Molecular cloning, expression, purification, and functional characterization of SP‐22 gene from Bombyx mori. Issue 9 (17th May 2019)

• Record Type: Journal Article
• Authors: Salah Eldein, Elshareef; Abdalla, Mohnad; Eltayb, Wafa Ali; El‐Arabey, Amr Ahmed; Ganash, Magdah; Alshammari, Fawaz D.; Barreto, George; Ashraf, Ghulam Md
• Is Part Of: Journal of cellular biochemistry. Volume 120:Issue 9(2019)
• Page Start: 15594
• Page End: 15603
• Publication Date: 2019-05-17
• Subjects: analysis -- Bombyx mori -- cloning -- expression -- serine protease; Cytochemistry -- Periodicals; 572
• DOI: 10.1002/jcb.28826
• Languages: English
• ISSNs: 0730-2312

Abstract

Abstract: Serine protease (SPs) is one of the immune enzyme's molecules that play a main role in the variation of a physiological process by controlling protease actions in vertebrates. For example, signaling cells, protector and improvement, which are included in melanization, are utilized to cascade with the meddling pathogens and defense the harmed tissue in insects. In this study, we explore the biochemical process of (SP‐22) from Bombyx mori . Reverse‐transcription polymerase chain reaction (RT‐PCR) discloses that BmSP‐22 is expressed in all tissues including the fat body. The formative expression profile of BmSP‐22 reveal that BmSP‐22 messenger RNA is expressed constitutively in larvae. Injection of recombinant BmSP‐22 into B. mori larvae reduces significantly the transcript levels of antimicrobial peptides in the fat body. Our results suggest that BmSP‐22 plays an important role in the innate immunity of B. mori and possibly in other insects. Abstract : Serine proteases are implicated in signaling cascades and pathogens defense.We explored the biochemical process of SP‐22 from Bombyx mori. Expression profile of BmSP‐22 shows that BmSP‐22 messenger RNA (mRNA) is expressed constitutively in larvae. Recombinant BmSP‐22 injection reduced mRNA levels of antimicrobial peptides.