Abstract:
:Colonization of mucosal respiratory surfaces is a prerequisite for the human pathobiont Streptococcus pneumoniae (the pneumococcus) to cause severe invasive infections. The arsenal of pneumococcal adhesins interacts with a multitude of extracellular matrix proteins. A paradigm for pneumococci is their interaction with the adhesive glycoprotein fibronectin, which facilitates bacterial adherence to host cells. Here, we deciphered the molecular interaction between fibronectin and pneumococcal fibronectin-binding proteins (FnBPs) PavA and PavB respectively. We show in adherence and binding studies that the pneumococcal interaction with fibronectin is a non-human specific trait. PavA and PavB target at least 13 out of 15 type III fibronectin domains as demonstrated in ligand overlay assays, surface plasmon resonance studies and SPOT peptide arrays. Strikingly, both pneumococcal FnBPs recognize similar peptides in targeted type III repeats. Structural comparisons revealed that the targeted type III repeat epitopes cluster on the inner strands of both β-sheets forming the fibronectin domains. Importantly, synthetic peptides of FnIII1 , FnIII5 or FnIII15 bind directly to FnBPs PavA and PavB respectively. In conclusion, our study suggests a common pattern of molecular interactions between pneumococcal FnBPs and fibronectin. The specific epitopes recognized in this study can potentially be tested as antimicrobial targets in further scientific endeavours.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Kanwal S,Jensch I,Palm GJ,Brönstrup M,Rohde M,Kohler TP,Somplatzki D,Tegge W,Jenkinson HF,Hammerschmidt Sdoi
10.1111/mmi.13740subject
Has Abstractpub_date
2017-09-01 00:00:00pages
839-859issue
6eissn
0950-382Xissn
1365-2958journal_volume
105pub_type
杂志文章abstract::Deletions or substitutions of amino acids at the carboxyl-terminus of the heat-labile enterotoxin B subunit (EtxB) affect its assembly into pentamers in a temperature-dependent manner. At 42 degrees C, the mutations prevent the B subunits from achieving their final pentameric structure resulting in membrane associatio...
journal_title:Molecular microbiology
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abstract::RepA, the initiator protein of plasmid P1, binds to multiple sites (iterons) in the origin. The binding normally requires participation of chaperones, DnaJ, DnaK and GrpE. When purified, RepA appears dimeric and is inactive in iteron binding. On reaction with chaperones, a species active in iteron binding is formed an...
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journal_title:Molecular microbiology
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更新日期:2005-04-01 00:00:00
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pub_type: 杂志文章
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更新日期:2003-10-01 00:00:00
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journal_title:Molecular microbiology
pub_type: 杂志文章
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更新日期:2000-11-01 00:00:00
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pub_type: 杂志文章
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更新日期:2012-10-01 00:00:00
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