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PubMed2006

Potential risk of pathogen transmission by acaricide-poisoned ticks.

Many aspects of tick poisoning with acaricides have yet to be elucidated. One of them is the influence of acaricide poisoning on tick infectivity to their hosts. To clarify this problem, we should know how tick poisoning develops after acaricide application. Data obtained during more than three decades of work with ticks of various species and with acaricides of different groups are presented in the paper. The first important phenomenon found was the gradual and progressive development of toxic symptoms after acaricide application, with death of the treated ticks delayed for days or even weeks ('slow-death syndrome'). The development of symptoms was much faster after the application of fenthion, an organophosphorous acaricide, when compared to DDT, a chlorinated hydrocarbon. The larger the adult ticks of a particular species, the more refractory they were to acaricide action. The duration of the development of toxic symptoms directly correlates with the degree of species-specific refractoriness. A special index T(LD(50)) (T(LC(50)) was introduced for comparing the duration of the poisoning development between different tick species, populations etc. The index determines the time when the final mortality is reached after using the LD(50) of a particular acaricide. Another index , T(LD(90)), was used for practical purposes. The values of these indices decreased with increasing age of tick populations. The prolonged duration of poisoning was also observed in nymphal ticks of species with a prolonged life-span and the ability to over-winter (Ixodes, Haemaphysalis) but not in ticks characterized by a short life-span (Dermacentor). During the entire period of poisoning, from acaricide application until tick death, the individual tick passes through six stages defined by its locomotor capabilities. The stages are the same for nymphs and adults of both hard and soft ticks after treatment with various acaricides. When ticks are at the initial stages of poisoning (1st to 3rd stage for DDT or 1st to 2nd for fenthion), they can attach to hosts and imbibe blood. The average body weight of such ticks after repletion corresponded to that of control ticks. Engorged nymphal ticks normally molted to adults, engorged females normally oviposited, and their progeny did not differ from the progeny of control females. This second important phenomenon, called 'overcoming the poisoning', was observed in all studied species of ticks from several genera. Thus, the slow development of tick poisoning creates a potential for ticks to attach to hosts and to gorge blood, and for infected ticks to transmit pathogens to those hosts, while the ability to overcome the poisoning allows the ticks to survive and makes possible the subsequent trans-stadial and transovarial passage of pathogens. These data can be considered as strong circumstantial evidence of the risk that ticks can present to humans and animals at the initial stages of poisoning after acaricide treatment.

Aging↗
PubMed1997

Utilization of similar mechanisms by Legionella pneumophila to parasitize two evolutionarily distant host cells, mammalian macrophages and protozoa.

The Legionnaires' disease bacterium, Legionella pneumophila, is an intracellular pathogen of humans that is amplified in the environment by intracellular multiplication within protozoa. Within both evolutionarily distant hosts, the bacterium multiplies in a rough endoplasmic reticulum-surrounded phagosome that is retarded from maturation through the endosomal-lysosomal degradation pathway. To gain an understanding of the mechanisms utilized by L. pneumophila to invade and replicate within two evolutionarily distant hosts, we isolated a collection of 89 mini-Tn10::kan insertion mutants that exhibited defects in cytotoxicity, intracellular survival, and replication within both U937 macrophage-like cells and Acanthamoeba polyphaga. Interestingly, the patterns of defects in intracellular survival and replication of the mutants within both host cells were highly similar, and thus we designated the defective loci in these mutants pmi (for protozoan and macrophage infectivity loci). On the basis of their ability to attach to host cells and their growth kinetics during the intracellular infection, the mutants were grouped into five groups. Groups 1 and 2 included 41 mutants that were severely defective in intracellular survival and were completely or substantially killed during the first 4 h of infection in both host cells. Three members of group 1 were severely defective in attachment to both U937 cells and A. polyphaga, and another four mutants of group 1 exhibited severe defects in attachment to A. polyphaga but only a mild reduction in their attachment to U937 cells. Four members of groups 1 and 2 were serum sensitive. Intracellular replication of mutants of the other three groups was less defective than that of mutants of groups 1 and 2, and their growth kinetics within both host cells were similar. The mutants were tested for several other phenotypes in vitro, revealing that 14 of the pmi mutants were resistant to NaCl, 3 had insertions in dot or icm, 3 were aflagellar, 12 were highly intolerant to a hyperosmotic medium, and one failed to grow in a minimal medium. Our data indicated that similar mechanisms are utilized by L. pneumophila to replicate within two evolutionarily distant hosts. Although some mechanisms of attachment to both host cells were similar, other distinct mechanisms were utilized by L. pneumophila to attach to A. polyphaga. Our data supported the hypothesis that preadaptation of L. pneumophila to infection of protozoa may play a major role in its ability to replicate within mammalian cells and cause Legionnaires' disease.

Acanthamoeba↗
PubMed1996

Interactions between Campylobacter jejuni and lipids.

We previously showed that motility plays several key roles in Campylobacter jejuni pathogenesis, including increasing the efficiency of C. jejuni attachment to host epithelial cells. To further characterize C. jejuni attachment, we first examined the role of carbohydrates. Experiments with Chinese hamster ovary (CHO) cell mutants with defined defects in complex carbohydrate biosynthesis revealed that oligosaccharide sequences probably play a subordinate role in C. jejuni attachment to eukaryotic cells. Simple sugars such as mannose, fucose, glucose, N-acetylglucosamine, maltose, and galactose also did not significantly alter the binding of C. jejuni to CHO cells. Thin-layer chromatography overlay analysis with lipids extracted from CHO cells suggested that C. jejuni binds to lipids. Lipid binding was further investigated using a receptor-based enzyme-linked immunosorbent assay. Hydrophobic interactions were determined to play a minor role in binding, since tetramethylurea, a strong inhibitor of hydrophobic interactions, did not significantly decrease binding between C. jejuni and lipids. The interaction was dissected further by comparing the binding of C. jejuni to lipids and their derivatives. The results showed that binding was greatest to the entire lipid structure and decreased in affinity when portions of the lipid were removed. Thin-layer chromatography overlay analysis showed that lipids with unsaturated fatty acids were bound with the highest affinity. Our results suggest that C. jejuni may interact with lipids in host cell membranes. However, lipids only partially inhibited C. jejuni binding to CHO cells, suggesting that multiple interactions occur between the bacteria and host cells.

Animals↗
PubMed1978

Multiple forms of dextran-binding proteins from Streptococcus mutans.

We have isolated a series of five proteins which appear to possess characteristic individual capacities for synthesizing dextrans and binding dextrans. Our suggestion that these proteins comprise an isozyme-like distribution of lectin and enzyme activities is, of course, very speculative and remains to be rigourously confirmed. However, the very identification of these several dextran binding proteins provides a biochemical basis to explain numerous observations suggesting that more than one mechanism for dextran binding is possessed by S. mutans (for instance: 24-27), especially the observations with mutants (24). These proteins probably are the molecular determinants of host infection by S. mutans and may prove to be potent immunogens for use in a vaccine. The presence of a dextran-binding lectin in S. mutans implicates this bacterial lectin in the earliest stage of infection: Attachment to host tissues. The multiplicity of proteins possessing characteristic dextran-synthesizing and dextran-binding capacities indicates the complexity of the adherence mechanisms evolved in S. mutans. Experiments with other bacteria (10-12, 28) suggest that bacterial lectins, in concert with host tissue carbohydrates, may be the molecular mediators of host recognition and subsequent initial attachment of bacterial cells to host tissues in non-pathogenic as well as pathogenic bacteria.

Bacterial Proteins↗
PubMed2002

Molecular mechanisms of adhesion, colonization, and invasion of group A streptococci.

The initial step in establishing a bacterial infection is adhesion of the organism to the epithelium of the host. Group A streptococci use multiple adhesins to attach to host cells and the types of adhesins expressed by a particular strain will determine its tissue specificity. Expression of adhesins is regulated in response to changing environmental and growth conditions. Thus, the array of adhesins expressed by a group A streptococcus will depend on the complement of its adhesin genes and on the environment. Expression of some adhesins may trigger internalization of the streptococci by host cells, which may enable the streptococci to evade antibiotics and to facilitate the penetration of deeper tissues. In this review, we present the different molecular mechanisms of adhesion utilized by group A streptococci and how these interactions lead to colonization and invasion.

Adhesins, Bacterial↗
PubMed1976

Boophilus microplus: cellular responses to larval attachment and their relationship to host resistance.

The histology of early feeding lesions of the cattle tick B. microplus has been studied using 32P labelled larvae to standardize the duration of attachment. Critical studies were made on 3-h lesions in six separate experiments on different groups of British breed animals. Each group consisted of three animals--one previously unexposed to ticks, one of high resistance and one of low resistance. The degree of mast cell disruption, eosinophil concentration and degranulation, and the extent of epidermal vesiculation were all significantly greater at the site of attachment on highly resistant hosts. In previously unexposed animals there was no mobilization of eosinophils nor mast cell breakdown and no epidermal vesiculation. Possible immune mechanisms producing mast cell disruption and the infiltration and concentration of eosinophils are suggested, and the effect of eosinophil degranulation on larval attachment and feeding is discussed.

Animals↗
PubMedDate not supplied

Entry of Coxiella burnetii into host cells.

The attachment to and entry into L mouse fibroblast cells of viable phase I and phase II Nine Mile Coxiella burnetii was investigated. The use of 32P-labelled rickettsiae showed that phase II C. burnetii attached more readily to L cells than phase I organisms; this probably accounts for the more rapid establishment of infection of host cells by the phase II agents. Two lines of evidence indicated that C. burnetii plays a passive role in both attachment and entry into host cells: (1) inactivation of rickettsiae by either heat or glutaraldehyde did not affect either process, and (2) metabolic inhibitors of L cell phagocytic function--NaF and cytochalasin B and D--abolished rickettsiae uptake. These results indicate that it is an endocytotic event. While the presence of purified phase I lipopolysaccharide (LPS) did not interfere with attachment of rickettsiae to the surface of host cells, it markedly impaired entry of C. burnetii in both phases. This suggests that LPS is not an adhesin and that it is toxic to the host cell. Treatment of L cells with either pronase, subtilisin or subtilopeptidase A significantly reduced the number of C. burnetii that adhered to the host cell surface; this result suggests that proteins are either proximate to or components of the C. burnetii attachment site.

Animals↗
PubMedDate not supplied

Location of attachment moiety on Mycoplasma pneumoniae.

Mycoplasma pneumoniae initiates infection in the human host by attachment to respiratory epithelium. The organism attaches by a specialized terminal structure. Monoclonal antibodies to an organism surface protein (P1) inhibited attachment to respiratory epithelium and were localized to the tip structure by a ferritin antibody label. The P1 protein was degraded by trypsin treatment to smaller polypeptides that possessed the same antigenic determinants as the larger P1 protein when reacted with the specific monoclonal antibody, and evidence has been provided for the existence of multiple antigenic determinants on the attachment protein.

Adhesins, Bacterial↗
PubMed2004

Homing of Gyrodactylus salaris and G. derjavini (Monogenea) on different hosts and response post-attachment.

In natural European waters, the congeneric monogeneans Gyrodactylus derjavini Mikailov, 1975 and G. salaris Malmberg, 1957 are primarily found on brown trout Salmo trutta L. and Atlantic salmon Salmo salar L., respectively. Interestingly, rainbow trout, Oncorhynchus mykiss (Walbaum), originating from North America, is as susceptible as brown trout to G. derjavini. However, the mechanisms involved in this host specificity are poorly understood but may include behavioural, mechanical and chemical factors affecting parasite attraction, attachment, feeding, reproduction and host responses. In the present laboratory work, this question has been studied. Detached parasites (either G. derjavini or G. salaris) were offered a choice in small aquaria between fry of rainbow trout, Atlantic salmon and carp Cyprinus carpio L. Within 48 hours more than 90% of G. derjavini colonised rainbow trout and left salmon almost uninfected. Some parasites were found on carp. During the same time span, more than 60% of G. salaris attached to salmon, the rest infected rainbow trout and none were found on carp. Following attachment, the parasites need appropriate stimuli to initiate feeding and reproduction but even such a successful specific colonisation can be followed by a host response. Both humoral and cellular elements have been suggested to participate in these reactions but in the present work it was demonstrated by immunoblotting and immunocytochemistry that no antibodies in host mucus and host plasma bound to any parasite structures or epitopes.

Animals↗
PubMed1990

Sites of attachment in Amblyomma triguttatum triguttatum Koch (Acari: Ixodidae) on natural hosts.

The sites of attachment of Amblyomma triguttatum truguttatum were studied from June to September 1981 on 146 feral pigs (Sus scrofa) and from March to August 1982 and January 1983 on 68 grey kangaroos (Macropus giganteus), naturally infested. Two hundred fifty hour (81%) of 314 nymphs were detected on the ears of the pigs; neither adults nor larvae of A. t. triguttatum were found on S. scrofa. Six hundred ninety four (97%) of 715 larvae; 283 (96%) of 295 nymphs and 11 (79%) of 14 adults of A. t. triguttatum were found on the ears of the kangaroos. The proportion of the larvae and nymphs on the ears of kangaroos and pigs respectively, decreased with the increase of tick load.

Acari↗
PubMedDate not supplied

Heterogeneous distribution of membrane cholesterol at the attachment site of Cryptosporidium muris to host cells.

Distribution of membrane cholesterol at the attachment site of Cryptosporidium muris was investigated by freeze-fracture cytochemistry using a polyene antibiotic filipin. Since the host plasma membrane enveloped C. muris, the inner and outer membranes were continuous with the parasite plasma membrane at the annular ring and with host membrane at the dense band, respectively. Although many filipin-cholesterol complexes were observed on the plasma membrane of host cells and parasites, a line showing no complexes was evident at the above two membrane junctures. These observations indicate that parasitic infection of C. muris altered the organization of membrane cholesterol.

Animals↗
PubMed1999

The Tir-binding region of enterohaemorrhagic Escherichia coli intimin is sufficient to trigger actin condensation after bacterial-induced host cell signalling.

Enterohaemorrhagic Escherichia coli (EHEC) has emerged as an important agent of diarrhoeal disease. Attachment to host cells, an essential step during intestinal colonization by EHEC, is associated with the formation of a highly organized cytoskeletal structure containing filamentous actin, termed an attaching and effacing (A/E) lesion, directly beneath bound bacteria. The outer membrane protein intimin is required for the formation of this structure, as is Tir, a bacterial protein that is translocated into the host cell and is thought to function as a receptor for intimin. To understand intimin function better, we fused EHEC intimin to a homologous protein, Yersinia pseudotuberculosis invasin, or to maltose-binding protein. The N-terminal 539 amino acids of intimin were sufficient to promote outer membrane localization of the C-terminus of invasin and, conversely, the N-terminal 489 amino acids of invasin were sufficient to promote the localization of the C-terminus of intimin. The C-terminal 181 residues of intimin were sufficient to bind mammalian cells that had been preinfected with an enteropathogenic E. coli strain that expresses Tir but not intimin. Binding of intimin derivatives to preinfected cells correlated with binding to recombinant Tir protein. Finally, the 181-residue minimal Tir-binding region of intimin, when purified and immobilized on latex beads, was sufficient to trigger A/E lesions on preinfected mammalian cells.

Actins↗
PubMed1993

Mechanisms of attachment of Mycoplasma arthritidis to host cells in vitro.

Although other investigators have reported that Mycoplasma arthritidis failed to attach to several types of mammalian cells in vitro, we showed that it attached well to rat synovial fibroblasts, lung cells, and skin cells but not to kidney cells, suggesting that receptor sites are unequally expressed or distributed among different rat tissues. M. arthritidis also attached poorly to canine kidney and to baby hamster kidney cells, although it did attach to human fetal lung and fetal amnion cells. Four M. arthritidis strains, two virulent and two avirulent, all attached equally well to rat lung cells. Attachment was inhibited by trypsinization, suggesting that the major adhesins are protein. Fab' fractions of rabbit antisera against four M. arthritidis strains partially inhibited adherence of both homologous and heterologous strains, although not to the same extent, indicating some degree of antigenic heterogeneity among their adhesins. A filter-cloned variant of M. arthritidis 158p10p9, designated LC1, attached poorly compared with the parent strain. Missing from this variant were two proteins migrating within the 81- to 90-kDa range by polyacrylamide gel electrophoresis; in their place was a 24-kDa antigen that may be a truncated version of one of these proteins. A monoclonal antibody that partially inhibited attachment recognized all these peptides by Western immunoblotting. An additional attachment-inhibiting monoclonal antibody recognized a 71-kDa antigen present in both low-adherence and fully adherent populations. The low-adherence variant LC1 induced slightly but significantly less arthritis in Lewis rats than did a fully adherent clone.

Animals↗
PubMed2002

The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica.

Entamoeba histolytica, as its name suggests, is an enteric parasite with a remarkable ability to lyse host tissues. However, the interaction of the parasite with the host is more complex than solely destruction and invasion. It is at the host-parasite interface that cell-signaling events commit the parasite to (a) commensal, noninvasive infection, (b) developmental change from trophozoite to cyst, or (c) invasion and potential death of the human host. The molecule central to these processes is an amebic cell surface protein that recognizes the sugars galactose (Gal) and N-acetylgalactosamine (GalNAc) on the surface of host cells. Engagement of the Gal/GalNAc lectin to the host results in cytoskeletal reorganization in the parasite. The parasite cytoskeleton regulates the extracellular adhesive activity of the lectin and recruits to the host-parasite interface factors required for parasite survival within its host. If the parasite lectin attaches to the host mucin glycoproteins lining the intestine, the result is commensal infection. In contrast, attachment of the lectin to a host cell surface glycoprotein leads to lectin-induced host cell calcium transients, caspase activation, and destruction via apoptosis. Finally, trophozoite quorum sensing via the lectin initiates the developmental pathway resulting in encystment. The structure and function of the lectin that controls these divergent cell biologic processes are the subject of this review.

Amebiasis↗
PubMed1985

An alternative route of infection for viruses: entry by means of the asialoglycoprotein receptor of a Sendai virus mutant lacking its attachment protein.

During the first stage of infection, the paramyxovirus Sendai virus attaches to host cells by recognizing specific receptors on the cell surface. Productive virus-cell interactions result in membrane fusion between the viral envelope and the cell surface membrane. It has recently been shown that the ganglioside GD1a and its more complex homologs GT1b and GQ1b are cell surface receptors for Sendai virus. We report in this paper that the temperature-sensitive mutant ts271 of the Enders strain of Sendai virus lacks the viral attachment protein HN and the biological activities of hemagglutination and sialidase activity associated with it when the virus is grown at 38 degrees C. This HN- virus was unable to infect or agglutinate conventional host cells that contained receptor gangliosides and were readily infected by the parental wild-type virus. The HN- virus did, however, attach to and infect Hep G2 cells, a line of hepatoma cells that retains the asialoglycoprotein receptor (ASGP-R) upon continuous culture. This receptor is a mammalian lectin that recognizes galactose- or N-acetylgalactosamine-terminated proteins. In accordance with the known properties of this receptor, infection by the HN- virus was abolished by treatment of Hep G2 cells with sialidase, by the presence of Ca2+ chelators, and by competition with N-acetylgalactosamine, asialoorosomucoid, and antibody to the receptor. F, the only glycoprotein on the HN- virus, was shown to compete with the galactose-terminated protein asialoorosomucoid for the ASGP-R. The ability of the HN- virus to cause cell-cell fusion of Hep G2 cells indicated that attachment of this virus to the ASGP-R still permitted viral entry by its usual mode--i.e., membrane fusion at the cell surface. These results open up the possibility that enveloped viruses, which contain glycosylated proteins or lipids, may make use of naturally occurring lectins in addition to their normal receptors as a means of attachment to host cells.

Animals↗