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Functional Analysis of an S-Layer-Associated Fibronectin-Binding Protein in Lactobacillus acidophilus NCFM.

Hymes JP, Johnson BR, Barrangou R, Klaenhammer TR - Appl. Environ. Microbiol. (2016)

Bottom Line: Bacterial surface layers (S-layers) are crystalline arrays of self-assembling proteinaceous subunits called S-layer proteins (Slps) that comprise the outermost layer of the cell envelope.To investigate the functional role of LBA0191 (designated FbpB) in L. acidophilus NCFM, an fbpB-deficient strain was constructed.The L. acidophilus mutant with a deletion off bpB lost the ability to adhere to mucin and fibronectin in vitro Homologues off bpB were identified in five additional putative S-layer-forming species, but no homologues were detected in species outside theL. acidophilus homology group.

View Article: PubMed Central - PubMed

Affiliation: Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Raleigh, North Carolina, USA.

No MeSH data available.


Related in: MedlinePlus

Amino acid sequence alignment of FbpB homologues in Lactobacillus species. The colored boxes represent domains predicted by InterProScan 5. The bar graph shows the mean pairwise identity across homologues at each position in the amino acid alignment (positions 1 to 473, labeled at top). Green bars indicate 100% identity, yellow bars indicate 30 to 100% identity, and red bars indicate <30% identity.
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Figure 1: Amino acid sequence alignment of FbpB homologues in Lactobacillus species. The colored boxes represent domains predicted by InterProScan 5. The bar graph shows the mean pairwise identity across homologues at each position in the amino acid alignment (positions 1 to 473, labeled at top). Green bars indicate 100% identity, yellow bars indicate 30 to 100% identity, and red bars indicate <30% identity.

Mentions: Bioinformatic analysis of L. acidophilus NCFM led to the identification of fbpB (lba0191), which was predicted to encode a fibronectin-binding protein. This protein was 463 amino acids in length and contained a putative C-terminal fibronectin type III domain (FN3) (cd00063) with a cytokine receptor motif (Fig. 1). A signal peptidase cleavage site was predicted between residues 24 and 25 (VQA/GT) of the hydrophobic N terminus. The 52-kDa protein has a basic isoelectric point (pI, ∼9.6) and a predicted GRAVY value of −0.589. No transmembrane domains were detected in the protein sequence of FbpB from L. acidophilus NCFM.


Functional Analysis of an S-Layer-Associated Fibronectin-Binding Protein in Lactobacillus acidophilus NCFM.

Hymes JP, Johnson BR, Barrangou R, Klaenhammer TR - Appl. Environ. Microbiol. (2016)

Amino acid sequence alignment of FbpB homologues in Lactobacillus species. The colored boxes represent domains predicted by InterProScan 5. The bar graph shows the mean pairwise identity across homologues at each position in the amino acid alignment (positions 1 to 473, labeled at top). Green bars indicate 100% identity, yellow bars indicate 30 to 100% identity, and red bars indicate <30% identity.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4836419&req=5

Figure 1: Amino acid sequence alignment of FbpB homologues in Lactobacillus species. The colored boxes represent domains predicted by InterProScan 5. The bar graph shows the mean pairwise identity across homologues at each position in the amino acid alignment (positions 1 to 473, labeled at top). Green bars indicate 100% identity, yellow bars indicate 30 to 100% identity, and red bars indicate <30% identity.
Mentions: Bioinformatic analysis of L. acidophilus NCFM led to the identification of fbpB (lba0191), which was predicted to encode a fibronectin-binding protein. This protein was 463 amino acids in length and contained a putative C-terminal fibronectin type III domain (FN3) (cd00063) with a cytokine receptor motif (Fig. 1). A signal peptidase cleavage site was predicted between residues 24 and 25 (VQA/GT) of the hydrophobic N terminus. The 52-kDa protein has a basic isoelectric point (pI, ∼9.6) and a predicted GRAVY value of −0.589. No transmembrane domains were detected in the protein sequence of FbpB from L. acidophilus NCFM.

Bottom Line: Bacterial surface layers (S-layers) are crystalline arrays of self-assembling proteinaceous subunits called S-layer proteins (Slps) that comprise the outermost layer of the cell envelope.To investigate the functional role of LBA0191 (designated FbpB) in L. acidophilus NCFM, an fbpB-deficient strain was constructed.The L. acidophilus mutant with a deletion off bpB lost the ability to adhere to mucin and fibronectin in vitro Homologues off bpB were identified in five additional putative S-layer-forming species, but no homologues were detected in species outside theL. acidophilus homology group.

View Article: PubMed Central - PubMed

Affiliation: Department of Food, Bioprocessing, and Nutrition Sciences, North Carolina State University, Raleigh, North Carolina, USA.

No MeSH data available.


Related in: MedlinePlus