Streptococcus pyogenes sclB encodes a putative hypervariable surface protein with a collagen-like repetitive structure

被引:73
作者
Whatmore, AM [1 ]
机构
[1] Univ Warwick, Dept Biol Sci, Infect Dis Res Grp, Coventry CV4 7AL, W Midlands, England
来源
MICROBIOLOGY-UK | 2001年 / 147卷
关键词
bacterial surface protein; genetic variation; short sequence repeats; tandem repeats;
D O I
10.1099/00221287-147-2-419
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Streptococcus pyogenes is the causative agent in a wide range of diseases of humans of varying severity. During a study scanning the genome sequence of a serotype M1 invasive isolate SF370 for novel surface proteins, an ORF, designated scIB, was identified. The putative protein encoded by scIB contains both a signal peptide and classic Gram-positive wall-associated sequences. Comparison of the sequences of this ORF with those from a number of unrelated isolates demonstrated that scIB encodes a putative surface protein with a variable N-terminal sequence followed by a variable length tract of collagen-like GXY(n) repeats. A further feature of scIB is the presence of CAAAA repeat tracts immediately downstream of the putative start codon, The number of these pentameric repeats varies from 4 to 15 between strains and variation in repeat number results in the predicted ScIB protein being either in or out of frame relative to the start codon, These observations suggest that expression of this protein may be regulated at the translational level as a result of gain or loss of CAAAA repeats. While the function of ScIB remains to be elucidated, an scIB-specific transcript was detected by RT-PCR during in vitro culture. Finally, it is shown that a second gene, sclA, potentially encoding a protein with a similar extensive collagen-like structure and variable N-terminal sequence, is present in all isolates of S. pyogenes tested to date. Thus S, pyogenes harbours a novel family of structurally related and surface-exposed proteins of potential importance in the pathogenic process.
引用
收藏
页码:419 / 429
页数:11
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