Effect of SrtA on Interspecies Adherence of Oral Bacteria

Song, Ying; He, Jinzhi; Wang, Ren-Ke; Ma, Jia; Zou, Ling

doi:10.1007/s11596-018-1860-y

Cited by 5 publications

(3 citation statements)

References 50 publications

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“…These membrane proteins are fundamental to many biological processes, such as cell division, control of cell volume, and control of which substances pass through the cell membrane. These results may be relevant because of the role of these proteins in the bacterial resistance to antibiotics [42][43][44][45][46].…”

Section: Discussionmentioning

confidence: 98%

Identification and localization of proteins associated with the formation of Streptococcus gordonii and Fusobacterium nucleatum biofilms

Gómez¹,

Bacilio-Amaranto²,

Torres³

et al. 2020

Preprint

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Background:To successfully colonize the oral cavity, bacteria must adhere directly or indirectly to the oral surfaces available. Fusobacterium nucleatum plays an important role in the development of the oral biofilm community due to its broad adhesion capabilities, serving as a bridge between the members of the oral biofilm community that cannot be directly joined together. The purpose of this study was to identify and localize the proteins associated with the formation of biofilms of Streptococcus gordonii and F. nucleatum. Methods: Multispecies biofilms were identified by amplification of the srtA and radD genes by real-time PCR. Biofilm cells cultured with sucrose were counted. The protein concentrations in the membrane and cytoplasmic fractions were quantified by western blot. Results: The proteins HSP40 and GAPDH were detected in the cytoplasmic fraction of biofilm and F. nucleatum, respectively. The available anti-GAPDH antibody is specific for GAPDH produced by F. nucleatum, which indicated the coaggregation of F. nucleatum on S. gordonii. Conclusions: HSP40 was only detected in the cytoplasmic fraction of the biofilms, making it one of the essential proteins for adherence. This complex set of interactions could have critical implications for the formation and maturation of oral biofilms in vivo and could provide clues to the mechanism behind the distribution of organisms within the human oral cavity.

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Section: Discussionmentioning

confidence: 98%

Identification and localization of proteins associated with the formation of Streptococcus gordonii and Fusobacterium nucleatum biofilms

Gómez¹,

Bacilio-Amaranto²,

Torres³

et al. 2020

Preprint

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show abstract

“…The cytoplasmic protein profiles of the biofilms harvested after 1, 4, 7, and 10 days of cultivation remained unchanged over time, demonstrating that the examined proteins are at constant levels throughout different aspects of biofilm formation, such as cell division, control of cell volume, and control of which substances pass through the cell membrane. These results may be relevant because of the role of these proteins in bacterial resistance to antibiotics [42][43][44][45][46].…”

Section: Discussionmentioning

confidence: 99%

Identification of Proteins Associated with the Formation of Oral Biofilms

Gómez

Amaranto

Torres

et al. 2021

Pesqui. Bras. Odontopediatria Clín. Integr.

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Objective: To identify proteins associated with the formation of Streptococcus gordonii and Fusobacterium nucleatum biofilms. Material and Methods: Biofilms composed of two bacterial species, S. gordonii and F. nucleatum, were cultured for 1, 4, 7, and 10 days. The presence of both species was confirmed via amplification of the srtA and radD genes using real-time PCR. The concentrations of proteins associated with the biofilms and individual species were quantified using Western blotting. Results: The protein profiles of S. gordonii and F. nucleatum from individual cultures determined using one-dimensional electrophoresis revealed proteins found in S. gordonii and in F. nucleatum. Ct and reciprocal Ct values were determined for the exposed S. gordonii and F. nucleatum biofilms. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein was detected in biofilms and F. nucleatum, whereas HSP40 protein was present only in biofilms after 7 and 10 days of formation. Conclusion: HSP40 was detected only in the formed biofilms; thus, HSP40 is an essential proteins for adhesion.

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“…The coaggregation assay was performed with the modified method described elsewhere. 28,29 S. mutans, including the wild-type and its mutants, P. gingivalis, P. intermedia, F. nucleatum, S. sanguins, S. salivarius, and A. actinomycetemcomitans were used for this assay. Preliminarily, the coaggregation of S. mutans UA159 with other oral bacteria was investigated.…”

Section: Coaggregation Assaymentioning

confidence: 99%

Comprehensive characterization of sortase A‐dependent surface proteins in Streptococcus mutans

Katsumata

Kawada‐Matsuo

et al. 2022

Microbiology and Immunology

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Streptococcus mutans, a cariogenic pathogen, adheres to the tooth surface and forms a biofilm. Bacterial cell surface proteins are associated with adherence to substrates. Sortase A (SrtA) mediates the localization of proteins with an LPXTG motifcontaining proteins to the cell surface by covalent binding to peptidoglycan. In S. mutans UA159, six SrtA-dependent proteins, SpaP, WapA, WapE, DexA, FruA, and GbpC, were identified. Although some of these proteins were characterized, a comprehensive analysis of the six proteins has not been reported. In this study, we constructed mutants deficient in each of these proteins and the SrtA-deficient mutant. The SrtA-deficient mutant showed drastically decreased binding to salivary components, biofilm formation, bacterial coaggregation activity, hydrophobicity, and cellular matrix binding (collagen type I, fibronectin, and laminin). The SpaP-deficient mutant showed significantly reduced binding to salivary components and partially increased coaggregation with Porphyromonas gingivalis, and decreased hydrophobicity, and collagen binding. The WapA-deficient mutant showed slightly decreased coaggregation with Fusobacterium nucleatum. Although the SrtA-deficient mutant showed drastically altered phenotypes, all SrtA-dependent protein-deficient mutants, except the SpaP-deficient mutant, did not show considerable alterations in binding to salivary components. These results indicate that the six proteins may coordinately contribute to these activities. In addition, using genomic data of 125 S. mutans strains, the amino acid sequences of each surface protein were compared and many variations were found among strains, which may affect the phenotype of cell surface proteins in S. mutans.

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Effect of SrtA on Interspecies Adherence of Oral Bacteria

Cited by 5 publications

References 50 publications

Identification and localization of proteins associated with the formation of Streptococcus gordonii and Fusobacterium nucleatum biofilms

Identification and localization of proteins associated with the formation of Streptococcus gordonii and Fusobacterium nucleatum biofilms

Identification of Proteins Associated with the Formation of Oral Biofilms

Comprehensive characterization of sortase A‐dependent surface proteins in Streptococcus mutans

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