SfbII protein, a fibronectin binding surface protein of group A streptococci, is a serum opacity factor with high serotype-specific apolipoproteinase activity.

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 Lett

authors

Kreikemeyer B,Martin DR,Chhatwal GS

doi

10.1111/j.1574-6968.1999.tb08692.x

keywords:

subject

Has Abstract

pub_date

1999-09-15 00:00:00

pages

305-11

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(99)00373-0

journal_volume

178

pub_type

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