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1 M986 (surface binding negative, resistant to bacteriolysis).
2 susceptible to anti-NspA complement-mediated bacteriolysis.
3 y to antibody-dependent, complement-mediated bacteriolysis.
4 f the Abs could activate complement-mediated bacteriolysis.
5 ortance of source of complement in eliciting bacteriolysis.
6 meningococcus to resist complement-mediated bacteriolysis.
7 ility of the organism to complement-mediated bacteriolysis.
8 increased sensitivity to complement-mediated bacteriolysis, a result that is consistent with recently
9 s that activate classical complement pathway bacteriolysis and also inhibit binding of the complement
10 gonococcal resistance to complement-mediated bacteriolysis and cationic antimicrobial peptides (CAMPs
11 tro studies to determine complement-mediated bacteriolysis and complement-mediated opsonization of an
12 Z232 (surface binding variable, resistant to bacteriolysis), and did not protect against strain M986
14 fant rats challenged by strains resistant to bacteriolysis, and the protective activity paralleled th
16 ligomeric FP, which is also dysfunctional in bacteriolysis but binds the AP proconvertase, C3 convert
17 hat were previously shown to be resistant to bacteriolysis by anti-NspA antibodies produced by immuni
19 s insufficient to elicit complement-mediated bacteriolysis in vitro but sufficient to confer protecti
20 ainst outer surface protein B (OspB), causes bacteriolysis of Borrelia burgdorferi in the absence of
21 t analysis of resultant human antibodies for bacteriolysis, opsonophagocytosis, and protective effica
22 antibody to achieve 50% complement-mediated bacteriolysis than conjugate-induced antibody (P < 0.001
23 ndent, classical complement pathway-directed bacteriolysis than were organisms containing 2 copies.
25 e binding positive, susceptible to anti-NspA bacteriolysis), was poorly protective against strain BZ2
26 aboons, implying reduced complement-mediated bacteriolysis, whereas treated animals showed slightly i
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