serum resistance by the action of sialyltransferase (STase) inNeisseria gonorrhoeae was followed with very low concentrations of CMP-NANA. This conversion could not be perceived at 2×10−3 nmol.ml−1 but was fully attainable from 8×10−3 to 2×10−2 nmol.ml−1 CMP-NANA. When pretreated up to 100 min in presence of the very low concentration of 2×10−3 nmol.ml−1, a potentiating effect on the conversion of gonococci by 2×10−2 nmol.ml−1 was observed in relation to the time of preincubation. This action was abolished after exposure to a subinhibitory concentration of chloramphenicol (0.5 µg.ml−1). The gonococci recovered their ability to convert to serum resistance following adequate washing. The potential for increase in STase activity should be of interest for understanding the conversion from a serum sensitive to a serum resistance state.
    Type of Medium: Electronic Resource
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