ABSTRACT
The bacteriolytic activity of nutritionally variant streptococci (NVS), fastidious microaerophilic bacteria, which are members of the genera Abiotrophia and Granulicatella, was characterized in a renaturating SDS polyacrylamide gel electrophoresis system. Bacteriolytic profiles appeared quite different for the three species of NVS examined. Granulicatella adiacens or Abiotrophia defectiva each presented at least seven lytic bands, four of which were in common, while the other three were species-specific, whereas Granulicatella elegans showed six bands, which were overlapping with the G. adiacens bands. Four lytic bands were identified for enzymatic activity; D-alanyl-L-lysine hydrolase, endo-N-acetylglucosaminidase, endoacetylmuramidase, D-glutamyl-L-lysine hydrolase and acetylmuramoyl-L-alanine amidase activities could be defined. The bacteriolytic enzymes were purified and characterized for the kinetics of production during growth, autolytic activity, temperature and pH stability.
Subject(s)
Bacteriolysis , Streptococcus/physiology , Bacteriolysis/physiology , Electrophoresis, Polyacrylamide Gel , Streptococcus/enzymologyABSTRACT
A human recombinant monoclonal Fab fragment that specifically recognizes all the influenza A virus strains tested was produced in transformed Escherichia coli using the phage display technique. No strain of influenza B virus reacted with it. It was purified after four cycles of panning and by a single passage through an immunoaffinity column. About 1 mg of pure monoclonal antibody was obtained from 1 liter of culture medium in 3 working days. The Fab fragment reacted with a viral 27-kDa protein, which could reasonably be a matrix protein. Indirect immunofluorescence tests performed on virus-infected MDCK cells showed that this Fab fragment was at least equally efficient as other commercial monoclonal antibody-based systems in detecting influenza A viral infections. The potential advantages of human recombinant Fabs on murine monoclonal antibodies are discussed.
