<b>Structure, function and immunogenicity of streptococcal antigen I/II polypeptides</b>

Jenkinson, Howard F.; Demuth, Donald R.

doi:10.1046/j.1365-2958.1997.2021577.x

Cited by 225 publications

(227 citation statements)

References 29 publications

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“…The sialic acid residues on gp340 mediate binding of some bacteria and viruses (18,43,44), and specific sialic acid adhesins, Hsa and GspB, have been identified in S. gordonii (45). Also, the AgI/II adhesins of viridans (oral) streptococci mediate binding to gp340 (17,18,46,47). The peptide core of SRCR domains of gp340, and especially the amino acid sequence VEVLXXXXW, has been identified to be important in these interactions (19).…”

Section: Discussionmentioning

confidence: 99%

Leucine-rich Repeats of Bacterial Surface Proteins Serve as Common Pattern Recognition Motifs of Human Scavenger Receptor gp340

Loimaranta¹,

Hytönen

Pulliainen

et al. 2009

Journal of Biological Chemistry

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Scavenger receptors are innate immune molecules recognizing and inducing the clearance of non-host as well as modified host molecules. To recognize a wide pattern of invading microbes, many scavenger receptors bind to common pathogenassociated molecular patterns, such as lipopolysaccharides and lipoteichoic acids. Similarly, the gp340/DMBT1 protein, a member of the human scavenger receptor cysteine-rich protein family, displays a wide ligand repertoire. The peptide motif VEVLXXXXW derived from its scavenger receptor cysteine-rich domains is involved in some of these interactions, but most of the recognition mechanisms are unknown. In this study, we used mass spectrometry sequencing, gene inactivation, and recombinant proteins to identify Streptococcus pyogenes protein Human gp340, also known as DMBT1 (deleted in malignant brain tumors 1), belongs to the innate immune protein family of scavenger receptor cysteine-rich (SRCR) 2 proteins, all of which contain one or more evolutionarily conserved SRCR domain linked to other conserved protein domains (1, 2). Many of these proteins serve as pattern recognition receptors for innate immunity. gp340 is expressed by epithelial cells and cells of the immune system, and its expression is up-regulated after inflammatory stimuli (3, 4). It inhibits bacterial invasion to epithelial cells and the secretion of proinflammatory cytokines (5-7).Thus, it appears to be an important mediator of host immune responses to various microbes and was recently linked to Crohn disease, a human inflammatory bowel disease (8). gp340 is also found in human secretions like tears and saliva, and the salivary form has long been known as salivary agglutinin, which is an important molecule in oral biofilm formation and is suggested to have a role in dental caries development (9 -12). The mechanisms of gp340 action in these different biological contexts are not known. Common to all scavenger receptors, the ligand repertoire of gp340 is wide; it binds many different types of bacteria as well as viruses (10,13,14). The wide ligand recognition pattern of scavenger receptors is thought to be based on the recognition of common microbial structures, such as lipopolysaccharides and lipoteichoic acids, but in the case of gp340, specific bacterial surface proteins are reported to be involved in the interactions characterized (15-18). Because the importance of gp340/salivary agglutinin in the oral environment has been evident for a long time, most of our knowledge of gp340-microbial interactions is from studies with oral bacteria. For example, viridans streptococci, such as Streptococcus mutans and Streptococcus gordonii, interact with saliva gp340 via their surface proteins AgI/II and the sialic acid-binding Hsa or GspB adhesin. In these interactions, gp340 shows a peculiar fluid phase versus surfaceadsorbed behavior, as evidenced by AgI/II polypeptides primarily mediating aggregation of bacteria by fluid phase gp340, whereas the Hsa adhesin primarily mediates adhesion of S. gordonii to surface-bound gp340 (18)...

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Section: Discussionmentioning

confidence: 99%

Leucine-rich Repeats of Bacterial Surface Proteins Serve as Common Pattern Recognition Motifs of Human Scavenger Receptor gp340

Loimaranta¹,

Hytönen

Pulliainen

et al. 2009

Journal of Biological Chemistry

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“…The ability of S. mutans to form biofilms is dependent on the secretion of extracellular GTFs and FTFs (Banas & Vickerman, 2003) and the cell surface-localized-protein adhesin P1 (antigen I/II, PAc) (Jenkinson & Demuth, 1997). The DyidC2 mutant is impaired in sucrosedependent biofilm formation and shows decreased clumping in defined media containing 0.5 % sucrose compared with wild-type NG8 (Fig.…”

Section: Effects Of Yidc1 and Yidc2 On Secreted Proteinsmentioning

confidence: 99%

YidC1 and YidC2 are functionally distinct proteins involved in protein secretion, biofilm formation and cariogenicity of Streptococcus mutans

et al. 2012

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“…Many adhesins belong to the superfamily of cell wall-anchored polypeptides with the C-terminal consensus motif LPxTz, including type I fimbriae of Actinomyces spp. [17], the streptococcal antigen I/II [18], and serine-rich repeat protein (SRRP) families [19][20][21][22][23]. In SRRP adhesins, which have been identified in both streptococci and lactobacilli [23], glycoconjugates play an important role for adhesion [21,24].…”

Section: Introductionmentioning

confidence: 99%

Osteopontin adsorption to Gram-positive cells reduces adhesion forces and attachment to surfaces under flow

Kristensen

Zeng

Neu

et al. 2017

Journal of Oral Microbiology

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The bovine milk protein osteopontin (OPN) may be an efficient means to prevent bacterial adhesion to dental tissues and control biofilm formation. This study sought to determine to what extent OPN impacts adhesion forces and surface attachment of different bacterial strains involved in dental caries or medical device-related infections. It further investigated if OPN's effect on adhesion is caused by blocking the accessibility of glycoconjugates on bacterial surfaces. Bacterial adhesion was determined in a shear-controlled flow cell system in the presence of different concentrations of OPN, and interaction forces of single bacteria were quantified using single-cell force spectroscopy before and after OPN exposure. Moreover, the study investigated OPN's effect on the accessibility of cell surface glycoconjugates through fluorescence lectin-binding analysis. OPN strongly affected bacterial adhesion in a dose-dependent manner for all investigated species (Actinomyces naeslundii, Actinomyces viscosus, Lactobacillus paracasei subsp. paracasei, Staphylococcus epidermidis, Streptococcus mitis, and Streptococcus oralis). Likewise, adhesion forces decreased after OPN treatment. No effect of OPN on the lectin-accessibility to glycoconjugates was found. OPN reduces the adhesion and adhesion force/energy of a variety of bacteria and has a potential therapeutic use for biofilm control. OPN acts upon bacterial adhesion without blocking cell surface glycoconjugates. ARTICLE HISTORY

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Structure, function and immunogenicity of streptococcal antigen I/II polypeptides

Cited by 225 publications

References 29 publications

Leucine-rich Repeats of Bacterial Surface Proteins Serve as Common Pattern Recognition Motifs of Human Scavenger Receptor gp340

Leucine-rich Repeats of Bacterial Surface Proteins Serve as Common Pattern Recognition Motifs of Human Scavenger Receptor gp340

YidC1 and YidC2 are functionally distinct proteins involved in protein secretion, biofilm formation and cariogenicity of Streptococcus mutans

Osteopontin adsorption to Gram-positive cells reduces adhesion forces and attachment to surfaces under flow

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