Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: A possible implication in dental root caries and endocarditis

2006 ◽  
Vol 343 (3) ◽  
pp. 787-792 ◽  
Author(s):  
Thomas K. Han ◽  
Chi Zhang ◽  
My Lien Dao
Keyword(s):  
Streptococcus Mutans ◽  
Protein A ◽  
Binding Activity ◽  
Root Caries ◽  
Collagen Binding ◽  
Identification And Characterization

Identification and characterization of a collagen-binding protein, Cbm, in Streptococcus mutans

2012 ◽  
Vol 27 (4) ◽  
pp. 308-323 ◽  
Author(s):  
R. Nomura ◽  
K. Nakano ◽  
S. Naka ◽  
H. Nemoto ◽  
K. Masuda ◽  
...  
Keyword(s):  
Streptococcus Mutans ◽  
Binding Protein ◽  
Collagen Binding ◽  
Identification And Characterization

Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin

2010 ◽  
Vol 55 (1) ◽  
pp. 34-39 ◽  
Author(s):  
K. Nakano ◽  
R. Nomura ◽  
N. Taniguchi ◽  
J. Lapirattanakul ◽  
A. Kojima ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Streptococcus Mutans ◽  
Gene Encoding ◽  
Collagen Binding

Identification and characterization of enolase as a collagen-binding protein inLactobacillus plantarum

2015 ◽  
Vol 55 (7) ◽  
pp. 890-897 ◽  
Author(s):  
Marzia Salzillo ◽  
Valeria Vastano ◽  
Ugo Capri ◽  
Lidia Muscariello ◽  
Margherita Sacco ◽  
...  
Keyword(s):  
Binding Protein ◽  
Collagen Binding ◽  
Identification And Characterization

scholarly journals A Nonfimbrial Adhesin ofAggregatibacter actinomycetemcomitansMediates Biofilm Biogenesis

2018 ◽  
Vol 87 (1) ◽  
Author(s):  
David R. Danforth ◽  
Gaoyan Tang-Siegel ◽  
Teresa Ruiz ◽  
Keith P. Mintz
Keyword(s):  
Biofilm Formation ◽  
Protein A ◽  
Three Dimensional ◽  
Binding Activity ◽  
Periodontal Pathogen ◽  
Collagen Binding ◽  
Content Type ◽  
Mutant Strains ◽  
Different Strains ◽  
Biofilm Development

ABSTRACTPeriodontitis is an inflammatory disease caused by polymicrobial biofilms. The periodontal pathogenAggregatibacter actinomycetemcomitansdisplays two proteinaceous surface structures, the fimbriae and the nonfimbrial extracellular matrix binding protein A (EmaA), as observed by electron microscopy. Fimbriae participate in biofilm biogenesis and the EmaA adhesins mediate collagen binding. However, in the absence of fimbriae,A. actinomycetemcomitansstill retains the potential to form robust biofilms, suggesting that other surface macromolecules participate in biofilm development. Here, isogenic mutant strains lacking EmaA structures, but still expressing fimbriae, were observed to have reduced biofilm potential. In strains lacking both EmaA and fimbriae, biofilm mass was reduced by 80%. EmaA enhanced biofilm formation in different strains, independent of the fimbriation state or serotype. Confocal microscopy revealed differences in cell density within microcolonies between the EmaA positive and mutant strains. EmaA-mediated biofilm formation was found to be independent of the glycosylation state and the precise three-dimensional conformation of the protein, and thus this function is uncorrelated with collagen binding activity. The data suggest that EmaA is a multifunctional adhesin that utilizes different mechanisms to enhance bacterial binding to collagen and to enhance biofilm formation, both of which are important forA. actinomycetemcomitanscolonization and subsequent infection.

scholarly journals Biochemical and Molecular Characterization of a Novel Type of Mutanase from Paenibacillus sp. Strain RM1: Identification of Its Mutan-Binding Domain, Essential for Degradation of Streptococcus mutans Biofilms

2008 ◽  
Vol 74 (9) ◽  
pp. 2759-2765 ◽  
Author(s):  
Isao Shimotsuura ◽  
Hiromitsu Kigawa ◽  
Motoyasu Ohdera ◽  
Howard K. Kuramitsu ◽  
Syozi Nakashima
Keyword(s):  
Streptococcus Mutans ◽  
Structural Integrity ◽  
Binding Activity ◽  
Etiologic Agent ◽  
Binding Domain ◽  
Intact Protein ◽  
Calculated Molecular Mass ◽  
Terminal Domain ◽  
Paenibacillus Sp

ABSTRACT A novel type of mutanase (termed mutanase RM1) was isolated from Paenibacillus sp. strain RM1. The purified enzyme specifically hydrolyzed α-1,3-glucan (mutan) and effectively degraded biofilms formed by Streptococcus mutans, a major etiologic agent in the progression of dental caries, even following brief incubation. The nucleotide sequence of the gene for this protein contains a 3,873-bp open reading frame encoding 1,291 amino acids with a calculated molecular mass of 135 kDa. The protein contains two major domains, the N-terminal domain (277 residues) and the C-terminal domain (937 residues), separated by a characteristic sequence composed of proline and threonine repeats. The characterization of the recombinant proteins for each domain which were expressed in Escherichia coli demonstrated that the N-terminal domain had strong mutan-binding activity but no mutanase activity whereas the C-terminal domain was responsible for mutanase activity but had mutan-binding activity significantly lower than that of the intact protein. Importantly, the biofilm-degrading activity observed with the intact protein was not exhibited by either domain alone or in combination with the other. Therefore, these results indicate that the structural integrity of mutanase RM1 containing the N-terminal mutan-binding domain is required for the biofilm-degrading activity.

scholarly journals Genomic Organization of the S Locus: Identification and Characterization of Genes in SLG/SRK Region of S9 Haplotype of Brassica campestris (syn. rapa)

Genetics ◽  
1999 ◽  
Vol 153 (1) ◽  
pp. 391-400 ◽  
Author(s):  
Go Suzuki ◽  
Naoko Kai ◽  
Tamaki Hirose ◽  
Kiichi Fukui ◽  
Takeshi Nishio ◽  
...  
Keyword(s):  
Brassica Campestris ◽  
Protein A ◽  
S Locus ◽  
Cysteine Rich Protein ◽  
Pollen Coat ◽  
Genes Encoding ◽  
Gene Rich Region ◽  
Identification And Characterization ◽  
S Locus Glycoprotein

Abstract In Brassica, two self-incompatibility genes, encoding SLG (S locus glycoprotein) and SRK (S-receptor kinase), are located at the S locus and expressed in the stigma. Recent molecular analysis has revealed that the S locus is highly polymorphic and contains several genes, i.e., SLG, SRK, the as-yet-unidentified pollen S gene(s), and other linked genes. In the present study, we searched for expressed sequences in a 76-kb SLG/SRK region of the S9 haplotype of Brassica campestris (syn. rapa) and identified 10 genes in addition to the four previously identified (SLG9, SRK9, SAE1, and SLL2) in this haplotype. This gene density (1 gene/5.4 kb) suggests that the S locus is embedded in a gene-rich region of the genome. The average G + C content in this region is 32.6%. An En/Spm-type transposon-like element was found downstream of SLG9. Among the genes we identified that had not previously been found to be linked to the S locus were genes encoding a small cysteine-rich protein, a J-domain protein, and an antisilencing protein (ASF1) homologue. The small cysteine-rich protein was similar to a pollen coat protein, named PCP-A1, which had previously been shown to bind SLG.

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