Peptide Mapping of a Functionally Versatile Fimbrial Adhesin from Porphyromonas gingivalis

Hajishengallis, George

doi:10.1007/s10989-007-9084-1

Cited by 8 publications

(13 citation statements)

References 96 publications

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“…Interactions between the major pili of P. gingivalis 33277 (including pilin FimA) and host molecules were studied extensively using peptide mapping (Hajishengallis, 2007). We mapped the adhesion and immune recognition sites onto a homology model of FimA, using FimA4 as a template (Figure 3E).…”

Section: Resultsmentioning

confidence: 99%

“…P. gingivalis pili are key virulence factors that are essential for host colonization and evasion of innate defenses (Amano, 2010; Hajishengallis et al, 2007; Hajishengallis et al, 2008). They are also involved in binding a wide array of oral or epithelial substrates and extracellular matrix proteins (Amano, 2003; Hajishengallis, 2007), in addition to co-aggregation with other pathogens, such as Streptococcus gordonii (Park et al, 2005). Two types of morphologically distinct pili have been identified in P. gingivalis : major or long (0.3 to 1.6 μm) and minor or short (80 to 120 nm) (Hamada et al, 1996; Yoshimura et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

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A Distinct Type of Pilus from the Human Microbiome

Shoji

Shibata

et al. 2016

Cell

157

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Summary Pili are proteinaceous polymers of linked pilins that protrude from the cell surface of many bacteria and often mediate adherence and virulence. We investigated a set of 20 Bacteroidia pilins from the human microbiome whose structures and mechanism of assembly were unknown. Crystal structures and biochemical data revealed a diverse protein superfamily with a common Greek-key β-sandwich fold with two transthyretin-like repeats that polymerize into a pilus through a strand-exchange mechanism. The assembly mechanism of the central, structural pilins involves proteinase-assisted removal of their N-terminal β-strand, creating an extended hydrophobic groove that binds the C-terminal donor strands of the incoming pilin. Accessory pilins at the tip and base have unique structural features specific to their location, allowing initiation or termination of the assembly. The bacteroidia pilus therefore has a biogenesis mechanism that is distinct from other known pili and likely represents a different type of bacterial pilus.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Distinct Type of Pilus from the Human Microbiome

Shoji

Shibata

et al. 2016

Cell

157

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“…Peptide-mapping studies of FimA have defined specific interactive domains involved in these interactions (reviewed in Ref. 16). However, several other P. gingivalis proteins, designated FimC, FimD, and FimE with molecular masses of 50, 80, and 60 kDa, respectively, have been identified as quantitatively minor components (Յ1%) of native fimbriae (17,18).…”

mentioning

confidence: 99%

Fimbrial Proteins of Porphyromonas gingivalis Mediate In Vivo Virulence and Exploit TLR2 and Complement Receptor 3 to Persist in Macrophages

Wang

Shakhatreh

James

et al. 2007

The Journal of Immunology

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179

266

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Porphyromonas gingivalis is an oral/systemic pathogen implicated in chronic conditions, although the mechanism(s) whereby it resists immune defenses and persists in the host is poorly understood. The virulence of this pathogen partially depends upon expression of fimbriae comprising polymerized fimbrillin (FimA) associated with quantitatively minor proteins (FimCDE). In this study, we show that isogenic mutants lacking FimCDE are dramatically less persistent and virulent in a mouse periodontitis model and express shorter fimbriae than the wild type. Strikingly, native fimbriae allowed P. gingivalis to exploit the TLR2/complement receptor 3 pathway for intracellular entry, inhibition of IL-12p70, and persistence in macrophages. This virulence mechanism also required FimCDE; indeed, mutant strains exhibited significantly reduced ability to inhibit IL-12p70, invade, and persist intracellularly, attributable to failure to interact with complement receptor 3, although not with TLR2. These results highlight a hitherto unknown mechanism of immune evasion by P. gingivalis that is surprisingly dependent upon minor constituents of its fimbriae, and support the concept that pathogens evolved to manipulate innate immunity for promoting adaptive fitness and thus their capacity to cause disease.

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“…Fimbriae are adhesive hair-like appendages emanating from the bacterial cell surface (Lamont and Jenkinson 1998, Hajishengallis 2007). The major fimbriae of P. gingivalis are encoded by the fimA operon and are indispensable for colonization and host cell invasion (Lamont and Jenkinson 1998, Hajishengallis 2007).…”

Section: P Gingivalis: Interfering With Host Immunity For the Micrmentioning

confidence: 99%

Pathogenic Microbes and Community Service Through Manipulation of Innate Immunity

Hajishengallis

Krauss

Liang

et al. 2011

Advances in Experimental Medicine and Biology

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The periodontal pathogen Porphyromonas gingivalis undermines major components of innate immunity, such as complement, Toll-like receptors (TLR), and their crosstalk pathways. At least in principle, these subversive activities could promote the adaptive fitness of the entire periodontal biofilm community. In this regard, the virulence factors responsible for complement and TLR exploitation (gingipain enzymes, atypical lipopolysaccharide molecules, and fimbriae) are released as components of readily diffusible membrane vesicles, which can thus become available to other biofilm organisms. This review summarizes important immune subversive tactics of P. gingivalis which might enable it to exert a supportive impact on the oral microbial community.

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Peptide Mapping of a Functionally Versatile Fimbrial Adhesin from Porphyromonas gingivalis

Cited by 8 publications

References 96 publications

A Distinct Type of Pilus from the Human Microbiome

A Distinct Type of Pilus from the Human Microbiome

Fimbrial Proteins of Porphyromonas gingivalis Mediate In Vivo Virulence and Exploit TLR2 and Complement Receptor 3 to Persist in Macrophages

Pathogenic Microbes and Community Service Through Manipulation of Innate Immunity

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