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Molecular cloning, expression, purification, and functional characterization of SP‐22 gene from Bombyx mori
Author(s) -
Salah Eldein Elshareef,
Abdalla Mohnad,
Eltayb Wafa Ali,
ElArabey Amr Ahmed,
Ganash Magdah,
Alshammari Fawaz D.,
Barreto George,
Ashraf Ghulam Md
Publication year - 2019
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.28826
Subject(s) - bombyx mori , biology , innate immune system , protease , bombyx , recombinant dna , gene , serine protease , messenger rna , microbiology and biotechnology , molecular cloning , gene expression , cloning (programming) , transcription factor , proteases , transcription (linguistics) , enzyme , immune system , biochemistry , genetics , linguistics , philosophy , computer science , programming language
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.