Effects of Bombyx mori nuclear polyhedrosis virus on serpin and antibacterial peptide expression in B. mori. 2019

Wei-Tao Dong, and Xiao-Dong Ling, and Long-Fei Xiao, and Jun-Jie Hu, and Xing-Xu Zhao, and Ji-Xing Liu, and Yong Zhang
College of Veterinary Medicine, Gansu Agricultural University, Lanzhou, 730070, China.

The silkworm (Bombyx mori) is a typical and economically important lepidopteran species, and research has resulted in the development and accumulation of breeding lines. Studies of immune-related silkworm genes not only promote our understanding of silkworm immune response mechanisms, but they also inform insect immune molecular diversity research. Here, silkworm proteins were screened using proteomics after Bombyx mori nuclear polyhedrosis virus (BmNPV) infection, and 2368 silkworm proteins were identified, including six antimicrobial peptides and 12 serpins. The mRNA expression levels of these 18 proteins were examined at different times. The results indicated that attacin had the highest expression level, while serpin-5 and cecropin-D exhibited a negative regulatory correlation. These results provide a significant step toward a deeper understanding of B. mori immunoregulation.

UI MeSH Term Description Entries
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D012831 Bombyx A genus of silkworm MOTHS in the family Bombycidae of the order LEPIDOPTERA. The family contains a single species, Bombyx mori from the Greek for silkworm + mulberry tree (on which it feeds). A native of Asia, it is sometimes reared in this country. It has long been raised for its SILK and after centuries of domestication it probably does not exist in nature. It is used extensively in experimental GENETICS. (From Borror et al., An Introduction to the Study of Insects, 4th ed, p519) Bombyx mori,Silkmoths,Silkworms,Silkmoth,Silkworm,Bombyx morus,Bombyxs,mori, Bombyx
D015843 Serpins A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition but differ in their specificity toward proteolytic enzymes. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES. Serpin,Serpin Superfamily,Serpin Peptidase Inhibitors,Serpin Protease Inhibitors,Inhibitors, Serpin Peptidase,Inhibitors, Serpin Protease,Peptidase Inhibitors, Serpin,Protease Inhibitors, Serpin,Superfamily, Serpin
D017924 Nucleopolyhedroviruses Genera of the family BACULOVIRIDAE, characterized by the formation of crystalline, polyhedral occlusion bodies in the host cell nucleus. Nucleopolyhedrovirus is the common name for viruses from the Alphabaculovirus, Deltabaculovirus, or Gammabaculovirus genera. Deltabaculovirus,Nuclear Polyhedrosis Virus,Nucleopolyhedrovirus,Alphabaculovirus,Gammabaculovirus,Alphabaculoviruses,Deltabaculoviruses,Gammabaculoviruses,Nuclear Polyhedrosis Viruses,Polyhedrosis Virus, Nuclear,Polyhedrosis Viruses, Nuclear,Virus, Nuclear Polyhedrosis,Viruses, Nuclear Polyhedrosis
D019476 Insect Proteins Proteins found in any species of insect. Insect Protein,Protein, Insect,Proteins, Insect
D020543 Proteome The protein complement of an organism coded for by its genome. Proteomes
D020869 Gene Expression Profiling The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell. Gene Expression Analysis,Gene Expression Pattern Analysis,Transcript Expression Analysis,Transcriptome Profiling,Transcriptomics,mRNA Differential Display,Gene Expression Monitoring,Transcriptome Analysis,Analyses, Gene Expression,Analyses, Transcript Expression,Analyses, Transcriptome,Analysis, Gene Expression,Analysis, Transcript Expression,Analysis, Transcriptome,Differential Display, mRNA,Differential Displays, mRNA,Expression Analyses, Gene,Expression Analysis, Gene,Gene Expression Analyses,Gene Expression Monitorings,Gene Expression Profilings,Monitoring, Gene Expression,Monitorings, Gene Expression,Profiling, Gene Expression,Profiling, Transcriptome,Profilings, Gene Expression,Profilings, Transcriptome,Transcript Expression Analyses,Transcriptome Analyses,Transcriptome Profilings,mRNA Differential Displays
D023181 Antimicrobial Cationic Peptides Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane. Cationic Antimicrobial Peptide,Cationic Antimicrobial Peptides,Cationic Host Defense Peptides,Host Defense Peptide,Microbicidal Cationic Proteins,Amphipathic Cationic Antimicrobial Peptides,Host Defense Peptides,Antimicrobial Peptide, Cationic,Antimicrobial Peptides, Cationic,Cationic Peptides, Antimicrobial,Cationic Proteins, Microbicidal,Defense Peptide, Host,Defense Peptides, Host,Peptide, Cationic Antimicrobial,Peptide, Host Defense,Peptides, Antimicrobial Cationic,Peptides, Cationic Antimicrobial,Peptides, Host Defense,Proteins, Microbicidal Cationic

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