ABSTRACT
The recognition of glycoconjugate receptors on sialidase-treated polymorphonuclear leukocytes (PMNs) by the Gal/GalNAc-reactive fimbrial lectin of Actinomyces viscosus T14V has previously been shown to initiate lactose-inhibitable phagocytosis and subsequent killing of the bacteria. Although a mutant lacking fimbriae, A. viscosus 147, was not destroyed by this mechanism, the present studies demonstrate that the deposition of C3 fragments on this bacterium by anti-A. viscosus 147 immunoglobulin M (IgM) prior to incubation with either untreated or sialidase-treated PMNs correlated with a reduction in viability of approximately 2 log10. This bactericidal activity was unaffected by lactose. A similar decrease in viability was observed following the addition of untreated PMNs to A. viscosus T14V preincubated with anti-A. viscosus 147 IgM and complement, conditions favorable for C3- but not lectin-mediated bactericidal activity. Neither IgM nor complement alone was opsonic for either strain, and individually they did not alter killing of A. viscosus T14V by sialidase-treated PMNs or inhibition of this bactericidal activity by lactose. The number of viable A. viscosus T14V cells was decreased by approximately 3.5 log10 when the bacteria were incubated with IgM and complement prior to the addition of sialidase-treated PMNs, and lactose only partially inhibited this response. Thus, the PMN-dependent bactericidal activity initiated by the participation of both the actinomyces lectin and complement was significantly greater than that achieved by either ligand alone.
