Contribution of &lt;i&gt;Streptococcus gordonii&lt;/i&gt; Hsa Adhesin to Biofilm Formation

Oguchi, Riyo; Takahashi, Yukihiro; Shimazu, Kisaki; Tashiro, Fumio; Kawarai, Taketo; Kawai, Kiyoshi; Karibe, Hiroyuki

doi:10.7883/yoken.jjid.2016.492

Cited by 11 publications

(7 citation statements)

References 38 publications

(51 reference statements)

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“…Other SRRP-BR regions are composed of two or more subdomains and include (from the N to the C terminal) the helical and CnaA folds for Fap1 ( 45 ), the CnaA, sialic acid-binding Ig-like lectin (siglec), and unique subdomains for GspB ( 13 ), the siglec and unique subdomains for SrpA ( 46 ), and a legume lectin-like fold, a β-grasp fold, and two eukaryotic cadherin-like modules for SraP ( 49 ). The GspB, Hsa, SrpA, and SraP SRRP-BRs have all been shown to bind to different types of sialylated ligands ( 13 , 49 , 61 – 71 ), whereas the binding ligand of Fap1 remains to be identified ( 45 ). Lr SRRP-BR did not recognize sialylated glycans but was found to bind to host epithelium or pectin-like components in a pH-dependent manner.…”

Section: Discussionmentioning

confidence: 99%

Structural basis for the role of serine-rich repeat proteins from Lactobacillus reuteri in gut microbe–host interactions

Sequeira

Kavanaugh

MacKenzie

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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SignificanceGut bacteria play a key role in health and disease, but the molecular mechanisms underpinning their interaction with the host remain elusive. The serine-rich repeat proteins (SRRPs) are a family of adhesins identified in many Gram-positive pathogenic bacteria. We previously showed that beneficial bacterial species found in the gut also express SRRPs and that SRRP was required for the ability of Lactobacillus reuteri strain to colonize mice. Here, our structural and biochemical data reveal that L. reuteri SRRP adopts a β-solenoid fold not observed in other structurally characterized SRRPs and functions as an adhesin via a pH-dependent mechanism, providing structural insights into the role of these adhesins in biofilm formation of gut symbionts.

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Section: Discussionmentioning

confidence: 99%

Structural basis for the role of serine-rich repeat proteins from Lactobacillus reuteri in gut microbe–host interactions

Sequeira

Kavanaugh

MacKenzie

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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“… S. gordonii expresses a second adhesin that interacts with sialic acid, Hsa, with this protein having a role in biofilm formation in this species [117]. Streptococcus oralis , a human oral bacterium that can also cause meningitis, binds platelets via recognition of a terminal sialic acid by the adhesin Fap1 [118].…”

Section: Attaching To the Host: Sialic Acid As A Cellular Receptor Fo...mentioning

confidence: 99%

“…The structure of these SLBRs is very similar to mammalian siglecs, but the glycan ligand they interact with quite different [116], suggesting it will be possible to target inhibitors to the bacterial proteins to treat infections. S. gordonii expresses a second adhesin that interacts with sialic acid, Hsa, with this protein having a role in biofilm formation in this species [117]. Streptococcus oralis, a human oral bacterium that can also cause meningitis, binds platelets via recognition of a terminal sialic acid by the adhesin Fap1 [118].…”

Section: Attaching To the Host: Sialic Acid As A Cellular Receptor Fo...mentioning

confidence: 99%

How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach

2022

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N -glycolylneuraminic acid (Neu5Gc), and its precursor N-acetylneuraminic acid (Neu5Ac), commonly referred to as sialic acids, are two of the most common glycans found in mammals. Humans carry a mutation in the enzyme that converts Neu5Ac into Neu5Gc, and as such, expression of Neu5Ac can be thought of as a ‘human specific’ trait. Bacteria can utilize sialic acids as a carbon and energy source and have evolved multiple ways to take up sialic acids. In order to generate free sialic acid, many bacteria produce sialidases that cleave sialic acid residues from complex glycan structures. In addition, sialidases allow escape from innate immune mechanisms, and can synergize with other virulence factors such as toxins. Human-adapted pathogens have evolved a preference for Neu5Ac, with many bacterial adhesins, and major classes of toxin, specifically recognizing Neu5Ac containing glycans as receptors. The preference of human-adapted pathogens for Neu5Ac also occurs during biosynthesis of surface structures such as lipo-oligosaccharide (LOS), lipo-polysaccharide (LPS) and polysaccharide capsules, subverting the human host immune system by mimicking the host. This review aims to provide an update on the advances made in understanding the role of sialic acid in bacteria-host interactions made in the last 5–10 years, and put these findings into context by highlighting key historical discoveries. We provide a particular focus on ‘molecular mimicry’ and incorporation of sialic acid onto the bacterial outer-surface, and the role of sialic acid as a receptor for bacterial adhesins and toxins.

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“…The cell wall-anchored proteins are (i) surface protein antigen of the Streptococcus mutans (AgI/II/PAc/SpaP) family (1200-1700 amino acid residues), which was first identified in cariogenic S. mutans [36][37][38][91][92][93][94][95] ; (ii) fibronectinbinding proteins such as FbpA (550 amino acids) 39 and one of the fibronectin-binding proteins of S. gordonii (CshA; 2508 amino acids) 40 ; (iii) collagen-binding proteins such as proteins of S. gordonii (CbdA; 694 amino acids) 41 ; and (iv) serine-rich repeat adhesins named Hsa (2178 amino acids) [96][97][98] and one of the serine-rich repeat adhesins of S. gordonii (GspB; 3072 amino acids). 42,65 As many excellent reviews are available on these cell wall-anchored proteins, 24,55,56,95 we do not further describe these proteins in this review.…”

Section: Cell Surface Proteins and Enzymes (1): Matrix-binding Proteinsmentioning

confidence: 99%

Oral mitis group streptococci: A silent majority in our oral cavity

Okahashi

Nakata

Kuwata

et al. 2022

Microbiology and Immunology

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Members of the oral mitis group streptococci including Streptococcus oralis, Streptococcus sanguinis, and Streptococcus gordonii are the most abundant inhabitants of human oral cavity and dental plaque, and have been implicated in infectious complications such as bacteremia and infective endocarditis. Oral mitis group streptococci are genetically close to Streptococcus pneumoniae; however, they do not produce cytolysin (pneumolysin), which is a key virulence factor of S. pneumoniae. Similar to S. pneumoniae, oral mitis group streptococci possess several cell surface proteins that bind to the cell surface components of host mammalian cells. S. sanguinis expresses long filamentous pili that bind to the matrix proteins of host cells. The cell wall–anchored nuclease of S. sanguinis contributes to the evasion of the neutrophil extracellular trap by digesting its web‐like extracellular DNA. Oral mitis group streptococci produce glucosyltransferases, which synthesize glucan (glucose polymer) from sucrose of dietary origin. Neuraminidase (NA) is a virulent factor in oral mitis group streptococci. Influenza type A virus (IAV) relies on viral NA activity to release progeny viruses from infected cells and spread the infection, and NA‐producing oral streptococci elevate the risk of IAV infection. Moreover, oral mitis group streptococci produce hydrogen peroxide (H2O2) as a by‐product of sugar metabolism. Although the concentrations of streptococcal H2O2 are low (1–2 mM), they play important roles in bacterial competition in the oral cavity and evasion of phagocytosis by host macrophages and neutrophils. In this review, we intended to describe the diverse pathogenicity of oral mitis group streptococci.

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Contribution of <i>Streptococcus gordonii</i> Hsa Adhesin to Biofilm Formation

Cited by 11 publications

References 38 publications

Structural basis for the role of serine-rich repeat proteins from Lactobacillus reuteri in gut microbe–host interactions

Structural basis for the role of serine-rich repeat proteins from Lactobacillus reuteri in gut microbe–host interactions

How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach

Oral mitis group streptococci: A silent majority in our oral cavity

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