Purification and characterization of haemagglutinin in the haemolymph of the silkworm, Bombyx mori
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Cited by (17)
β-Galactoside binding lectin from caddisfly larvae, Stenopsyche kodaikanalensis with selective modes of antibacterial activity: Purification and characterization
2018, International Journal of Biological MacromoleculesCitation Excerpt :In this study, the purified lectin has a molecular weight of approximately 360 kDa. Similar such high molecular weight lectins ranging from 200 to 300 kDa have also been found in the many insect species [63–67]. The subjection of tryptic digested purified lectin to the MALDI-TOF-MS and subsequent annotation with databases deduced the aminoacid sequence that had considerable homology with putative conserved sequence of mannose/glucose specific lectin from Lathyrus sativus, a leguminous species [68].
Purification, characterization, and analysis of antibacterial activity of a serum lectin from the grub of rhinoceros beetle, Oryctes rhinoceros
2017, Process BiochemistryCitation Excerpt :These results were in accordance with many insect agglutinins reported [39–42]. It has been reported that the galactose-specific lectins from insects Bombyx mori [60], Manduca sexta [61], Drosophila melanogaster [62], Helicoverpa armigera [63], Aedes albopictus [64], and Spodoptera littoralis [7] can agglutinate gram-negative and gram-positive bacteria by binding to carbohydrate moieties on their surface. They also require Ca2+ for their biological activity.
Lectins, as non-self-recognition factors, in crustaceans
2000, AquacultureCitation Excerpt :In view of these observations, Inamori et al. (1999) and Kawabata and Iwanaga (1999) proposed that the innate immune system of the horseshoe crab may recognise invading pathogens through a combinatorial method by using broad and highly specific lectins against molecules exposed on pathogen surface and function synergistically to ensure an effective host defence. Apart from these two well-characterised examples, multiple lectins have also been purified in other insects, such as the silkworm Bombyx mori (Amanai et al., 1990; Yoshida et al., 1996) and the American cockroach Periplaneta americana (Kubo and Natori, 1987; Jomori et al., 1990; Kubo et al., 1990, 1993; Kawasaki et al., 1996). Likewise, in the American horseshoe crab L. polyphemus, multiple lectins have also been isolated (Marchalonis and Edelman, 1968; Oppenheim et al., 1974; Roche and Monsigny, 1974; Robey and Liu, 1981; Brandin and Pistole, 1983; Fujii et al., 1992; Tsuboi et al., 1993).
Effect of lysozyme on the lectin-mediated phagocytosis of Bacillus cereus by haemocytes of the cockroach, Blaberus discoidalis
2000, Journal of Insect PhysiologyCitation Excerpt :This work shows how the insect cellular and humoral antibacterial defences may interact in the removal of foreign microbial invaders. In other insect orders, such as the lepidopteran Bombyx mori, not only are the multiple lectins present (Amanai et al., 1990; Yoshida et al., 1996), but also an array of antibacterial proteins, including lysozyme (Morishima et al., 1995). One of the B. mori lectins is a peptidoglycan-binding protein (Yoshida et al., 1996) which may, as in B. discoidalis, have its opsonic activity modulated by lysozyme present in the haemolymph.
A pattern recognition protein for peptidoglycan: Cloning the cDNA and the gene of the silkworm, Bombyx mori
1999, Journal of Biological Chemistry