Molecular characterization of PcpA:: a novel choline-binding protein of Streptococcus pneumoniae

被引:57
作者
Sánchez-Beato, AR [1 ]
López, R [1 ]
García, JL [1 ]
机构
[1] CSIC, Ctr Invest Biol, Dept Mol Microbiol, E-28006 Madrid, Spain
关键词
adhesin; choline-binding domain; leucine-rich repeat; pneumococcus;
D O I
10.1111/j.1574-6968.1998.tb13087.x
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The gene pcpA that encodes a novel pneumococcal choline-binding protein has been cloned and characterized. Northern blot analysis revealed that pcpA is expressed during the exponential phase of growth of pneumococci as a monocistronic transcript of about 2.3 kb. The transcription start site has been located 132 bp upstream of the start codon and the proposed -35 and -10 boxes that are highly similar to those of the typical sigma(70) promoters from Escherichia coli. This gene encodes a putative 79 kDa protein that contains a typical C-terminal choline-binding domain (ChBD). The ChBD of PcpA is built up by 11 identical motifs of 20 amino acids plus a tail of 19 amino acids, which represents the longest ChBD that has been characterized so far. Interestingly, two tandem arrays of five characteristic amphipatic leucine reach repeats (LRRs) of 22-26 amino acids in length have been found in the N-terminal region of PcpA. Since LRRs have been proposed to be involved in protein-protein and protein-lipid interactions our finding suggests a role for PcpA in pneumococcal adhesion. (C) 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V. Ali rights reserved.
引用
收藏
页码:207 / 214
页数:8
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