Role of
            <i>Tannerella forsythia</i>
            NanH Sialidase in Epithelial Cell Attachment

Honma, Kiyonobu; Mishima, Elina; Sharma, Ashu

doi:10.1128/iai.00629-10

Cited by 61 publications

(80 citation statements)

References 43 publications

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“…forsythia has been detected intra-cellularly in buccal and crevicular epithelium of patients with periodontitis (Rudney et al, 2005) and has been shown to invade epithelial cells in vitro (Inagaki et al, 2006;Mishima and Sharma, 2011). We observed over-representation in periodontitis of a homolog of the cell-surface-associated protein sialidase NanH (locus VBITanFor42681_2003) required for attachment to epithelial cells (Honma et al, 2011).…”

Section: Discussionmentioning

confidence: 70%

Community-wide transcriptome of the oral microbiome in subjects with and without periodontitis

Duran-Pinedo¹,

et al. 2014

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Despite increasing knowledge on phylogenetic composition of the human microbiome, our understanding of the in situ activities of the organisms in the community and their interactions with each other and with the environment remains limited. Characterizing gene expression profiles of the human microbiome is essential for linking the role of different members of the bacterial communities in health and disease. The oral microbiome is one of the most complex microbial communities in the human body and under certain circumstances, not completely understood, the healthy microbial community undergoes a transformation toward a pathogenic state that gives rise to periodontitis, a polymicrobial inflammatory disease. We report here the in situ genome-wide transcriptome of the subgingival microbiome in six periodontally healthy individuals and seven individuals with periodontitis. The overall picture of metabolic activities showed that iron acquisition, lipopolysaccharide synthesis and flagellar synthesis were major activities defining disease. Unexpectedly, the vast majority of virulence factors upregulated in subjects with periodontitis came from organisms that are not considered major periodontal pathogens. One of the organisms whose gene expression profile was characterized was the uncultured candidate division TM7, showing an upregulation of putative virulence factors in the diseased community. These data enhance understanding of the core activities that are characteristic of periodontal disease as well as the role that individual organisms in the subgingival community play in periodontitis.

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Section: Discussionmentioning

confidence: 70%

Community-wide transcriptome of the oral microbiome in subjects with and without periodontitis

Duran-Pinedo¹,

et al. 2014

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“…While a number of periodontal bacteria are known to exploit host sialylated glycoproteins as a nutrient source, sialidase activity also plays an important role in their pathogenicity. Sialidase treatment of immunoglobulins can make them more susceptible to proteolytic degradation; sialidases may also reveal cryptic receptors and/or adhesion sites for bacterial binding/interaction and hence tissue and host tropism (5,19). Our studies have identified three sialidase-related genes in P. gingivalis which have shown a specific pattern of clustering with other related genes from the bacteria.…”

Section: Discussionmentioning

confidence: 85%

Sialidase and Sialoglycoproteases Can Modulate Virulence in Porphyromonas gingivalis

et al. 2011

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The Porphyromonas gingivalis recombinant VimA can interact with the gingipains and several other proteins, including a sialidase. Sialylation can be involved in protein maturation; however, its role in virulence regulation in P. gingivalis is unknown. The three sialidase-related proteins in P. gingivalis showed the characteristic sialidase Asp signature motif (SXDXGXTW) and other unique domains. To evaluate the roles of the associated genes, randomly chosen P. gingivalis isogenic mutants created by allelic exchange and designated FLL401 (PG0778::ermF), FLL402 (PG1724::ermF), and FLL403 (PG0352::ermF-ermAM) were characterized. Similar to the wild-type strain, FLL402 and FLL403 displayed a black-pigmented phenotype in contrast to FLL401, which was not black pigmented. Sialidase activity in P. gingivalis FLL401 was reduced by approximately 70% in comparison to those in FLL402 and FLL403, which were reduced by approximately 42% and 5%, respectively. Although there were no changes in the expression of the gingipain genes, their activities were reduced by 60 to 90% in all the isogenic mutants compared to that for the wild type. Immunoreactive bands representing the catalytic domains for RgpA, RgpB, and Kgp were present in FLL402 and FLL403 but were missing in FLL401. While adhesion was decreased, the capacity for invasion of epithelial cells by the isogenic mutants was increased by 11 to 16% over that of the wild-type strain. Isogenic mutants defective in PG0778 and PG0352 were more sensitive to hydrogen peroxide than the wild type. Taken together, these results suggest that the P. gingivalis sialidase activity may be involved in regulating gingipain activity and other virulence factors and may be important in the pathogenesis of this organism.

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“…Neuraminidase activity has also been detected in several oral bacteria, such as Tannerella forsythia and Porphyromonas gingivalis (44,66). T. forsythia possesses two neuraminidases, and one of them (NanH) is associated with bacterial colonization and invasion (28,51).…”

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confidence: 99%

Abrogation of Neuraminidase Reduces Biofilm Formation, Capsule Biosynthesis, and Virulence of Porphyromonas gingivalis

Kurniyati

Hu³

et al. 2012

Infect Immun

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The oral bacterium Porphyromonas gingivalis is a key etiological agent of human periodontitis, a prevalent chronic disease that affects up to 80% of the adult population worldwide. P. gingivalis exhibits neuraminidase activity. However, the enzyme responsible for this activity, its biochemical features, and its role in the physiology and virulence of P. gingivalis remain elusive. In this report, we found that P. gingivalis encodes a neuraminidase, PG0352 (Sia Pg ). Transcriptional analysis showed that PG0352 is monocistronic and is regulated by a sigma 70 -like promoter. Biochemical analyses demonstrated that Sia Pg is an exo-␣-neuraminidase that cleaves glycosidic-linked sialic acids. Cryoelectron microscopy and tomography analyses revealed that the PG0352 deletion mutant (⌬PG352) failed to produce an intact capsule layer. Compared to the wild type, in vitro studies showed that ⌬PG352 formed less biofilm and was less resistant to killing by the host complement. In vivo studies showed that while the wild type caused a spreading type of infection that affected multiple organs and all infected mice were killed, ⌬PG352 only caused localized infection and all animals survived. Taken together, these results demonstrate that Sia Pg is an important virulence factor that contributes to the biofilm formation, capsule biosynthesis, and pathogenicity of P. gingivalis, and it can potentially serve as a new target for developing therapeutic agents against P. gingivalis infection.

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Role of Tannerella forsythia NanH Sialidase in Epithelial Cell Attachment

Cited by 61 publications

References 43 publications

Community-wide transcriptome of the oral microbiome in subjects with and without periodontitis

Community-wide transcriptome of the oral microbiome in subjects with and without periodontitis

Sialidase and Sialoglycoproteases Can Modulate Virulence in Porphyromonas gingivalis

Abrogation of Neuraminidase Reduces Biofilm Formation, Capsule Biosynthesis, and Virulence of Porphyromonas gingivalis

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