Purification, crystallization and preliminary crystallographic analysis of the SpaA backbone-pilin subunit from probiotic<i>Lactobacillus rhamnosus</i>GG

Singh, Deepak; Ossowski, Ingemar von; Palva, Airi; Krishnan, Vengadesan

doi:10.1107/s1744309113024676

Cited by 13 publications

(20 citation statements)

References 13 publications

(12 reference statements)

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“…This was expected as bacterial adhesion to cellular surfaces is multifactorial and involves different specific and non-specific interactions between bacterial and cell surface components. Non-specific mechanisms involve electrostatic and hydrophobic interactions, whereas the specific mechanisms are related to surface molecules, such as outer membrane proteins (Frece et al, 2005; Chen et al, 2007; Johnson-Henry et al, 2007; Zhang et al, 2013; Meng et al, 2014), exopolysaccharides (EPSs, Lebeer et al, 2011), lipoteichoic acids (Granato et al, 1999), peptidoglycans (Van Tassell and Miller, 2011), glycosaminoglycans (Martin et al, 2013), flagella, and fimbriae (Singh et al, 2013). This complex scenario results in species-specific adhesion (Deepika and Charalampopoulos, 2010; Messaoudi et al, 2012; Verdenelli et al, 2014) and may be related to the differences observed in the present study.…”

Section: Discussionmentioning

confidence: 99%

Lactobacillus fermentum ATCC 23271 Displays In vitro Inhibitory Activities against Candida spp.

et al. 2016

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Lactobacilli are involved in the microbial homeostasis in the female genital tract. Due to the high prevalence of many bacterial diseases of the female genital tract and the resistance of microorganisms to various antimicrobial agents, alternative means to control these infections are necessary. Thus, this study aimed to evaluate the probiotic properties of well-characterized Lactobacillus species, including L. acidophilus (ATCC 4356), L. brevis (ATCC 367), L. delbrueckii ssp. delbrueckii (ATCC 9645), L. fermentum (ATCC 23271), L. paracasei (ATCC 335), L. plantarum (ATCC 8014), and L. rhamnosus (ATCC 9595), against Candida albicans (ATCC 18804), Neisseria gonorrhoeae (ATCC 9826), and Streptococcus agalactiae (ATCC 13813). The probiotic potential was investigated by using the following criteria: (i) adhesion to host epithelial cells and mucus, (ii) biofilm formation, (iii) co-aggregation with bacterial pathogens, (iv) inhibition of pathogen adhesion to mucus and HeLa cells, and (v) antimicrobial activity. Tested lactobacilli adhered to mucin, co-aggregated with all genital microorganisms, and displayed antimicrobial activity. With the exception of L. acidophilus and L. paracasei, they adhered to HeLa cells. However, only L. fermentum produced a moderate biofilm and a higher level of co-aggregation and mucin binding. The displacement assay demonstrated that all Lactobacillus strains inhibit C. albicans binding to mucin (p < 0.001), likely due to the production of substances with antimicrobial activity. Clinical isolates belonging to the most common Candida species associated to vaginal candidiasis were inhibited by L. fermentum. Collectively, our data suggest that L. fermentum ATCC 23271 is a potential probiotic candidate, particularly to complement candidiasis treatment, since presented with the best probiotic profile in comparison with the other tested lactobacilli strains.

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Section: Discussionmentioning

confidence: 99%

Lactobacillus fermentum ATCC 23271 Displays In vitro Inhibitory Activities against Candida spp.

et al. 2016

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“…The molecular packing in the crystal resembles native pili, with each C‐terminus adjacent to a linking lysine of the next molecule. A backbone pilin, SpaA in SpaCBA pili from L. rhamnosus GG is also a two‐domain backbone pilin (unpublished data, ).…”

Section: Backbone Pilinsmentioning

confidence: 92%

“…Structural information of pilins in non‐pathogenic bacteria is yet to emerge. However, preliminary data is available for two backbone pilins, SpaA and SpaD . Like Spy0128, SpaA is a two‐domain pilin.…”

Section: Pilins From Non‐pathogenic Gram‐positive Bacteriamentioning

confidence: 99%

“…B) described below appears conserved across several Gram‐positive pathogenic strains . Recently, pilins were also been identified in non‐pathogenic bacteria like Lactobacillus rhamnosus GG , and structural information has begun to emerge . There are also recent structural reports for pilins ( e.g ., PilJ and PilA1), which form Type IV pili in Gram‐positive bacteria similar to Gram‐negative bacteria .…”

Section: Introductionmentioning

confidence: 99%

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Pilins in gram‐positive bacteria: A structural perspective

Krishnan

2015

IUBMB Life

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Pilins or fimbrilins are a class of proteins found in bacterial surface pilus, a hair-like surface appendage. Both the Gramnegative and -positive bacteria produce pilins to assemble pili on their cell-surface for different purposes including adherence, twitching motility, conjugation, immunomodulation, biofilm formation, and electron transfer. Immunogenic properties of the pilins make them attractive vaccine candidates. The polymerized pilins play a key role in the initiation of host adhesion, which is a critical step for bacterial colonization and infection. Because of their key role in adhesion and exposure on the cell surface, targeting the pilins-mediated adhesion (anti-adhesion therapy) is also seen as a promising alternative approach for preventing and treating bacterial infections, one that may overcome their ever-increasing repertoires of resistance mechanisms. Individual pilins interact with each other non-covalently to assemble the pilus fiber with the help of associated proteins like chaperones and Usher in Gramnegative bacteria. In contrast, the pilins in Gram-positive bacteria often connect with each other covalently, with the help of sortases. Certain unique structural features present on the pilins distinguish them from one another across different bacterial strains, and these dictate their cellular targets and functions. While the structure of pilins has been extensively studied in Gram-negative pathogenic bacteria, the pilins in Gram-positive pathogenic bacteria have been in only during the last decade. Recently, the discovery of pilins in nonpathogenic bacteria, such as Lactobacillus rhamnosus GG, has received great attention, though traditionally the attention was on pathogenic bacteria. This review summarizes and discusses the current structural knowledge of pilins in Gram-positive bacteria with emphasis on those pilins which are sortase substrates. V C 2015 IUBMB Life, 67(7): [533][534][535][536][537][538][539][540][541][542][543] 2015

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“…Hence, a similar structural approach using the TG/SG motif would further contribute to understanding the docking details of sortases and their dedicated substrates in L. rhamnosus GG and other Gram-positive species. A recent report indicated that the structure of the SpaA pilin of L. rhamnosus GG is soon to be solved, bringing to light important data to support the present regulatory model (58).…”

Section: Discussionmentioning

confidence: 99%

Functional Identification of Conserved Residues Involved in Lactobacillus rhamnosus Strain GG Sortase Specificity and Pilus Biogenesis

Douillard

Rasinkangas

Ossowski

et al. 2014

Journal of Biological Chemistry

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Background: Lactobacillus rhamnosus GG produces pili assembled and anchored by two distinct sortases, SrtC and SrtA, respectively. Results: Residue substitution within the triple glycine (TG) motif of pilin proteins impacts sortase-mediated polymerization. Conclusion:The TG motif determines sortase specificity during pilus biogenesis in GG. Significance: These results help explain the signaling involved in the assembly and anchoring of sortase-dependent pili.

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Purification, crystallization and preliminary crystallographic analysis of the SpaA backbone-pilin subunit from probioticLactobacillus rhamnosusGG

Cited by 13 publications

References 13 publications

Lactobacillus fermentum ATCC 23271 Displays In vitro Inhibitory Activities against Candida spp.

Lactobacillus fermentum ATCC 23271 Displays In vitro Inhibitory Activities against Candida spp.

Pilins in gram‐positive bacteria: A structural perspective

Functional Identification of Conserved Residues Involved in Lactobacillus rhamnosus Strain GG Sortase Specificity and Pilus Biogenesis

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