Abstract:
:Serum opacity factor (SOF) is produced by group A streptococci belonging to certain M types. SOF cleaves the apolipoprotein component of the high density lipoprotein fraction of serum rendering it insoluble which in turn leads to serum opacity. SfbII protein, a fibronectin binding surface protein cloned from group A streptococci, was obtained from a strain of M75. Here we show that this protein has a second functional domain responsible for SOF activity. The fibronectin binding region was located in the C-terminal end of the protein. Deletion analysis showed that the remainder of the protein was required for SOF activity. Sequence analysis of SfbII, when compared with the published sequence of SOF22, showed 99% identity with a difference of only four amino acids. In spite of this high homology, SOF from M75 was type-specific and antibody evoked specifically inhibited only SOF produced by M75. Antibodies found in human serum following natural infection also inhibited the SOF of SfbII in a type-specific manner. The results showed that the SfbII protein from M75 is SOF with a high serotype-specific enzyme activity.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Kreikemeyer B,Martin DR,Chhatwal GSdoi
10.1111/j.1574-6968.1999.tb08692.xkeywords:
subject
Has Abstractpub_date
1999-09-15 00:00:00pages
305-11issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(99)00373-0journal_volume
178pub_type
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