Limits...
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

Putative SLAPs of parent and ΔfbpB strains (NCK1909 and NCK2393). Proteins were extracted by washing in LiCl and dialyzing in molecular porous membranes. Relative molecular masses are labeled (ladder). Lane 1, SLAPs from parent, NCK1909; lane 2, pure SlpA from parent, NCK1909; lane 3, SLAPs from ΔfbpB mutant. The faint band remaining at ∼52 kDa (corresponding to FbpB) in lane 3 is likely from SLAPs of similar size (SlpX, 54 kDa; LBA0864, 55 kDa).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4836419&req=5

Figure 6: Putative SLAPs of parent and ΔfbpB strains (NCK1909 and NCK2393). Proteins were extracted by washing in LiCl and dialyzing in molecular porous membranes. Relative molecular masses are labeled (ladder). Lane 1, SLAPs from parent, NCK1909; lane 2, pure SlpA from parent, NCK1909; lane 3, SLAPs from ΔfbpB mutant. The faint band remaining at ∼52 kDa (corresponding to FbpB) in lane 3 is likely from SLAPs of similar size (SlpX, 54 kDa; LBA0864, 55 kDa).

Mentions: Electrophoresis of SLAP extractions revealed nearly identical protein banding patterns in the parent strain and the ΔfbpB mutant (Fig. 6). The faint band remaining at ∼52 kDa (corresponding to FbpB) in lane 3 of Fig. 6 is likely from SLAPs of similar size (SlpX, 54 kDa; LBA0864, 55 kDa).


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)

Putative SLAPs of parent and ΔfbpB strains (NCK1909 and NCK2393). Proteins were extracted by washing in LiCl and dialyzing in molecular porous membranes. Relative molecular masses are labeled (ladder). Lane 1, SLAPs from parent, NCK1909; lane 2, pure SlpA from parent, NCK1909; lane 3, SLAPs from ΔfbpB mutant. The faint band remaining at ∼52 kDa (corresponding to FbpB) in lane 3 is likely from SLAPs of similar size (SlpX, 54 kDa; LBA0864, 55 kDa).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 6: Putative SLAPs of parent and ΔfbpB strains (NCK1909 and NCK2393). Proteins were extracted by washing in LiCl and dialyzing in molecular porous membranes. Relative molecular masses are labeled (ladder). Lane 1, SLAPs from parent, NCK1909; lane 2, pure SlpA from parent, NCK1909; lane 3, SLAPs from ΔfbpB mutant. The faint band remaining at ∼52 kDa (corresponding to FbpB) in lane 3 is likely from SLAPs of similar size (SlpX, 54 kDa; LBA0864, 55 kDa).
Mentions: Electrophoresis of SLAP extractions revealed nearly identical protein banding patterns in the parent strain and the ΔfbpB mutant (Fig. 6). The faint band remaining at ∼52 kDa (corresponding to FbpB) in lane 3 of Fig. 6 is likely from SLAPs of similar size (SlpX, 54 kDa; LBA0864, 55 kDa).

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