Serpin-14 negatively regulates prophenoloxidase activation and expression of antimicrobial peptides in Chinese oak silkworm Antheraea pernyi

Kausar, Saima; Abbas, Muhammad Nadeem; Qian, Cen; Zhu, Bing; Sun, Yu; Sun, Yuxuan; Wang, Lei; Wei, Guoqing; Maqsood, Iram; Liu, Chao-Liang

doi:10.1016/j.dci.2017.05.017

Cited by 43 publications

(23 citation statements)

References 46 publications

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“…Then, fat body was collected at 24, 48 and 72 h post‐injection and the gene expression of BmQM was detected by qRT‐PCR. The expression of PGRPS6 , Gloverin0 , Lysozyme , Moricin , proPO1 and proPO2 were checked after 72 h of BmQM silencing, using specific primers (Table ) (Udompetcharaporn et al ., ; Kausar et al ., ).…”

Section: Methodsmentioning

confidence: 90%

A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein

Zhou

Chen

et al. 2019

Insect Molecular Biology

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The QM gene that encodes for the ribosomal protein L10 was firstly identified from human tumour cells as a tumour suppressor. In this study, a QM gene was identified in silkworm Bombyx mori (BmQM) and its immunomodulatory function was explored. BmQM messenger RNA (mRNA) and protein were highly expressed in the silk gland and fat body, and expressed in all stages of silkworm growth. After challenged with four different microorganisms, the expression levels of BmQM mRNA in fat body or haemocytes were significantly upregulated compared with the control. After knock‐down of BmQM gene, the expressions of some immune genes (PGRPS6, Gloverin0, Lysozyme and Moricin) were affected, and the transcripts of prophenoloxidase1 and prophenoloxidase2 have different degrees of change. The phenoloxidase activity was significantly reduced when the purified recombinant BmQM protein was injected. Recombinant BmQM protein inhibited systemic melanization and suppressed prophenoloxidase activation stimulated by Micrococcus luteus, but it did not affect phenoloxidase activity. Far‐western blotting assays showed that the BmQM protein interacted with silkworm BmJun protein, which negatively regulates AP‐1 expression. Our results indicated that BmQM protein could affect some immune gene expression and negatively regulate the prophenoloxidase‐activating system, and it may play an important role in regulation of the innate immunity in insects.

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Section: Methodsmentioning

confidence: 90%

A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein

Zhou

Chen

et al. 2019

Insect Molecular Biology

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“…In addition to the above mechanisms of serpins acting on proteases to function as host defense factors, there are also other ways that serpins participate in host defense. For example, serpins can induce the expression of host antimicrobial peptides and cytokines ( Kausar et al, 2017 ; Zhao et al, 2014 ). Serpins can also directly bind to bacterial pathogens and cause membrane disruptions ( Malmstrom et al, 2009 ).…”

Section: Survey Methodologymentioning

confidence: 99%

Serpin functions in host-pathogen interactions

Bao

Pan

Poncz

et al. 2018

PeerJ

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Serpins are a broadly distributed superfamily of protease inhibitors that are present in all kingdoms of life. The acronym, serpin, is derived from their function as potent serine proteases inhibitors. Early studies of serpins focused on their functions in haemostasis since modulating serine proteases activities are essential for coagulation. Additional research has revealed that serpins function in infection and inflammation, by modulating serine and cysteine proteases activities. The aim of this review is to summarize the accumulating findings and current understanding of the functions of serpins in host-pathogen interactions, serving as host defense proteins as well as pathogenic factors. We also discuss the potential crosstalk between host and pathogen serpins. We anticipate that future research will elucidate the therapeutic value of this novel target.

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“…In addition, the effect of endogenous Apserpin‐12 on the PPO activation cascade was assayed according to Kausar et al. (). In Brief, 10 μl of hemolymph from Apserpin‐12 ‐dsRNA‐treated A. pernyi larvae was preincubated with 5 μl (0.5 μg/μl) M. luteus at 25°C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Role of Antheraea pernyi serpin 12 in prophenoloxidase activation and immune responses

Kausar

Abbas

Qian

et al. 2017

Arch Insect Biochem Physiol

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Serine protease inhibitors play a key role in the immune system of invertebrates by controlling proteolytic cascades. Besides its importance, the knowledge on immune functions of serpins in most of insects is fragmentary. In the present study, we identified serpin-12 from Antheraea pernyi encoding a predicted 402 amino acid residue protein (Apserpin-12). We expressed the recombinant protein in Escherichia coli and the purified protein was used for the synthesis of rabbit anti-Apserpin-12 polyclonal antibodies and functional studies. Quantitative real-time ploymerase chain reaction (qRT-PCR) analysis revealed that the knock-down of Apserpin-12 enhanced the prophenoloxidase (PPO) cascade stimulated by Micrococcus luteus in hemolymph, whereas addition of recombinant Apserpin-12 protein along with same elicitor led to down-regulate PPO activation. Following different microbial challenge (E. coli, Beauveria bassiana, M. Luteus, and nuclear polyhedrosis virus), the expression of Apserpin-12 mRNA was induced significantly. Furthermore, the Apserpin-12 double-stranded RNA administration elicited the expression of antimicrobial peptides, while the treatment with recombinant protein suppressed their expression. Tissue profile of Apserpin-12 indicated that it is expressed in all examined tissues, that is, hemolymph, malpighian tubules, midgut, silk gland, integument, and fat body with variation in their transcript levels. We concluded that Apserpin-12 may regulate PPO activation and inhibit the production of antimicrobial peptides in A. pernyi, suggesting important role in its immune system.

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Serpin-14 negatively regulates prophenoloxidase activation and expression of antimicrobial peptides in Chinese oak silkworm Antheraea pernyi

Cited by 43 publications

References 46 publications

A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein

A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein

Serpin functions in host-pathogen interactions

Role of Antheraea pernyi serpin 12 in prophenoloxidase activation and immune responses

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