Receptins: a novel term for an expanding spectrum of natural and engineered microbial proteins with binding properties for mammalian proteins

Kronvall, Göran; Jönsson, Klas

doi:10.1002/(sici)1099-1352(199901/02)12:1<38::aid-jmr378>3.0.co;2-q

Cited by 33 publications

(21 citation statements)

References 134 publications

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“…The proposed anchorage protein could be either mycoplasma or host derived. Many pathogenic bacteria have evolved surface molecules or receptors capable of binding host proteins that enhance adherence, colonization, and invasion of host epithelial surfaces (15,26,33). For instance, binding to fibronectin by pathogenic bacteria can enhance initial colonization of the epithelial cells on mucosal surfaces (12,22,25,30) and trigger cellular invasion (33).…”

Section: Vol 72 2004mentioning

confidence: 99%

Proteolytic Processing of theMycoplasma hyopneumoniaeCilium Adhesin

et al. 2004

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Mycoplasma hyopneumoniae is an economically significant swine pathogen that colonizes the respiratory ciliated epithelial cells. Cilium adherence is mediated by P97, a surface protein containing a repeating element (R1) that is responsible for binding. Here, we show that the cilium adhesin is proteolytically processed on the surface. Proteomic analysis of strain J proteins identified cleavage products of 22, 28, 66, and 94 kDa. N-terminal sequencing showed that the 66-and 94-kDa proteins possessed identical N termini and that the 66-kDa variant was generated by cleavage of the 28-kDa product from the C terminus. The 22-kDa product represented the N-terminal 195 amino acids of the cilium adhesin preprotein, confirming that the hydrophobic leader signal sequence is not cleaved during translocation across the membrane. Comparative studies of M. hyopneumoniae strain 232 showed that the major cleavage products of the cilium adhesin are similar, although P22 and P28 appear to be processed further in strain 232. Immunoblotting studies using antisera raised against peptide sequences within P22 and P66/P94 indicate that processing is complex, with cleavage occurring at different frequencies within multiple sites, and is strain specific. Immunogold electron microscopy showed that fragments containing the cilium-binding site remained associated with the cell surface whereas cleavage products not containing the R1 element were located elsewhere. Not all secreted proteins undergo multiple cleavage, however, as evidenced by the analysis of the P102 gene product. The ability of M. hyopneumoniae to selectively cleave its secreted proteins provides this pathogen with a remarkable capacity to alter its surface architecture.Mycoplasma hyopneumoniae, the etiological agent of enzootic pneumonia, significantly impacts swine production (28). During colonization, M. hyopneumoniae forms an intricate association with the ciliated epithelial lining of the porcine respiratory tract, leading to chronic respiratory disease. Colonization disrupts the normal function of the mucociliary escalator through ciliostasis, loss of cilia, epithelial cell death, and acute inflammation. This results in a purulent exudate (composed primarily of neutrophils and mononuclear cells) in the airways (17). Disease resolution occurs only after a prolonged period (if at all). M. hyopneumoniae colonization also predisposes the host to more-severe infections from secondary pathogens (2). For example, it is now clear that colonization by M. hyopneumoniae leads to more-severe and longer-lasting disease with the porcine respiratory and reproductive syndrome virus (34). Thus, the impact of M. hyopneumoniae on swine production has not been fully realized.It is known that the initial event in colonization by M. hyopneumoniae is binding to swine respiratory cilia (19,32). In the absence of binding activity, colonization does not occur (38). Identification of the molecules involved in cilium binding occurred only after the discovery of adherence-blocking monoclonal antibod...

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Section: Vol 72 2004mentioning

confidence: 99%

Proteolytic Processing of theMycoplasma hyopneumoniaeCilium Adhesin

et al. 2004

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“…S. aureus produces a number of cell surface-localized binding proteins, including fibronectin binding proteins (FnBPs) (15,44), a collagen binding protein (38), fibrinogen binding proteins (FgBP) (4,30), a vitronectin binding protein (39) and an elastin binding protein (37). A recent suggestion is to term these proteins receptins (28). Receptins are proposed to contribute to the success of colonization and persistence at various sites of the host.…”

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confidence: 99%

Extracellular Adherence Protein from Staphylococcus aureus Enhances Internalization into Eukaryotic Cells

Haggar¹,

Hussain

Lönnies³

et al. 2003

Infect Immun

105

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In this study we have shown that Eap (extracellular adherence protein) plays a role in the internalization process of Staphylococcus aureus into eukaryotic cells. Eap is a protein that is mostly extracellularly and to a lesser extent is bound to the bacterial surface as a result of rebinding. Eap is able to bind to several plasma proteins, such as fibronectin, fibrinogen, and prothrombin. It has the capacity to form oligomers and is able to agglutinate S. aureus. A mutant strain, Newman mAH12 (eap:: Ery r ), with a deficient eap gene was used in the present study. We have demonstrated that (i) strain Newman mAH12 could adhere to and become internalized to a higher extent by eukaryotic cells than the isogenic mutant, (ii) strain Newman mAH12 complemented with the eap gene displayed restoration of the internalization level, (iii) externally added Eap enhanced the internalization of laboratory and clinical S. aureus strains as well as of S. carnosus (a coagulasenegative species devoid of proteins important for internalization), and (iv) antibodies against Eap were able to block the internalization process in strain Newman mAH12 and clinical isolates. Eap, with its broad binding capacity and its surface localization, thus seems to contribute to the internalization of S. aureus into eukaryotic cells. We therefore propose a novel internalization pathway for S. aureus in which Eap plays an enhancing role.

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“…Adherence of bacteria to host cell receptors (composed of lipids, proteins, glycolipids or glycoproteins) triggers cellular changes that include signal transduction cascades, leading to infiltration of inflammatory cells (neutrophils and monocytes) and eventually to persistence of the microorganism (95). A receptin, however, does not necessarily induce a secondary effect (41). It has become evident over the past decade that many microorganisms express cell surface receptins mediating microbial adherence to host tissues.…”

Section: Rationale For Bacterial Adhesins and Receptinsmentioning

confidence: 99%

“…and that some of these interactions are of high affinity: they could thus play an important role in the infectious process. Microbial proteins with binding properties for mammalian proteins are now called receptins (41), and this term is used throughout this review. This term excludes the first step of adherence to the mammalian cell surface required for a microorganism to establish itself in a host; rather, it refers to the later stages that permit the persistence of a long-lasting infectious process through binding to soluble host cell proteins.…”

Section: Introductionmentioning

confidence: 99%

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

Dubreuil¹,

Giudice²,

Rappuoli³

2002

Microbiol Mol Biol Rev

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Helicobacter pylori, a gram-negative spiral-shaped bacterium, specifically colonizes the stomachs of humans. Once established in this harsh ecological niche, it remains there virtually for the entire life of the host. To date, numerous virulence factors responsible for gastric colonization, survival, and tissue damage have been described for this bacterium. Nevertheless, a critical feature of H. pylori is its ability to establish a long-lasting infection. In fact, although good humoral (against many bacterial proteins) and cellular responses are observed, most infected persons are unable to eradicate the infection. A large body of evidence has shown that the interaction between H. pylori and the host is very complex. In addition to the effect of virulence factors on colonization and persistence, binding of specialized bacterial proteins, known as receptins, to certain host molecules (ligands) could explain the success of H. pylori as a chronically persisting pathogen. Some of the reported interactions are of high affinity, as revealed by their calculated dissociation constant. This review examines the binding of host proteins (serum and extracellular matrix proteins) to H. pylori and considers the significance of these interactions in the infectious process. A more thorough understanding of the kinetics of these receptin interactions could provide a new approach to preventing deeper tissue invasion in H. pylori infections and could represent an alternative to antibiotic treatment

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Receptins: a novel term for an expanding spectrum of natural and engineered microbial proteins with binding properties for mammalian proteins

Cited by 33 publications

References 134 publications

Proteolytic Processing of theMycoplasma hyopneumoniaeCilium Adhesin

Proteolytic Processing of theMycoplasma hyopneumoniaeCilium Adhesin

Extracellular Adherence Protein from Staphylococcus aureus Enhances Internalization into Eukaryotic Cells

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

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