Amino acid sequence requirements in the human IgA1 hinge for cleavage by streptococcal IgA1 proteases.
All the IgA1 proteases of the different pathogenic species of Streptococcus cleave the hinge of the alpha chain of human IgA1 only at one proline-threonine peptide bond. In order to study the importance of these amino acids for cleavage, several hinge mutant recombinant IgA1 antibodies were constructed. The mutations were found to be without major effect upon the structure or functional abilities of the antibodies. However, they had a major effect upon their sensitivity to cleavage by some of the IgA1 proteases.
Senior
B W
BW
Department of Molecular and Cellular Pathology, University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK. b.w.senior@dundee.ac.uk
Batten
M R
MR
Kilian
M
M
Woof
J M
JM
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000378:metabolism*; D006801:Humans; D007070:Immunoglobulin A / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013296:Streptococcus pneumoniae / Q000201:enzymology; D013379:Substrate Specificity
D007070:Immunoglobulin A; D011994:Recombinant Proteins; D010450:Endopeptidases