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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

Conserved genomic context of FbpB homologues in the genomes of closely related lactobacilli (top group of species). The transcriptional profile graph shows RNA coverage over the contextual region of four species with FbpB homologues (blue, L. acidophilus NCFM; red, L. amylovorus GRL1112; green, L. crispatus ST1; purple, L. helveticus CNRZ32). The genome of L. helveticus (asterisk) contains a putative 1.3-kb mobile genetic element between the glucan modification protein and FbpB. The region of the transcriptional profile corresponding to the mobile genetic element was deleted from L. helveticus CNRZ32 to allow for comparison to other species. FbpB is absent from all other lactobacilli, although the genomic context is conserved in many species (bottom group of species). The percent identity values indicate amino acid sequence similarity of respective open reading frames (ORFs).
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Figure 2: Conserved genomic context of FbpB homologues in the genomes of closely related lactobacilli (top group of species). The transcriptional profile graph shows RNA coverage over the contextual region of four species with FbpB homologues (blue, L. acidophilus NCFM; red, L. amylovorus GRL1112; green, L. crispatus ST1; purple, L. helveticus CNRZ32). The genome of L. helveticus (asterisk) contains a putative 1.3-kb mobile genetic element between the glucan modification protein and FbpB. The region of the transcriptional profile corresponding to the mobile genetic element was deleted from L. helveticus CNRZ32 to allow for comparison to other species. FbpB is absent from all other lactobacilli, although the genomic context is conserved in many species (bottom group of species). The percent identity values indicate amino acid sequence similarity of respective open reading frames (ORFs).

Mentions: Three genes immediately upstream of fbpB and one gene immediately downstream of fbpB were conserved among all occurrences of homologues (Fig. 2). In contrast, this genomic context was present with no medial fbpB homologue in the genomes of closely related lactobacilli, including L. acetotolerans, L. apis, L. gigeriorum, L. hamsteri, L helsingborgensis, L. intestinalis, L. kalixensis, L. kimbladii, L. kullabergensis, L. kefiranofaciens, L. melliventris, L. pasteurii, and L. ultunensis. In these genomes, no such fbpB homologues were present, and the tyrosyl-tRNA synthetase gene was located directly downstream of the glucan modification gene. The G+C content of fbpB was consistent across species, ranging from 35.7% to 38.3%. Each of these values varied by <1% from the overall G+C content of each full genome (34.7% to 38.2%).


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)

Conserved genomic context of FbpB homologues in the genomes of closely related lactobacilli (top group of species). The transcriptional profile graph shows RNA coverage over the contextual region of four species with FbpB homologues (blue, L. acidophilus NCFM; red, L. amylovorus GRL1112; green, L. crispatus ST1; purple, L. helveticus CNRZ32). The genome of L. helveticus (asterisk) contains a putative 1.3-kb mobile genetic element between the glucan modification protein and FbpB. The region of the transcriptional profile corresponding to the mobile genetic element was deleted from L. helveticus CNRZ32 to allow for comparison to other species. FbpB is absent from all other lactobacilli, although the genomic context is conserved in many species (bottom group of species). The percent identity values indicate amino acid sequence similarity of respective open reading frames (ORFs).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 2: Conserved genomic context of FbpB homologues in the genomes of closely related lactobacilli (top group of species). The transcriptional profile graph shows RNA coverage over the contextual region of four species with FbpB homologues (blue, L. acidophilus NCFM; red, L. amylovorus GRL1112; green, L. crispatus ST1; purple, L. helveticus CNRZ32). The genome of L. helveticus (asterisk) contains a putative 1.3-kb mobile genetic element between the glucan modification protein and FbpB. The region of the transcriptional profile corresponding to the mobile genetic element was deleted from L. helveticus CNRZ32 to allow for comparison to other species. FbpB is absent from all other lactobacilli, although the genomic context is conserved in many species (bottom group of species). The percent identity values indicate amino acid sequence similarity of respective open reading frames (ORFs).
Mentions: Three genes immediately upstream of fbpB and one gene immediately downstream of fbpB were conserved among all occurrences of homologues (Fig. 2). In contrast, this genomic context was present with no medial fbpB homologue in the genomes of closely related lactobacilli, including L. acetotolerans, L. apis, L. gigeriorum, L. hamsteri, L helsingborgensis, L. intestinalis, L. kalixensis, L. kimbladii, L. kullabergensis, L. kefiranofaciens, L. melliventris, L. pasteurii, and L. ultunensis. In these genomes, no such fbpB homologues were present, and the tyrosyl-tRNA synthetase gene was located directly downstream of the glucan modification gene. The G+C content of fbpB was consistent across species, ranging from 35.7% to 38.3%. Each of these values varied by <1% from the overall G+C content of each full genome (34.7% to 38.2%).

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