Cloning of the gene encoding streptococcal immunoglobulin A protease and its expression in Escherichia coli.
We have identified and cloned a 6-kilobase-pair segment of chromosomal DNA from Streptococcus sanguis ATCC 10556 that encodes immunoglobulin A (IgA) protease activity when cloned into Escherichia coli. The enzyme specified by the iga gene in plasmid pJG1 accumulates in the periplasm of E. coli MM294 cells and has a substrate specificity for human IgA1 identical to that of native S. sanguis protease. Hybridization experiments with probes from within the encoding DNA showed no detectable homology at the nucleotide sequence level with chromosomal DNA of gram-negative bacteria that excrete IgA protease. Moreover, the S. sanguis iga gene probes showed no detectable hybridization with chromosomal DNA of S. pneumoniae, although the IgA proteases of these two streptococcal species cleaved the identical peptide bond in the human IgA1 heavy-chain hinge region.
Gilbert
J V
JV
Department of Medicine, Tufts-New England Medical Center Hospital, Boston, Massachusetts.
Plaut
A G
AG
Fishman
Y
Y
Wright
A
A
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000235:genetics*; D011994:Recombinant Proteins; D012697:Serine Endopeptidases; D013298:Streptococcus sanguis / Q000201:enzymology / Q000235:genetics*
D004269:DNA, Bacterial; D011994:Recombinant Proteins; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase