2017
DOI: 10.1111/febs.14200
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Streptococcus pneumoniae surface protein PfbA is a versatile multidomain and multiligand‐binding adhesin employing different binding mechanisms

Abstract: Streptococcus pneumoniae, one of the major human respiratory pathogens, uses its repertoire of surface proteins to adhere to the epithelium of the nasopharynx and lungs leading to colonization. PfbA is a conserved surface protein of S. pneumoniae and helps the bacterium to colonize the host by recognizing the extracellular matrix (ECM) molecule fibronectin, as well as blood proteins like plasminogen and human serum albumin. The crystal structure of rPfbA revealed it to possess a beta-helical region similar to … Show more

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Cited by 19 publications
(15 citation statements)
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“…Some lectins of pathogens work as ligand for TLR2 and TLR4 (48). We previously reported that PfbA can interact with glycolipid and glycoprotein fractions of red blood cells, several monosaccharides, D-sucrose, and D-raffinose (26, 27). Hence, to determine whether PfbA works as a TLR ligand, we performed a SEAP assay using HEK-293 cells stably transfected with either TLR2 or TLR4, NF-κB, and SEAP (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…Some lectins of pathogens work as ligand for TLR2 and TLR4 (48). We previously reported that PfbA can interact with glycolipid and glycoprotein fractions of red blood cells, several monosaccharides, D-sucrose, and D-raffinose (26, 27). Hence, to determine whether PfbA works as a TLR ligand, we performed a SEAP assay using HEK-293 cells stably transfected with either TLR2 or TLR4, NF-κB, and SEAP (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…TLR2 has four N -glycans whose structures still remain unknown, and the N -glycans are critical for the lectins to induce TLR2-mediated activation (48). PfbA binds to various carbohydrates via the groove residues in the β-helix (26, 27). There is a possibility that PfbA induces TLR2 signaling by binding to TLR2 N -glycans.…”
Section: Discussionmentioning
confidence: 99%
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“…The crystal structure of the large recombinant fragment, PfbA 150-607 , revealed it to possess a beta-helical region followed by a C-terminal disordered segment with structural and sequence features that resemble the Fn-binding regions of FnBPA of S. aureus and BBK32 of Borrelia burgdorferi [97]. Recently, it has been reported that the open reading frame spr0075 encodes for a 120 kDa protein, named plasminogen/fibronectin-binding protein B (PfbB), which displays an LPXTG cell wall anchoring motif and six repetitive domains that directly interact with Fn, allowing adherence of S. pneumoniae to various epithelial respiratory tract cell lines [98].…”
Section: Fn-binding Proteins From Other Streptococcal Speciesmentioning
confidence: 99%
“…The DNA fragments were assembled using the GeneArt ® Seamless Cloning and Assembly Kit (Thermo Fisher Scientific, Waltham, MA, USA). The constructed plasmid was transformed into E. coli XL-10 Gold (Agilent, Santa Clara, CA, USA), and recombinant CbpJ was purified as described previously 31,33,[64][65][66] .…”
Section: Preparation Of Recombinant Cbpjmentioning
confidence: 99%