2002
DOI: 10.1016/s0145-305x(01)00081-7
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Calreticulin enriched as an early-stage encapsulation protein in wax moth Galleria mellonella larvae

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Cited by 49 publications
(40 citation statements)
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“…Antibody and Immunochemistry-The generation and use of anti-Draper (14), anti-Croquemort (14), anti-focal adhesion kinase (21), anti-Pretaporter (17), and anti-Calreticulin (22,23) antibodies were reported previously. Anti-Drosophila DmCaBP1 antibody was raised by immunizing rats with recombinant DmCaBP1 expressed in E. coli as a protein fused to GST.…”
Section: Methodsmentioning
confidence: 99%
“…Antibody and Immunochemistry-The generation and use of anti-Draper (14), anti-Croquemort (14), anti-focal adhesion kinase (21), anti-Pretaporter (17), and anti-Calreticulin (22,23) antibodies were reported previously. Anti-Drosophila DmCaBP1 antibody was raised by immunizing rats with recombinant DmCaBP1 expressed in E. coli as a protein fused to GST.…”
Section: Methodsmentioning
confidence: 99%
“…A proleg was amputated, and hemolymph was allowed to drip into an ice-cold, sterile Eppendorf tube containing 1.5 ml of decoagulation buffer (Deco; pH 5.5) prepared as described previously (32) and saturated with phenylthiourea (PTU) to inhibit the prophenoloxidase system. Hemocytes were washed twice by centrifugation at 200 ϫ g for 2 min at 4°C and resuspended as described for each assay below.…”
Section: Insect Rearing and Bleedingmentioning
confidence: 99%
“…These include the highly conserved multifunctional Ca 2ϩ transport protein, calreticulin (32); an 86-kDa protein with sequence homology to insect diapause protein 1 (33); as well as a novel 56-kDa protein (34). The role of calreticulin in mammalian immunity has only recently been reported, but it appears to be important for cell adhesion, Ag presentation, phagocytosis, and inflammation (35).…”
mentioning
confidence: 99%
“…The possible reason might be formation of a nodule requires that circulating haemocytes change from non-adhesive to adhesive cells that are able to bind to the target and one another and this change requires the involvement of plasma (Clark et al, 1997;Choi et al, 2002;Nardi et al, 2005;Shu et al, 2016). Some molecules have been reported to be involved in this process, such as extracellular matrix (ECM) proteins lacunin and the ligand for peanut agglutinin (PNA) lectin in M. sexta (Nardi et al, 2005), calrecticulin in Galleria melonella (Choi et al, 2002), and plasmatocyte spreading peptide (PSP) in the soybean looper moth, Pseudoplusia includens Walker (Lepidoptera: Noctuidae) (Clark et al, 1997) etc. Therefore, we hypothesize that Asian corn borer plasma supplies similar molecules for the nodule formation upon the challenge of B. bassiana conidia.…”
Section: Discussionmentioning
confidence: 99%