Structural integrity of infant salivary immunoglobulin A (IgA) in IgA1 protease-rich environments.

IgA1 protease-secreting Streptococcus mitis often dominate the oral flora of the neonate and young infant at a time when salivary IgA concentrations are low and usually enriched in the secretory IgA1 subclass. To study the possible influence of these degradative enzymes on emerging host immunity, the presence of IgA1 protease-secreting streptococci was related to the structural integrity of salivary IgA in 24 infants who were between 3 and 18 weeks of age. At least one IgA1 protease-secreting strain could be isolated from the oral mucosa of 79% of the infants and comprised a mean of 38% of the total streptococcal flora of these infants. Chromatographic analyses of resting whole saliva from 16 infants revealed, however, that 95% of the secretory IgA (range 88-100%) remained intact, indicating that minimal immediate IgA proteolysis occurred in the bulk salivary phase. Proteolysis of infant salivary IgA, presumably by indigenous IgA1 protease, could be observed after extended (more than 7 h) in situ incubation of whole saliva at 37 degrees C. Salivary IgA antibody activities to S. mitis components were demonstrated by Western blot in infants colonized with an IgA1 protease-secreting flora. Preliminary evidence suggested that salivary antibody activity in some infants may be directed to IgA1 protease. Thus, the infant's antibody defenses not only appear very early in life but are substantively intact in the bulk salivary phase, even when the oral cavity is colonized with IgA1 protease-secreting streptococcal flora.