2002Infection and ImmunityOpen access

Opsonization of Actinobacillus actinomycetemcomitans by Immunoglobulin G Antibody Reactive with Phosphorylcholine

Donald Purkall, John G. Tew, Harvey A. Schenkein

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Abstract

We used two strains of Actinobacillus actinomycetemcomitans, one bearing phosphorylcholine (PC) (strain D045D-40) and one devoid of PC antigens (strain DB03A-42), as well as a nonencapsulated strain of Streptococcus pneumoniae (strain 39937), to examine the opsonic properties of physiological concentrations (</=30 micro g/ml) of purified human anti-PC immunoglobulin G (IgG). Anti-PC bound to both A. actinomycetemcomitans DO45D-40 and S. pneumoniae 39937 and induced superoxide anion production by polymorphonuclear neutrophils; induction of the oxidative burst was inhibited by antibodies to either CD16 or CD32. Thus, anti-PC IgG at concentrations present in most human sera promotes the opsonization of PC-expressing strains of A. actinomycetemcomitans in the absence of complement, implying that anti-PC may be a protective antibody against such strains of bacteria.

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We used two strains of Actinobacillus actinomycetemcomitans, one bearing phosphorylcholine (PC) (strain D045D-40) and one devoid of PC antigens (strain DB03A-42), as well as a nonencapsulated strain of Streptococcus pneumoniae (strain 39937), to examine the opsonic properties of physiological concentrations (</=30 micro g/ml) of purified human anti-PC immunoglobulin G (IgG). Anti-PC bound to both A. actinomycetemcomitans DO45D-40 and S. pneumoniae 39937 and induced superoxide anion production by polymorphonuclear neutrophils; induction of the oxidative burst was inhibited by antibodies to either CD16 or CD32. Thus, anti-PC IgG at concentrations present in most human sera promotes the opsonization of PC-expressing strains of A. actinomycetemcomitans in the absence of complement, implying that anti-PC may be a protective antibody against such strains of bacteria.

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Available abstract

We used two strains of Actinobacillus actinomycetemcomitans, one bearing phosphorylcholine (PC) (strain D045D-40) and one devoid of PC antigens (strain DB03A-42), as well as a nonencapsulated strain of Streptococcus pneumoniae (strain 39937), to examine the opsonic properties of physiological concentrations (</=30 micro g/ml) of purified human anti-PC immunoglobulin G (IgG). Anti-PC bound to both A. actinomycetemcomitans DO45D-40 and S. pneumoniae 39937 and induced superoxide anion production by polymorphonuclear neutrophils; induction of the oxidative burst was inhibited by antibodies to either CD16 or CD32. Thus, anti-PC IgG at concentrations present in most human sera promotes the opsonization of PC-expressing strains of A. actinomycetemcomitans in the absence of complement, implying that anti-PC may be a protective antibody against such strains of bacteria.

Key concepts: Antibody opsonization, Phosphorylcholine, Actinobacillus, Microbiology, Opsonin, Antibody, Streptococcus pneumoniae, Immunoglobulin G

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