EVIDENCE FOR INDEPENDENT BINDING DOMAINS WITHIN A GROUP-A STREPTOCOCCAL TYPE IIO IGG-BINDING PROTEIN

Citation
M. Tsivitse et Mdp. Boyle, EVIDENCE FOR INDEPENDENT BINDING DOMAINS WITHIN A GROUP-A STREPTOCOCCAL TYPE IIO IGG-BINDING PROTEIN, Canadian journal of microbiology, 42(11), 1996, pp. 1172-1175
Citations number
22
Categorie Soggetti
Microbiology,Immunology,"Biothechnology & Applied Migrobiology",Biology
ISSN journal
00084166
Volume
42
Issue
11
Year of publication
1996
Pages
1172 - 1175
Database
ISI
SICI code
0008-4166(1996)42:11<1172:EFIBDW>2.0.ZU;2-G
Abstract
The gene for a type IIo IgG-binding protein has previously been cloned and sequenced. The similar to 60 000 M(r) recombinant gene product bi nds all four human IgG subclasses and fibrinogen. Treatment of this re combinant protein with CNBr results in generation of a series of fragm ents. One fragment, an similar to 32 000 M(r) polypeptide, binds IgG(1 ), IgG(2), and IgG(4) but neither IgG(3) nor fibrinogen. N-terminal am ino sequencing of this fragment indicated that this was an internal fr agment of the protein starting at amino acid 186 of the mature protein . These findings provide evidence for two distinct domains for binding IgG1, IgG(2), and IgG(4) and binding IgG(3) within a single bacterial IgG-binding protein.