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PubMed2001

How species-specific is the phoretic relationship between the broad mite, Polyphagotarsonemus latus (Acari: Tarsonemidae), and its insect hosts?

Broad mite, Polyphagotarsonemus latus (Acari: Tarsonemidae), is a serious plant pest in tropical and subtropical regions. Phoretic associations between broad mite and two genera of whiteflies (Insecta: Homoptera: Aleyrodidae). namely Bemisia and Trialeurodes, have been reported from different parts of the world. Our purpose was to determine the specificity of the association between the mite and its phoretic hosts. Two host plants, potatoes and cucumbers, were used to study these relationships in the laboratory. Insects frozen for 24 h were used as potential phoretic hosts in all experiments. Attachment levels were monitored by counting the number of mites attached to each insect. All tests were conducted for 4-6 h. as attachment to Bemisia tabaci on potato shoots leveled off after 4 h, increasing only marginally after 8 h. Attachment levels to thrips (the western flower thrips, Frankliniella occidentalis) and to allate aphids (Myzus persicae) was negligible relative to the attachment to B. tabaci. Broad mite also attached to the whiteflies Dialeurodes citri, Aleyrodes singularis and Trialeurodes lauri, the latter being the least attractive species (including B. tabaci). Washing B. tabaci with pentane greatly reduced attachment. Using cucumbers as hosts did not substantially change the general trend, but attachment levels were lower. The phoretic relationship between broad mite and its insect hosts appears to be specific to whiteflies, with some whiteflies having a higher potential as phoretic hosts.

Animals↗

PubMed2006

Attachment and fusion of endoplasmic reticulum with vacuoles containing Legionella pneumophila.

Legionella pneumophila is an intracellular pathogen that replicates in a unique vacuole that avoids endocytic maturation. Previous studies have shown host vesicles attached to the L. pneumophila-containing vacuole (LCV) minutes after uptake. Here we examine the origin and content of these vesicles by electron microscopy (EM). Our data demonstrate that the attached vesicles are derived from endoplasmic reticulum (ER) based the presence of the resident ER proteins glucose-6-phosphatase, protein disulphide isomerase (PDI) and proteins having the ER-retention signal lysine-aspartic acid-glutamic acid-leucine (KDEL). After tethering occurred, ER markers inside of attached vesicles were delivered into the lumen of the LCV, indicating ER fusion. Treatment of cells with brefeldin A did not interfere with the attachment of ER vesicles with the LCV, suggesting that tethering of these vesicles does not require activities mediated by ADP-ribosylation factor (ARF). ER vesicles were not tethered to the LCV in cells producing the Sar1H79G protein, indicating that vesicles produced by the Sar1/CopII system are necessary for vesicle attachment. From these data we conclude that formation of the organelle that supports L. pneumophila replication is a two-stage process that involves remodelling of the LCV by early secretory vesicles produced by the Sar1/CopII system, followed by attachment and fusion of ER.

ADP-Ribosylation Factors↗

PubMed1989

Neutralization of small RNA viruses by antibodies and antiviral agents.

The 3-dimensional structures of a number of small animal RNA viruses are now known to near-atomic resolution. All these viruses have similar structures and have, in all probability, diverged from a common ancestral virus able to infect a variety of organisms. The structures have elucidated the site of attachment to host cell receptors and the mode of protection of this site against host immune pressure. An internal hydrophobic pocket in rhinoviruses is the site for binding of antiviral drugs that inhibit uncoating and can inhibit attachment in some viruses. The pocket is probably a functional necessity, and thus is a suitable target for well-designed antiviral agents in many viruses.

Antibodies, Viral↗

PubMed1993

Molecular mechanism of host specificity in legume-rhizobium symbiosis.

Rhizobium - legume symbiosis is a highly specific interaction between the two partners. Host specificity is evident at early stages of infection and results from multiple interactions involving signalling among bacteria and host plants. Host specific plant signals (flavanoids) convert the NodD protein to an active form and its binding with nod box initiates the transcription of inducible nod operons. Common nod genes (nodABC) code for an extracellular mitogenic Nod factor which is required for nodule organogenesis. Host specific genes (hsn) modify the Nod factor to induce root hair deformation on specific hosts. The structure of Nod factor controls host range distinction between species and biovars of rhizobia. Interactions of lectins and Exopolysaccharide/Lipopolysaccharide result in host specific attachment of Rhizobium and its subsequent invasion. Change in Expopolysaccharide structure by the transfer of hsn genes enables the Rhizobium to bind with heterologous host lectins. Conversely, changes in root lectins via gene manipulation enables the heterologous rhizobia to bind and initiate nodulation on heterologous hosts. Finally, host specific signals are required to initiate nitrogen fixation in nodules that are formed.

Journal Article↗

PubMed1992

Microbial interaction with animal cell surface carbohydrates.

Microbes have selected primarily carbohydrates for attachment to host animal cells. Recent studies have revealed essential characteristics in the recognition of receptor carbohydrates. Of importance is the property of recognizing also sequences placed inside an oligosaccharide chain, which differs from most animal antibodies. This is the basis for series of isoreceptors with the minimum receptor sequence in common but with separate neighbouring groups. There are families of microbial ligands that show different preferences for members within one series of isoreceptors, indicating only slight differences in the complementary binding sites of the proteins. Such differences may explain shifts in the selectivity of separate host tissues for infection. A second characteristic is the low affinity interaction often found where simple receptor-containing saccharides are unable to inhibit attachment. Technical possibilities are rapidly developing for the design of synthetic receptor analogues to be used in the therapy of clinical infections. This is urgently needed in cases where no rational therapy exists today.

Adhesins, Escherichia coli↗

PubMed2002

Structure of the immunodominant surface antigen from the Toxoplasma gondii SRS superfamily.

Toxoplasma gondii is a persistent protozoan parasite capable of infecting almost any warm-blooded vertebrate. The surface of Toxoplasma is coated with a family of developmentally regulated glycosylphosphatidylinositol (GPI)-linked proteins (SRSs), of which SAG1 is the prototypic member. SRS proteins mediate attachment to host cells and interface with the host immune response to regulate the virulence of the parasite. The 1.7 A structure of the immunodominant SAG1 antigen reveals a homodimeric configuration in which the dimeric interface is mediated by an extended beta-sheet that forms a deep groove lined with positively charged amino acids. This basic groove seems to be conserved among SRS proteins and potentially serves as a sulfated proteoglycan-binding site on target cell surfaces, thus rationalizing the promiscuous attachment properties of Toxoplasma to a broad range of host cell types.

Amino Acid Sequence↗

PubMed1988

Attachment of Mycoplasma bovoculi to bovine conjunctival epithelium and lung fibroblasts.

A specialized tip structure in some mycoplasmas facilitates their attachment to host cells. Mycoplasma bovoculi strains FS8-7 and M165/69 did not have specialized membrane structure and did not exhibit capsule when stained with ruthenium red and examined by use of transmission electron microscopy. The organisms attached in vitro to bovine lung fibroblasts, with no apparent specialized structure. Attachment to conjunctival epithelium in vivo was observed (after death) in a calf infected with M bovoculi. Close association between M bovoculi and the host cells was noticed. Mycoplasmal cells pretreated with hyperimmune rabbit serum and labeled with protein A-gold complex had gold particles randomly distributed around the membrane. Gold-labeled monoclonal antibodies, M25.5 and M7.3, which were directed against 2 surface antigens of M bovoculi, also were distributed randomly on the mycoplasmal surface as seen in results of double-labeling experiments.

Animals↗

PubMed1999

Adherence of pathogenic mycoplasmas to host cells.

The significant genome compaction in mycoplasmas was made possible by adoption of a parasitic lifestyle. During their evolution and adaptation to a parasitic mode of life the mycoplasmas have developed various genetic systems enabling their attachment to host tissues as well as a highly plastic set of variable surface proteins. The generation of a versatile surface coat through high-frequency phase and size variation provides the organism with a useful tool for immune system avoidance, allowing the mycoplasmas to escape antibody attack, explaining why these minute organisms are such successful parasites.

Adhesins, Bacterial↗

PubMed2026

Crown ethers as artificial decoys: A supramolecular strategy to block SARS-CoV-2 entry via host-guest interactions.

Coronavirus disease (COVID-19) remains a major global health challenge, highlighting the need for antiviral strategies that act at the earliest stages of infection. Given that viral entry and spike-receptor interaction are critical steps in the coronavirus life cycle, targeting these processes represents a powerful strategy to block infection at its earliest stage. Inspired by the glycan-recognition and extracellular viral-trapping functions of pulmonary surfactant collectins (SP-A and SP-D), this work integrates supramolecular chemistry, pulmonary surfactant biology, and antiviral research to establish a biomimetic supramolecular molecular-decoy framework based on crown ethers, cyclodextrins, and related macrocyclic architectures. Through host-guest molecular recognition, these macrocyclic scaffolds can be engineered to mimic sialylated host receptors and multivalent glycan motifs, enabling competitive binding to viral spike proteins, virion capture, and sequestration away from epithelial surfaces. By redirecting viruses toward artificial host-mimetic structures, supramolecular decoys could intercept SARS-CoV-2 and other enveloped respiratory viruses before host-cell attachment, membrane fusion, or genome release. Acting upstream of intracellular replication, this strategy may prevent initiation of the viral replication cycle and subsequent hijacking of the host protein synthesis machinery, while potentially minimizing interference with host metabolic pathways and reducing the likelihood of resistance development. Furthermore, it can be translated into inhalation nanoformulations for pulmonary delivery and localized formulations targeting the upper respiratory tract. Overall, by integrating the biological principles of pulmonary surfactant immunity with supramolecular host-guest chemistry, this work provides a conceptual foundation for biomimetic molecular-decoy antivirals and highlights a promising direction for next-generation broad-spectrum antiviral design against emerging respiratory viruses.

Antiviral Agents↗

PubMed2002

Prevention of respiratory infections by povidone-iodine gargle.

Bacterial attachment to host cells is the initial step in the pathogenesis of infection. Our studies and those of others also showed that there is a significant correlation between the attachment of bacteria to human pharyngeal epithelial cells and the occurrence of respiratory tract infections. We identified the receptor on human pharyngeal epithelial cells which mediate binding of Moraxella catarrhalis and Haemophilus influenzae. In an attempt to prevent occurrence of infections, the effects of povidone-iodine gargling on the incidence of respiratory infections were investigated. The subjects included a total of 23 adult patients, both males and females, with chronic respiratory diseases showing repeated infections. Patients were asked to gargle more than 4 times/day with povidone-iodine gargle over extended periods of time, i.e. from several months up to over 2 years. The incidence of episodes of acute exacerbation of chronic respiratory infections decreased significantly when compared with that before use of povidone-iodine gargle. Episodes of infections with Pseudomonas aeruginosa, Staphylococcus aureus (including MRSA) and H. influenzae were reduced by about 50%. Results of this study suggest that povidone-iodine gargle is effective in providing a significant reduction in the incidence of acute exacerbations of chronic respiratory disease. We assume that the colonized bacteria were destroyed and thus infection could not occur. Therefore, povidone-iodine gargle may be used in these patients as a preventive therapy. Further studies are needed to find out the mechanism of action of this drug for the prevention of respiratory tract infections.

Adult↗

PubMed2000

Observations on a lesser-known monogenean, Udonella myliobati, from a copepod parasite, Lepeophtheirus natalensis, parasitizing the spotted ragged-tooth shark, Carcharias taurus, from South African waters.

The phylogeny of the genus Udonella has been disputed for quite some time, but recent phylogenetic analysis of molecular data confirms that the genus is a monopisthocotylean monogenean. Specimens of Udonella myliobati parasitizing the copepod Lepeophtheirus natalensis, an ectoparasite of the spotted ragged-tooth shark, (Carcharias taurus), were collected and studied. A total of 771 monogenean specimens were recovered from 54 infected copepods examined, with a mean intensity of 14,3 worms per copepod. Most of the monogeneans were found attached to the dorsal surface of the lateral and frontal marginal membranes of the copepod carapace. Eggs, with filaments and adhesive discs, were found ventrally on the host, mainly attached to the maxillae and maxillipeds, in clusters of 12-14. Observations on the morphology, distribution and behaviour of this monogenean are presented with the aid of light and scanning electron microscopy.

Animals↗

PubMed1951

The first two steps of the invasion of host cells by bacterial viruses. II.

At 37 degrees C., the attachment of T1 virus to its host cell in solution containing 10(-3)M CaCl(2) or 10(-2)M NaCl is extremely rapid (in the neighborhood of 100 per cent collision efficiency) and irreversible. At 1 degrees C., the attachment rate is almost equally rapid but largely reversible. If a suboptimal concentration of the necessary ions is employed when T2 virus attaches to host cells, the resulting binding is largely reversible, even at 37 degrees C. Reversible T2 attachment to host cells leaves the cell undamaged and capable of normal reproduction. Irreversible attachment results in death of the cell. Zn(++) exercises a specific inhibitory action on the invasion of E. coli B by T1 virus. The virus can still attach to the host cell at a rate closely approximating the maximum value, but the reaction remains reversible and the cell is protected against permanent damage. The protective action of the Zn against T1 invasion is exerted through an action on the cell, rather than on the virus. Studies of the uptake of radioactive Zn(65) show that cells become completely immune to T1 invasion when, on the average, 4 x 10(7) atoms of Zn have been taken up by each cell. Cells killed by ultraviolet irradiation still bind T1 at the maximum rate, but the reaction is reversible even when taking place at 37 degrees C., in optimum salt concentration. The tryptophane-deficient mutant of T4 bacteriophage requires its specific cofactor for the initial step of attachment to the host cell. These experiments support the picture previously developed that virus invasion of host cells consists in an initial, reversible attachment whose properties are those to be expected from the operation of electrostatic binding forces. The step is followed by an enzymatic transformation which is irreversible, strongly temperature-dependent, and in the case of T1 virus, susceptible to inactivation by ultraviolet radiation. The resistance of mutant cells to specific bacteriophages is of two types, depending on whether the first or second of these steps is blocked.

Escherichia coli↗

PubMed2004

Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation.

Diarrhea-causing Escherichia coli strains are responsible for numerous cases of gastrointestinal disease and constitute a serious health problem throughout the world. The ability to recognize and attach to host intestinal surfaces is an essential step in the pathogenesis of such strains. AIDA is a potent bacterial adhesin associated with some diarrheagenic E. coli strains. AIDA mediates bacterial attachment to a broad variety of human and other mammalian cells. It is a surface-displayed autotransporter protein and belongs to the selected group of bacterial glycoproteins; only the glycosylated form binds to mammalian cells. Here, we show that AIDA possesses self-association characteristics and can mediate autoaggregation of E. coli cells. We demonstrate that intercellular AIDA-AIDA interaction is responsible for bacterial autoaggregation. Interestingly, AIDA-expressing cells can interact with antigen 43 (Ag43)-expressing cells, which is indicative of an intercellular AIDA-Ag43 interaction. Additionally, AIDA expression dramatically enhances biofilm formation by E. coli on abiotic surfaces in flow chambers.

Adhesins, Escherichia coli↗

PubMed1967

Primary virus-cell interactions in the immunofluorescence assay of Venezuelan equine encephalomyelitis virus.

The conditions under which Venezuelan equine encephalomyelitis (VEE) virus attached to host cells markedly influenced the assay of virus by the fluorescent cell-counting technique. When virus inoculum was centrifuged onto McCoy cell monolayers, approximately 97% of virus was attached to cells within 10 min, in contrast to 34% after stationary incubation at 35 C for 2 hr. Maximal binding of virus occurred only in the presence of 0.1 to 0.15 m NaCl. This salt requirement, added to evidence of (p)H dependence and temperature independence of VEE virus attachment to cells, indicated that the initial union involved electrostatic forces. Virus penetration, measured by the insensitivity of virus-cell complexes to viral antiserum, was complete in 30 min at 35 C. The process was temperature-dependent and un-affected by the ionic content of medium. For assay of VEE virus by the fluorescent cell-counting technique, infected cells may be enumerated as early as 12 hr after infection of cell monolayers. The relationship between virus concentration and cell-infecting units was linear; the distribution of fluorescent cells was random. The virus assay was equivalent in sensitivity but more precise and rapid than that of intracerebral inoculation of mice.

Animals↗

PubMed1979

Scanning electron-microscopic study of the uptake of Leishmania parasites by macrophages.

The interaction of promastigotes of the protozoan parasite Leishmania tropica with mouse peritoneal macrophages in vitro was studied by scanning electron microscopy. Motile promastigotes attached to host cells by their flagellar tips to which the macrophages responded by producing rather closely fitting lamellar sheaths and progressively enveloping first the flagellum and then the body of the parasite. Lamellar advance during engulfment was rapid in the first 10 min but much slower later on. Fully engulfed parasites could be seen after 1 h but most parasites associated with host cells remained extracellular even after 4 h. On the other hand, parasites immobilized by fixation adhered by either their flagellar or somatic ends. Engulfment proceeded at a steady rate, and by 4 h most of them were completely engulfed. Both the attachment and engulfment stages of parasite uptake were inhibited by low temperature, cytochalasin D and mild fixation of macrophages. The rheological features of the host cells' response to parasite adherence indicate that invasion by parasites is through phagocytosis rather than penetration.

Animals↗

PubMed1999

Enterohemorrhagic Escherichia coli O157:H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated.

Intimate attachment to the host cell leading to the formation of attaching and effacing (A/E) lesions is an essential feature of enterohemorrhagic Escherichia coli (EHEC) O157:H7 pathogenesis. In a related pathogen, enteropathogenic E. coli (EPEC), this activity is dependent upon translocation of the intimin receptor, Tir, which becomes tyrosine phosphorylated within the host cell membrane. In contrast, the accumulation of tyrosine-phosphorylated proteins beneath adherent EHEC bacteria does not occur, leading to questions about whether EHEC uses a Tir-based mechanism for adherence and A/E lesion formation. In this report, we demonstrate that EHEC produces a functional Tir that is inserted into host cell membranes, where it serves as an intimin receptor. However, unlike in EPEC, in EHEC Tir is not tyrosine phosphorylated yet plays a key role in both bacterial adherence to epithelial cells and pedestal formation. EHEC, but not EPEC, was unable to synthesize Tir in Luria-Bertani medium but was able to secrete Tir into M9 medium, suggesting that Tir synthesis and secretion may be regulated differently in these two pathogens. EHEC Tir and EPEC Tir both bind intimin and focus cytoskeletal rearrangements, indicating that tyrosine phosphorylation is not needed for pedestal formation. EHEC and EPEC intimins are functionally interchangeable, but EHEC Tir shows a much greater affinity for EHEC intimin than for EPEC intimin. These findings highlight some of the differences and similarities between EHEC and EPEC virulence mechanisms, which can be exploited to further define the molecular basis of pedestal formation.

Adhesins, Bacterial↗

PubMed2003

A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen.

Gram-positive pathogens such as staphylococci contain multiple cell wall-anchored proteins that serve as an interface between the microbe and its environment. Some of these proteins act as adhesins and mediate bacterial attachment to host tissues. SdrG is a cell wall-anchored adhesin from Staphylococcus epidermidis that binds to the Bbeta chain of human fibrinogen (Fg) and is necessary and sufficient for bacterial attachment to Fg-coated biomaterials. Here, we present the crystal structures of the ligand binding region of SdrG as an apoprotein and in complex with a synthetic peptide analogous to its binding site in Fg. Analysis of the crystal structures, along with mutational studies of both the protein and of the peptide, reveals that SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism. We propose that this mechanism represents a general mode of ligand binding for structurally related cell wall-anchored proteins of gram-positive bacteria.

Adhesins, Bacterial↗

PubMed2006

The mechanical properties of E. coli type 1 pili measured by atomic force microscopy techniques.

The first step in the encounter between a host and a pathogen is attachment to the host epithelium. For uropathogenic Escherichia coli, these interactions are mediated by type 1 and P adhesive pili, which are long (approximately 1 microm) rods composed of more than 1000 protein subunits arranged in a helical structure. Here we used single-molecule atomic force microscopy to study the mechanical properties of type 1 pili. We found that type 1 pili readily extend under an applied force and that this extensibility is the result of unwinding the pilus rod's helical quaternary structure. The forced unraveling is also reversible, with helical rewinding taking place under considerable forces (approximately 60 pN). These data are similar to those obtained on P pili using optical tweezers, indicating that these are conserved properties of uropathogenic E. coli pili. We also show that our data can readily be reproduced using Monte Carlo simulation techniques based on a two-state kinetic model. This model provides a simple way to extrapolate the mechanical behavior of pili under a wide range of forces. We propose that type 1 pilus unraveling is an essential mechanism for absorbing physiological shear forces encountered during urinary tract infections and probably essential for adhesion and colonization of the bladder epithelium.

Biomechanical Phenomena↗