M1 protein and protein H: IgGFc- and albumin-binding streptococcal surface proteins encoded by adjacent genes

Åkesson, Per; Schmidt, Karl‐Hermann; Cooney, Jakki C.; Björck, Lars

doi:10.1042/bj3000877

Cited by 164 publications

(271 citation statements)

References 67 publications

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“…with several characterized interactions with plasma proteins. 13,14,16 Hence we expected large differences in the protein abundance levels of known interacting plasma proteins, which we could confirm in the data (Fig. 4, red bars, left axis).…”

Section: Differences In Plasma Protein Interaction Profiles Between Asupporting

confidence: 76%

A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network

et al. 2014

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Link to publication Citation for published version (APA): Sjöholm, K., Karlsson, C., Linder, A., & Malmström, J. (2014). A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network. Molecular BioSystems, 10(7), 1698-1708. DOI: 10.1039/c3mb70555bGeneral rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights.• Users may download and print one copy of any publication from the public portal for the purpose of private study or research.• You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal

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Section: Differences In Plasma Protein Interaction Profiles Between Asupporting

confidence: 76%

A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network

et al. 2014

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“…Cloning and expression of rM1 has been described [38]. The emm3 gene and a fragment encoding the N-terminal 58 residues of the M3 protein (rM3N 58 ) were amplified by PCR and cloned into the expression plasmids pET25b (Novagen) for rM3 and pGEX-5x-3 for rM3N 58 .…”

Section: Recombinant M Proteins and Solid-phase Radioimmunoassaymentioning

confidence: 99%

Critical role for complement receptor 3 (CD11b/CD18), but not for Fc receptors, in killing of Streptococcus pyogenes by neutrophils in human immune serum

et al. 2005

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During phagocytosis, surface receptors on neutrophils interact with pathogens opsonized with complement factor C3b/iC3b and in some cases with antibodies. In human immune sera antibodies directed against surface‐bound M proteins mediated killing of Streptococcus pyogenes by neutrophils. Surprisingly, blocking of the Fc receptors had little effect on the killing. In contrast, inhibition of C3b/iC3b generation, or blocking of the major neutrophil iC3b receptor CD11b/CD18, enabled S. pyogenes to grow efficiently in immune sera. Inhibition of CD11b/CD18, but not of CD32, the major neutrophil signaling Fc receptor, prevented Streptococcus‐induced NADPH oxidase‐dependent respiratory burst, and blocking of C3b/iC3b formation inhibited Streptococcus‐induced activation of Cdc42, a small GTPase critically involved in transmitting pro‐inflammatory signals to the cytoskeleton. Consequently, ligation of CD11b/CD18 by bacteria‐bound iC3b is necessary for inducing a neutrophil response leading to elimination of S. pyogenes in immune human serum.

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“…Some strains showed high binding also to BSAcoated beads. Human albumin is recognized by M proteins and protein H of S. pyogenes (29), and it is possible that cross-reactions to BSA may occur. Still, all strains bound more efficiently to gp340-coated than to BSA-coated beads.…”

Section: Common Binding Of Clinical S Pyogenes Isolates To Gp340-mentioning

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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M1 protein and protein H: IgGFc- and albumin-binding streptococcal surface proteins encoded by adjacent genes

Cited by 164 publications

References 67 publications

A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network

A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network

Critical role for complement receptor 3 (CD11b/CD18), but not for Fc receptors, in killing of Streptococcus pyogenes by neutrophils in human immune serum

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

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