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opencc-by-4.0Nov 2021View details →

Figure 2 in A new order of fishes as hosts of blood flukes (Aporocotylidae); description of a new genus and three new species infecting squirrelfishes (Holocentriformes, Holocentridae) on the Great Barrier Reef

Figure 2. Species of Holocentricola from Great Barrier Reef Holocentridae, whole worms, ventral views. (A) Holocentricola rufus n. sp. ex Sargocentron rubrum from off Heron Island (holotype, QM G239429); (B) Holocentricola exilis n. sp. ex Neoniphon sammara from off Lizard Island (paratype, QM G239111); (C) Holocentricola coronatus n. sp. ex Sargocentron diadema from off Lizard Island (holotype, QM G239125). Scale-bars: A–C, 200 µm.

opencc-by-4.0Dec 2020View details →

Figure 1 in Host conservation through their parasites: molecular surveillance of vector-borne microorganisms in bats using ectoparasitic bat flies

Figure 1. Number of detected vector-borne microorganisms in bats (A) and bat flies (B). Black colour corresponds to Miniopterus natalensis (A), and Nycteribia schmidlii scotti (B), whereas grey shows Miniopterus schreibersii (A) and Nycteribia schmidlii (B).

opencc-by-4.0Dec 2016View details →

Figure 2. Dendrogram resulting from a in Host specificity and the structure of helminth parasite communities of fishes in a Neotropical river in Mexico

Figure 2. Dendrogram resulting from a similarity matrix based on the Sørensen measure for component communities of adult autogenic helminth parasites of 10 fish species from Apazapan, Río La Antigua, Veracruz, Mexico. Host species are: Amex, A. mexicanus; Rgua, R. guatemalensis; Smar, S. marmoratus; Hbim, P. bimaculata; Pmex, Poecilia mexicana; Pgra, Poeciliosis gracilis; Psph, Poecilia sphenops; Xell, X. helleri; Tell, T. ellioti; Vfen, V. fenestrata.

opencc-by-4.0Dec 2016View details →

Figure 1 in Host specificity and the structure of helminth parasite communities of fishes in a Neotropical river in Mexico

Figure 1. Patterns of relative abundance of 24 species of helminths in 11 component communities of freshwater fishes from Río Apazapan, Río La Antigua basin, Mexico (fish species: Am, A. mexicanus; Rg, Rhamdia guatemalensis; Hb, Pseudoxiphophorus bimaculata; Pm, Poecilia mexicana; Ps, P. sphenops; Pg, Poeciliopsis gracilis; Xh, Xiphophorus helleri; Te, Thorichthys helleri; Vf, Vieja fenestrata; Sm, Sicydium gymnogaster).

Figure 1 in Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration

Figure 1. Selection and identification of the stably expressed cell line. (A) Schematic diagram of vector construction. Replacement of the GFP with a sequence containing 50 IgK SP and 30 myc-His sequence using an isocaudamer technique resulted in the creation of pBobi-IMHIP vector. Lentiviral vector pBobi-cathB1 was generated by insertion of Ac-cathB-1 coding sequence excluding SP into the pBobi-IMHIP vector by XbaI and BamHI restriction sites. (B) Lentiviral packaging of pBobi-cathB1 and pBobi-GFP. Under the fluorescence microscope, more than 90% of cells in the pBobi-GFP transfected group displayed green fluorescence. (C) Assessment of the establishment of 293T-cathB1. Anti-Myc IF staining was performed in the two cell lines. All cells in 293T-cathB1 showed red fluorescence representing 100% positive, while all cells in 293T-GFP showed no fluorescence under the red fluorescent filter due to the lack of myc-tag expression. (D) Tests for rAccathB-1 expression. Total RNA and protein samples were extracted from two groups of cells. Results of RT-PCR (top two panels) and western blot (lower two panels) showed that rAc-cathB-1 was highly expressed in 293T-cathB1 at both mRNA and protein levels. Actb, RT-PCR control and B-actin, loading control for western blot; WL, white light; and bar = 100 µm.

Figure 2 in Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration

Figure 2. Purification and identification of rAc-cathB-1. (A) Purification of rAc-cathB-1 from the cell culture supernatant. Lanes: MW, molecular weight markers (listed in kDa on the side); 1, concentrated culture supernatant in binding buffer; 2, column flowthrough; 3, binding buffer wash; 4–6, successive eluate fractions (during the elution step, the eluate was collected in one 5 ml tube after another); 7, eluate from gel filtration. (B) Identification of purified rAc-cathB-1 by western blot with an antiserum against Ac-cathB-1 expressed in E. coli and an anti-Myc antibody.

Figure 5 in Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration

Figure 5. Effects of antiserum on the hydrolytic activity of activated rAc-cathB-1 and larval gut penetration. (A) The inhibition of activated rAc-cathB-1 by antiserum. One microgram of rAc-cathB-1 was activated and incubated with the positive serum (6.0 µg) or negative serum (6.0 µg) for 30 min, respectively, prior to assessment of the degradation of Z-RR-AMC. The hydrolytic reaction was performed at 37 °C for 30 min and the fluorescence of released AMC was measured. All data were presented as relative activities of activated rAc-cathB-1, where the activity of the control (without serum treatment) was taken as 100%. (B) Inhibition of larval penetration ability. Two hundred L3 larvae were pretreated with the undiluted positive serum, the undiluted negative serum, or PBS at 37 °C for 30 min, respectively. The three groups of larvae were separately injected into lumens of rat gut sacks and kept in sterilized Tyrode's solution at 37 °C for 3 h. Each trial was conducted in triplicate and the numbers of larvae remaining in the gut lumen were counted. Numbers of L3 that penetrated the isolated gut were calculated and presented as indicated. Asterisk (*), P <0.05; ns, not significant.

Figure 4 in Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration

Figure 4. Assessment of the hydrolytic activity of activated rAc-cathB-1. (A) Activated rAc-cathB-1 completely degraded fibronectin and laminin but did not cleave type I collagen over a 12-h period. In the incubation buffer (pH 6.0), 10 µg of the respective substrates was treated with equal volumes of PBS, activated rAc-cathB-1, or activated rAc-cathB-1 plus E64 at 37 °C for 12 h. After incubation, all samples were analyzed on a 5% SDS-PAGE gel followed by Coomassie brilliant blue staining. Molecular weight markers (in kDa) are listed on the side. The substrate used for each experiment is indicated at the top of the gel, and the presence or absence of a recombinant protease or protease inhibitor is indicated at the bottom of each lane. (B) Influence of rAc-cathB-1 on IEC-6 monolayer. IEC-6 cells were grown to confluence and equal amounts of rAc-cathB-1 with or without E64 were applied to cells for 2 h. The blank was made of IEC-6 with PBS added. After incubation, the adherent IEC-6 partly rounded up and the integrity of the cell sheet was disrupted by activated rAc-cathB-1. The cytoplasm and ECM were then labeled with an anti-laminin antibody (green), and the nucleus was stained with DAPI. On the merged images, the dark regions represent the intercellular space. (C) Statistical analysis of the changes to the intercellular space of IEC-6 cells. The dark area was measured and analyzed. The difference between the means for each group of samples was estimated using one-way ANOVA followed by Duncan's multiple comparison test. Asterisk (*), P <0.05; WL, white light; ns: not significant; and bar = 100 µm.

Figure 3 in Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetration

Figure 3. Activation and pH-dependence profile of rAc-cathB-1. (A) Processing of rAc-cathB-1. Purified rAc-cathB-1 (0.2 mg/mL) was incubated with activation solution or reference solution in a 2:1 (v/v) ratio. Mixtures were incubated at 37 °C for 30 min, and the reaction was stopped by addition of pepstatin A (Sigma-Aldrich) to a final concentration of 1 mM. Samples were analyzed on a 12% SDS-PAGE gel followed by Coomassie brilliant blue staining. MW, molecular weight markers; purified rAc-cathB-1 incubated with activation solution and reference solution as indicated. (B) Enzymatic activity assay. Z-Arg-Arg-7-amido-4-methylcoumarin hydrochloride was used for studying the activity of pepsin-treated rAc-cathB-1 and the control. The fluorescence was measured with excitation and emission wavelengths of 355 and 460 nm, respectively, and data were presented as relative activities, where activity of the control was taken as 1. (C) The pH-dependence profile of activated rAc-cathB-1. The assay was performed with the fluorescent substrate at a final concentration of 50 µM. Fluorescence was measured and data were presented as relative activities of activated rAc-cathB-1, where the highest activity at the pH optimum was taken as 100%. Asterisk (*), P <0.05.

Fig. 13 in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Fig. 13. Unrooted Maximum-likelihood (ML) consensus tree inferred from 18S SSU rDNA sequences illustrating the phylogenetic position of Trichodina koloti sp. nov. (at the top of the tree in bold), derived from 2551 nucleotide positions. Support values at the nodes are for bootstrap values/Bayesian posterior probabilities (ML/BI). Synonyms for both T. koloti and T. hypsilepis Wellborn, 1967 are indicated in brackets.

Figs 12a–f in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Figs 12a–f. Denticle dimensions, as proposed by van As and Basson (1989; 1992), of Trichodina hypsilepis Wellborn, 1967 (syn. T. heterodentata) as recorded by and redrawn from: a – Population A of Duncan (1977), b – Population B of Duncan (1977), c – from van As and Basson (1989), d – from Tang and Zhao (2007), e – from Pádua et al. (2012), f – from Valladão et al. (2013).

Figs 10a–f in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Figs 10a–f. Denticle dimensions, as by van As and Basson (1989, 1992), of Trichodina koloti sp. nov. representatives from six different populations collected at the Nxamasere Floodplain, where a–e from Sclerophrys gutturalis (Power, 1927) and f – S. poweri (Hewitt, 1935) tadpoles during the 2016 winter (July to August) expedition (scale = 10 µm).

Figs 2–5 in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Figs 2–5. Micrographs of representative Trichodina koloti sp. nov. specimens from each of the six populations measured from the Nxamasere Floodplain; 2 – Haematoxylin stained nuclear material; 3–5 – collected from the skin and gills of Sclerophrys gutturalis (Power, 1927) (scale = 10 µm).

Fig. 1 in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Fig. 1. Map of the Okavango River System in southern Africa, including the Nxamasere Floodplain where Sclerophrys gutturalis (Power, 1923) and S. poweri (Hewitt, 1953) were collected (redrawn and adapted from West et al. 2015) (scale = 200 km).

Figs 11a–f in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Figs 11a–f. Denticle dimensions, as proposed by van As and Basson (1989, 1992), of Trichodina koloti sp. nov. as recorded by and redrawn from: a and b – Arthur and Lom (1984), c – Kruger et al. (1993a), d – Dias et al. (2009), e and f – Pala et al. (2018).

Figs 6–9 in A New Trichodina Species (Peritrichia: Mobilida) from Anuran Tadpole Hosts, Sclerophrys spp. in the Okavango Panhandle, Botswana, with Comments on this Taxon

Figs 6–9. Micrographs of representative Trichodina koloti sp. nov. specimens from each of the six populations measured from the Nxamasere Floodplain; 6–8 – collected from the skin and gills of Sclerophrys gutturalis (Power, 1927); 9 – collected from the skin and gills of S. poweri (Hewitt, 1935) tadpoles during the 2016 winter (July to August) expedition (scale = 10 µm).

opencc-zeroJul 2024View details →

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Data from: A host-adapted auxotrophic gut symbiont induces mucosal immunodeficiency

The microbiome holds great promise as a source of novel therapeutic targets for many diseases. Mining for causative microorganisms that impact processes underlying disease states should utilize Koch's postulates. Here we show a functional screen for the bacterial microbiota of intestinal immunoglobulin A (IgA)-deficient mice; we identified a novel Gram-negative bacterium, proposed to be named as Tomasiella immunophila that induces and degrades IgA in mouse intestine. T. immunophila is auxotrophic for the bacterial cell wall amino sugar N-acetylmuramic acid (MurNAc). T. immunophila secretes IgA-degrading enzymes into outer membrane vesicles that preferentially degrade rodent antibodies with kappa but not lambda light chains. We propose this study uncovers a new paradigm for the role of symbionts in immunodeficiency that can ultimately be applied to human disease.

opencc-by-4.0Dec 2017View details →

Fig.1 in Population Dynamics And Characterization Of Clostridium Macerans On Host Plant Of Flax

Fig.1. The AUDPC of Clostridium macerans as pathogen on the genotypes of flax during ontogenesis. abcd - AUDPC followed by the same letters in each column are not statistically significant by LSD0.05 (1.69).

opencc-by-4.0Dec 2017View details →

Fig.2 in Population Dynamics And Characterization Of Clostridium Macerans On Host Plant Of Flax

Fig.2. Correlation coefficient between disease severity index of Clostridium macerans and sum of precipitation (mm). * − correlation significant at p≤0.05, ** − correlation significant at p≤0.01