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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

Neighbor-joining phylogenetic tree based on fibronectin-binding proteins in L. acidophilus NCFM and other fbpB-containing lactobacilli. FbpA and FbpB protein sequences were aligned, and the phylogenetic tree was created in Geneious 8.1.7.
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Figure 3: Neighbor-joining phylogenetic tree based on fibronectin-binding proteins in L. acidophilus NCFM and other fbpB-containing lactobacilli. FbpA and FbpB protein sequences were aligned, and the phylogenetic tree was created in Geneious 8.1.7.

Mentions: An unrooted phylogenetic tree was constructed from an alignment of the two known fibronectin-binding proteins in the L. acidophilus homology group, FbpA and FbpB (Fig. 3). The two distinct clusters in the tree illustrate the low sequence identity between the two proteins. For each set of proteins, homologues share identities of at least 75%, with the exception of FbpB in L. amylovorus. The two groups contain different functional domains for binding fibronectin. In FbpA, a fibronectin-binding domain similar to that of Fbp54 in Staphylococcus aureus is considered the functional domain involved in binding. This domain is unrelated to the FN3 domain found in FbpB. The signal peptide cleavage sequence of FbpB in L. acidophilus (VQA/GT) was conserved in L. crispatus, L, kitasatonis, L. gallinarum, and L. helveticus. Although the signal peptide cleavage sequence varies in strains of L. amylovorus (VNA/AS), the position of the cleavage site was conserved.


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)

Neighbor-joining phylogenetic tree based on fibronectin-binding proteins in L. acidophilus NCFM and other fbpB-containing lactobacilli. FbpA and FbpB protein sequences were aligned, and the phylogenetic tree was created in Geneious 8.1.7.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 3: Neighbor-joining phylogenetic tree based on fibronectin-binding proteins in L. acidophilus NCFM and other fbpB-containing lactobacilli. FbpA and FbpB protein sequences were aligned, and the phylogenetic tree was created in Geneious 8.1.7.
Mentions: An unrooted phylogenetic tree was constructed from an alignment of the two known fibronectin-binding proteins in the L. acidophilus homology group, FbpA and FbpB (Fig. 3). The two distinct clusters in the tree illustrate the low sequence identity between the two proteins. For each set of proteins, homologues share identities of at least 75%, with the exception of FbpB in L. amylovorus. The two groups contain different functional domains for binding fibronectin. In FbpA, a fibronectin-binding domain similar to that of Fbp54 in Staphylococcus aureus is considered the functional domain involved in binding. This domain is unrelated to the FN3 domain found in FbpB. The signal peptide cleavage sequence of FbpB in L. acidophilus (VQA/GT) was conserved in L. crispatus, L, kitasatonis, L. gallinarum, and L. helveticus. Although the signal peptide cleavage sequence varies in strains of L. amylovorus (VNA/AS), the position of the cleavage site was conserved.

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