Serpin-15 from Bombyx mori inhibits prophenoloxidase activation and expression of antimicrobial peptides

Molecular identification, characterization, and expression analysis of a novel trypsin inhibitor-like cysteine-rich peptide from the cotton bollworm, Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae)

“…As HaTIL2 was consistently expressed in the fat body, it shows that the fat body is the major site of serine protease inhibitor genes. Our results are also in accordance with the studies of Chamankhah et al (2003), Li et al (2012) and Liu et al (2015), where serine protease inhibitor genes were highly expressed in the fat body. The HaTIL2 showed high expression at the prepupal stage and 5th, 8th, 9th, and 10th days of pupal stage, whereas it was low on other days of the pupal stage and at the adult stage ( Fig.…”

Characterization and functional analysis of the serpin-10 gene from oak silkworm, Antheraea pernyi (Lepidoptera: Saturniidae)

“…Several serpins in A. pernyi such as serpin-1 (Yu et al, 2017), serpin-3 (Wang et al, 2017) and serpin-14 (Kausar et al, 2017 are reported to be up-regulated after pathogen challenge. Furthermore, serpin-15 mRNA expression increases in the fat body of B. mori following bacterial, fungal and viral injections (Liu et al, 2015). This kind of trend in the expression is also reported for most insect serpins (Danielli et al, 2003;Zheng et al, 2009;Zou et al, 2009;Gulley et al, 2013).…”

Silkworm larvae plasma (SLP) assay for detection of bacteria: False positives secondary to inflammation in vivo

“…Among the steps leading to melanin formation (Fig. 2A), the protease cascade would be remarkably sensitive to interference from exogenous enzymes; indeed, B. mori , similar to other insects, maintains specific protease inhibitors in order to exert control against uncontrolled proteolytic activation in situ [Liu et al , 2015] as well as inhibitors that function at other points in the cascade [Liu et al , 2012]. In an earlier study, [Percopo et al , 2015] we determined that L. plantarum administered to the respiratory mucosa resulted in significant up-regulation of several proteases, including matrix metalloproteinase 12 (29-fold), and cysteine proteases cathepsins B, S and Z (2-, 4-, and 3- fold, respectively; GSE66721).…”