Molecular biology of Haemophilus influenzae IgA1 proteases.
IgA1 proteases of two distinct specificities were demonstrated among 95 isolates of Haemophilus influenzae and nine isolates of H. aegyptius. The two enzymes cleaved two different peptide bonds in the hinge region of the alpha chain of IgA1: a prolyl-seryl bond located at position 231-232 (type A cleavage) and a prolyl-threonyl peptide bond between residues 235 and 236 (type B cleavage). Each strain of H. influenzae produced either one or both of these types of enzymes, whereas all H. aegyptius strains produced type A enzyme only. The application of enzyme-neutralizing antibodies to the study of IgA1 proteases produced by the 104 strains of H. influenzae and H. aegyptius revealed at least 15 different types of protease activities based on inhibition patterns in nine selected antibody preparations. The types of IgA1 proteases closely correlated with the serotype of encapsulated strains of H. influenzae. The study suggests that H. influenzae strains produce at least two serologically different IgA1 proteases with distinct or identical enzymatic activities.
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D006190:Haemophilus / Q000201:enzymology; D006193:Haemophilus influenzae / Q000201:enzymology*; D007106:Immune Sera / Q000276:immunology; D010447:Peptide Hydrolases / Q000032:analysis* / Q000276:immunology; D012697:Serine Endopeptidases
D007106:Immune Sera; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase