Drosophila C-type lectins enhance cellular encapsulation

Ao, Jingqun; Ling, Erjun; Yu, Xiao‐Qiang

doi:10.1016/j.molimm.2006.12.024

Cited by 135 publications

(100 citation statements)

References 47 publications

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“…Positive sites were found to cluster spatially within a known structure of this domain, consistent with positive selection having acted upon a binding function. The sixth gene (CG9134), a C-type lectin, is expressed during eye development (Michaut et al 2003) but is also thought to act as a peptidoglycan recognition protein in innate immunity (Ao et al 2007).…”

Section: Site-specific Analysismentioning

confidence: 99%

Evolutionary rate analyses of orthologs and paralogs from 12 Drosophila genomes

Heger¹,

Ponting²

2007

Genome Res.

123

115

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The newly sequenced genome sequences of 11 Drosophila species provide the first opportunity to investigate variations in evolutionary rates across a clade of closely related species. Protein-coding genes were predicted using established Drosophila melanogaster genes as templates, with recovery rates ranging from 81%-97% depending on species divergence and on genome assembly quality. Orthology and paralogy assignments were shown to be self-consistent among the different Drosophila species and to be consistent with regions of conserved gene order (synteny blocks). Next, we investigated the rates of diversification among these species' gene repertoires with respect to amino acid substitutions and to gene duplications. Constraints on amino acid sequences appear to have been most pronounced on D. ananassae and least pronounced on D. simulans and D. erecta terminal lineages. Codons predicted to have been subject to positive selection were found to be significantly over-represented among genes with roles in immune response and RNA metabolism, with the latter category including each subunit of the Dicer-2/r2d2 heterodimer. The vast majority of gene duplications (96.5%) and synteny rearrangements were found to occur, as expected, within single Müller elements. We show that the rate of ancient gene duplications was relatively uniform. However, gene duplications in terminal lineages are strongly skewed toward very recent events, consistent with either a rapid-birth and rapid-death model or the presence of large proportions of copy number variable genes in these Drosophila populations. Duplications were significantly more frequent among trypsin-like proteases and DM8 putative lipid-binding domain proteins.[Supplemental material is available online at www.genome.org. Multiple alignments, species trees, and orthologous groups can be found at http://genserv.anat.ox.ac.uk/clades/flies.]Of all species, the fruit fly Drosophila melanogaster has perhaps best illuminated the conserved biology of animals. Not only is Drosophila an organism of choice in evolutionary genetics, population genetics, and ecology (Rubin and Lewis 2000), it is also fast becoming one in comparative genomics. To add to the accurate, comprehensive, and well-annotated euchromatic genome of D. melanogaster (Ashburner and Bergman 2005), there are now 11 other Drosophila genomes that recently have been sequenced and assembled (Richards et al. 2005; Drosophila 12 Genomes Consortium 2007). These species sample different branches of the Drosophila phylogeny. Relative to D. melanogaster, four (D. willistoni, D. grimshawi, D. virilis, and D. mojavensis) are divergent species, two (D. pseudoobscura and D. persimilis) are from the obscura group, and five close relatives (D. simulans, D. sechellia, D. yakuba, D. erecta, and D. ananassae) are from the melanogaster subgroup.This broad span of species presents unprecedented opportunities to investigate the evolution, not of a pair, or a few, species as hitherto, but of a diverse clade of species, each associated with ve...

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Section: Site-specific Analysismentioning

confidence: 99%

Evolutionary rate analyses of orthologs and paralogs from 12 Drosophila genomes

Heger¹,

Ponting²

2007

Genome Res.

123

115

View full text Add to dashboard Cite

show abstract

“…Nevertheless, BLL2 was able to efficiently agglutinate all the tested bacteria. In general, agglutination concentration for other C-type lectins described so far are not lower than 0.01 μg/ml [15][16][17][18]20,21], with an average value of about 1 μg/ml. To our knowledge, BLL2 is the lectin with the ability to induce bacterial agglutination at the lowest concentration described so far.…”

Section: Discussionmentioning

confidence: 73%

“…In contrast to the exceptional high activity of BLL2 for bacterial agglutination, the BLL1 and BLL3 showed agglutinating activity at more standard concentrations (0.01-1 μg/ml) [15][16][17][18]. Between the two of them, the BLL1 was showing the lowest values of minimal concentration for the Gramand Gram+ species tested.…”

Section: Resultsmentioning

confidence: 79%

High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from <em>Spodoptera exigua</em> (Lepidoptera: Noctuidae)

Gasmi

Ferré

Herrero

2017

Preprint

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Abstract:Lectins are carbohydrate-interacting proteins playing a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through the carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensor for capturing and identification of bacterial species. In this work, we have characterized the bacterial agglutination properties of three C-type lectins from the Lepidoptera Spodoptera exigua. One of these lectins, BLL2, was able to agglutinate cells from a broad range of bacterial species at an extremely low concentration, becoming a very interesting protein to be used as biosensor or other biotechnological applications involving bacterial capturing.

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“…this multifunction in pathogen recognition has been suspected to be abolished because of protein functional differentiation in arthropods. through pathogen recognition, Prrs further mediate in opsonic effect, benefiting pathogen cleaning, such as agglutination mediated by c-type lectins [2,26,27], antibacterial activity mediated by PGrP-sB1 [16] and sr-enhanced phagocytosis [8]. PtLGBP exhibited obvious agglutination activity against Gram-negative bacteria V. parahaemolyticus, V. alginolyticus, and e. coli; Gram-positive bacteria B. megaterium; and fungi s. cerevisiae.…”

Section: Discussionmentioning

confidence: 99%

PtLGBP, a pattern recognition receptor inPortunus trituberculatusinvolved in the immune response against different challenges

Chen

Jin

Zhao

et al. 2014

Acta Biologica Hungarica

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Lipopolysaccharide and b-1,3-glucan binding protein (LGBP) is a pattern recognition receptor that can recognize and bind LPs and b-1,3-glucan.LGBP has crucial roles in innate immune defense against Gram-negative bacteria and fungi. in this study, LGBP functions in Portunus trituberculatus innate immunity were analyzed. first, the mrna expression of PtLGBP in hemocytes, hepatopancreas, and muscle toward three typical pathogen-associated molecular patterns (PamPs) stimulations were examined using real-time Pcr. results show that the overall trend of relative expressions of the LGBP gene in three tissues is consistent, showing up-down trend. in each group, the highest expression of the LGBP gene was at 3 and 12 h post-injection. The LGBP gene is also expressed significantly higher in the hemocytes and hepatopancreas than in the muscle. the highest level of LGBP was in the lipopolysaccharides (LPs) and glucan-injected group, whereas the lowest level was in the PGn-injected group. furthermore, bacterial agglutination assay with polyclonal antibody specifically for PtLGBP proved that the recombinant PtLGBP (designated as rPtLGBP) could exhibit obvious agglutination activity toward Gramnegative bacteria escherichia coli, Vibrio parahaemolyticus, and V. alginolyticus; Gram-positive bacteria Bacillus subtilis; and fungi saccharomyces cerevisiae. LGBP in Portunus trituberculatus possibly served as a multi-functional Prr. in addition, LGBP is not only involved in the immune response against Gramnegative and fungi, as manifested in other invertebrates, but also has a significant role in anti-Grampositive bacteria infection.

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Drosophila C-type lectins enhance cellular encapsulation

Cited by 135 publications

References 47 publications

Evolutionary rate analyses of orthologs and paralogs from 12 Drosophila genomes

Evolutionary rate analyses of orthologs and paralogs from 12 Drosophila genomes

High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from <em>Spodoptera exigua</em> (Lepidoptera: Noctuidae)

PtLGBP, a pattern recognition receptor inPortunus trituberculatusinvolved in the immune response against different challenges

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