Genome-based identification and characterization of a putative mucin-binding protein from the surface of Streptococcus pneumoniae

被引:18
作者
Bumbaca, Daniela
Littlejohn, James E.
Nayakanti, Hannah
Lucas, Alexander H.
Rigden, Daniel J.
Galperin, Michael Y.
Jedrzejas, Mark J.
机构
[1] Childrens Hosp Oakland, Res Inst, Ctr Immunobiol & Vaccine Dev, Oakland, CA 94609 USA
[2] Univ Liverpool, Sch Biol Sci, Liverpool L69 7ZB, Merseyside, England
[3] Natl Lib Med, NIH, Natl Ctr Biotechnol Informat, Bethesda, MD 20894 USA
关键词
adhesin; carbohydrate; mucin; mucin-binding protein; Streptococcus pneumoniae; gram-positive bacteria;
D O I
10.1002/prot.21205
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Streptococcus pneumoniae open reading frame SP1492 encodes a surface protein that contains a novel conserved domain similar to the repeated fragments of mucin-binding proteins from lactobacilli and lactococci. To investigate the functional role(s) of this protein and its potential adhesive properties, the surface-exposed region of SP1492 was expressed in Escherichia coli, purified to homogeneity, and partially characterized by biophysical and immunological methods. Circular dichroism and sedimentation measurements confirmed that SP1492 is an all-P protein that exists in solution as a monomer. The SP1492 protein has been shown to be expressed by S. pneumoniae and was experimentally localized to its surface. The protein functional domain binds to mucins II and III from porcine stomach and to purified submaxillary bovine gland mucin. It appears to be one of the very few unambiguous pneumococcal adhesin molecules known to date. A hypothetical model constructed by ab initio techniques predicts a novel P-sandwich protein structure. Proteins 2007; 66:547-558. (c) 2006 Wiley-Liss, Inc.
引用
收藏
页码:547 / 558
页数:12
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