Degradation of IgA proteins by Pseudomonas aeruginosa elastase.
Human colostral IgA and myeloma proteins of both IgA1 and IgA2 subclasses were susceptible to cleavage by Pseudomonas aeruginosa elastase. Detailed analysis of the cleavage products of IgA myeloma proteins revealed complete degradation of Fab with no evidence of intact Fab fragments as intermediate cleavage products. In contrast, both IgA1 and IgA2 proteins were resistant to cleavage by alkaline protease from P. aeruginosa. The susceptibility of human IgA proteins to elastase suggests a mechanism by which P. aeruginosa might evade the potentially protective function of IgA by producing this enzyme.
Heck
L W
LW
Department of Medicine, University of Alabama, Birmingham School of Medicine 35294.
Alarcon
P G
PG
Kulhavy
R M
RM
Morihara
K
K
Russell
M W
MW
Mestecky
J F
JF
D001427:Bacterial Toxins / Q000276:immunology; D006460:Hemolysin Proteins; D006801:Humans; D007070:Immunoglobulin A / Q000378:metabolism*; D007071:Immunoglobulin A, Secretory / Q000378:metabolism; D066298:In Vitro Techniques; D010196:Pancreatic Elastase / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism
D001427:Bacterial Toxins; D006460:Hemolysin Proteins; D007070:Immunoglobulin A; D007071:Immunoglobulin A, Secretory; D010446:Peptide Fragments; C021091:staphylococcal alpha-toxin; D012697:Serine Endopeptidases; D010196:Pancreatic Elastase; C032923:microbial serine proteinases