Active detachment of Streptococcus mutans cells adhered to epon–hydroxylapatite surfaces coated with salivary proteins in vitro

Vats, Neeraj; Lee, Song F.

doi:10.1016/s0003-9969(99)00139-9

Cited by 36 publications

(30 citation statements)

References 28 publications

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“…This may expedite the exchange of coat proteins during an antigenic switch, and at the same time divert the host immune system from live trypanosomes expressing the same VSG. A similar mechanism has been recently observed with the oral pathogen Streptococcus mutans, which expresses an enzyme that releases the adhesin P1 from its cell wall (70). This activity might allow the bacterium to shed P1-antibody complexes or to recolonize after detaching from an adherent surface.…”

Section: Structural Conservation Of Variable Borrelia Lipoproteinssupporting

confidence: 63%

Structural Conservation of Neurotropism-associated VspA within the Variable Borrelia Vsp-OspC Lipoprotein Family

Zückert

Kerentseva

Lawson

et al. 2001

Journal of Biological Chemistry

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Vsp surface lipoproteins are serotype-defining antigens of relapsing fever spirochetes that undergo multiphasic antigenic variation to avoid the immune response. One of these proteins, VspA of Borrelia turicatae, is also associated with neurotropism in infected mice. Vsp proteins are highly polymorphic in sequence, which may relate to their specific antibody reactivities and host cell interactions. To determine whether sequence variations affect protein structure, we compared B. turicatae VspA with three related proteins: VspB of B. turicatae, Vsp26 of the relapsing fever agent Borrelia hermsii, and OspC of the Lyme disease spirochete Borrelia burgdorferi. Recombinant non-lipidated proteins were purified by affinity or ion exchange chromatography. Circular dichroism spectra revealed similar, highly ␣-helical secondary structures for all four proteins. In vitro assays demonstrated proteaseresistant, thermostable Vsp cores starting at a conserved serine at position 34 (Ser 34 ). All proteins aggregate as dimers in solution. In situ trypsin treatment and surface protein cross-linking showed that the native lipoproteins also form protease-resistant dimers. These findings indicate that Vsp proteins have a common compact fold and that their established functions are based on localized polymorphisms. Two forms of VspA crystals suitable for structure determination by x-ray diffraction methods have been obtained.

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Section: Structural Conservation Of Variable Borrelia Lipoproteinssupporting

confidence: 63%

Structural Conservation of Neurotropism-associated VspA within the Variable Borrelia Vsp-OspC Lipoprotein Family

Zückert

Kerentseva

Lawson

et al. 2001

Journal of Biological Chemistry

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“…Chromosomal DNA was isolated from Strep. mutans as described previously (Vats & Lee, 2000). Briefly, cells were harvested by centrifugation from 10 ml of an 18-hold culture in THB, washed in GTE (50 mM glucose ; 25 mM Tris, pH 8n0 ; 10 mM EDTA) and incubated with 10 kU lysozyme and 1 kU mutanolysin per ml GTE at 37 mC for 1-2 h. Cells were lysed with 2 % SDS at room temperature for 10 min.…”

Section: Methodsmentioning

confidence: 99%

“…mutans cells (Vats & Lee, 2000). Upon mapping the Tn917 insertion site, we found that the transposon had inserted adjacent to the promoter region of a small protein that shared extensive homology with the CopY protein of Ent.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a copper-transport operon, copYAZ, from Streptococcus mutans The GenBank accession number for the cop operon sequence reported in this paper is AF296446.

Vats

Lee

2001

Microbiology

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A copper-transport (copYAZ) operon was cloned from the oral bacterium Streptococcus mutans JH1005. DNA sequencing showed that the operon contained three genes (copY, copA and copZ), which were flanked by a single promoter and a factor-independent terminator. copY encoded a small protein of 147 aa with a heavy-metal-binding motif (CXCX 4 CXC) at the C-terminus. CopY shared extensive homology with other bacterial negative transcriptional regulators. copA encoded a 742 aa protein that shared extensive homology with P-type ATPases. copZ encoded a 67 aa protein that also contained a heavymetal-binding motif (CXXC) at the N-terminus. Northern blotting showed that a 32 kb transcript was produced by Cu 2M -induced Strep. mutans cells, suggesting that the genes were synthesized as a polycistronic message. The transcriptional start site of the cop operon was mapped and shown to lie within the inverted repeats of the promoter-operator region. Strep. mutans wild-type cells were resistant to 800 µM Cu 2M , whereas cells of a cop knock-out mutant were killed by 200 µM Cu 2M . Complementation of the cop knock-out mutant with the cop operon restored Cu 2M resistance to wild-type level. The wild-type and the mutant did not show any differences in susceptibility to other heavy metals, suggesting that the operon was specific for copper. By using a chloramphenicol acetyltransferase reporter gene fusion, the cop operon was shown to be negatively regulated by CopY and could be derepressed by Cu 2M .

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“…S. mutans, an initiator of dental plaque, attaches to the surfaces of teeth via its cell surface adhesin P1 using a salivary receptor agglutinin (35). Degradation of P1 by exogenous addition of a surface protein-releasing enzyme (SPRE) leads to detachment of an S. mutants monolayer formed on saliva-conditioned epon-hydroxylapatite rods (332). The importance of SPRE in dispersal is underscored by the fact that SPRE-defective mutants of S. mutans are unable to detach from substrata.…”

Section: Mechanisms Of Dispersalmentioning

confidence: 99%

Signals, Regulatory Networks, and Materials That Build and Break Bacterial Biofilms

Karatan

Watnick

2009

Microbiol Mol Biol Rev

877

690

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SUMMARY Biofilms are communities of microorganisms that live attached to surfaces. Biofilm formation has received much attention in the last decade, as it has become clear that virtually all types of bacteria can form biofilms and that this may be the preferred mode of bacterial existence in nature. Our current understanding of biofilm formation is based on numerous studies of myriad bacterial species. Here, we review a portion of this large body of work including the environmental signals and signaling pathways that regulate biofilm formation, the components of the biofilm matrix, and the mechanisms and regulation of biofilm dispersal.

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Active detachment of Streptococcus mutans cells adhered to epon–hydroxylapatite surfaces coated with salivary proteins in vitro

Cited by 36 publications

References 28 publications

Structural Conservation of Neurotropism-associated VspA within the Variable Borrelia Vsp-OspC Lipoprotein Family

Structural Conservation of Neurotropism-associated VspA within the Variable Borrelia Vsp-OspC Lipoprotein Family

Characterization of a copper-transport operon, copYAZ, from Streptococcus mutans The GenBank accession number for the cop operon sequence reported in this paper is AF296446.

Signals, Regulatory Networks, and Materials That Build and Break Bacterial Biofilms

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