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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

Percent adherence of ΔfbpB mutant (NCK2393) to fibronectin, mucin, and collagen substrates relative to the parent strain (NCK1909, 100%). The data presented here are means and standard errors from the results from three independent replicates. Asterisks indicate significance (mucin, P < 0.02; fibronectin, P < 0.01).
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Figure 4: Percent adherence of ΔfbpB mutant (NCK2393) to fibronectin, mucin, and collagen substrates relative to the parent strain (NCK1909, 100%). The data presented here are means and standard errors from the results from three independent replicates. Asterisks indicate significance (mucin, P < 0.02; fibronectin, P < 0.01).

Mentions: The ΔfbpB mutant exhibited a statistically significant reduction in adherence to fibronectin and mucin in vitro relative to that of the parent strain (Fig. 4). Adherence of the ΔfbpB mutant to human plasma fibronectin was reduced by 72%, and adherence to type III mucin from porcine stomach was reduced by 47%. The ΔfbpB mutant exhibited no significant reduction in adhesion (7.2%) to type IV collagen.


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)

Percent adherence of ΔfbpB mutant (NCK2393) to fibronectin, mucin, and collagen substrates relative to the parent strain (NCK1909, 100%). The data presented here are means and standard errors from the results from three independent replicates. Asterisks indicate significance (mucin, P < 0.02; fibronectin, P < 0.01).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 4: Percent adherence of ΔfbpB mutant (NCK2393) to fibronectin, mucin, and collagen substrates relative to the parent strain (NCK1909, 100%). The data presented here are means and standard errors from the results from three independent replicates. Asterisks indicate significance (mucin, P < 0.02; fibronectin, P < 0.01).
Mentions: The ΔfbpB mutant exhibited a statistically significant reduction in adherence to fibronectin and mucin in vitro relative to that of the parent strain (Fig. 4). Adherence of the ΔfbpB mutant to human plasma fibronectin was reduced by 72%, and adherence to type III mucin from porcine stomach was reduced by 47%. The ΔfbpB mutant exhibited no significant reduction in adhesion (7.2%) to type IV collagen.

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