Jul 2026· Journal of Invertebrate Pathology· Vol 219, pp.
108705
· 0 citations· 34 references
Medicine
TL;DR
Findings suggest that BmRNF181 acts as a negative regulator of the silkworm immune response and dramatically increased the expression of antimicrobial peptide genes.
Abstract
The RING finger E3 ligase group is a broadly distributed subfamily of E3 ubiquitin ligases characterized by the presence of a RING domain and is involved in various immunological responses. In this study, Ring finger protein 181 (RNF181) in Bombyx mori (B. mori) was identified and investigated its immunoregulatory function. The BmRNF181 gene is located on chromosome 6 and contains an open reading frame of 441 base pairs, encoding a protein consisting of 146 amino acids. The predicted molecular weight is 16.71 kDa, with a the theoretical isoelectric point of 6.50. The encoded protein possesses a characteristic RING domain and seven predicted phosphorylation sites. The recombinant protein was successfully expressed and purified using the pET-28a-BmRNF181 construct. Quantitative real-time PCR (qRT-PCR) analysis revealed that BmRNF181 was expressed in all examined tissues, with the highest level in the fat body and the lowest in the Malpighian tubules. Developmental expression profiling showed that the highest expression level occurs at the fifth instar larval stage. Following challenge with four different pathogens (Escherichia coli (E. coli), Beauveria bassiana (B. bassiana), Bacillus thuringiensis (B. thuringiensis), and B. mori nuclear polyhedrosis virus (BmNPV)). BmRNF181 expression in the fat body was significantly upregulated. Moreover, RNA interference-mediated knockdown of BmRNF181 dramatically increased the expression of antimicrobial peptide genes. These findings suggest that BmRNF181 acts as a negative regulator of the silkworm immune response.
Toll-like receptors (TLRs) are important pattern recognition receptors involved in crustacean innate immunity. In this study, the full-length cDNA of
HtTLR2
was cloned from the mudflat crab
Helice tientsinensis
using rapid amplification of cDNA ends (RACE). The
HtTLR2
cDNA was 3854 bp in length and contained a 3036-bp open reading frame (ORF) encoding a 1011-amino-acid protein. Bioinformatics analysis showed that the HtTLR2 protein possessed conserved structural features typical of TLR family members. Phylogenetic analysis indicated that HtTLR2 was closely related to Toll2 from
Eriocheir sinensis
. Tissue distribution analysis revealed high
HtTLR2
expression in the gills and hepatopancreas and its expression was significantly upregulated in both tissues following infection with
Vibrio parahaemolyticus
(Fujino et al., 1951) Sakazaki et al., 1963. This study provides new insights into the
TLR
gene family of
H. tientsinensis
and lays a foundation for further investigation of the immune mechanisms of this species.
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Xiao-Yuan Liu, Xing-Yu Zhou, Hao-Ran Wen et al.· Current Issues in Molecular...· 0 citations
S-domain receptor-like kinases (S-RLKs) represent a typical RLK subfamily, which plays key roles in various biological processes in plants. However, the genome-wide evolutionary and functional differentiation of this family remains unclear in rice. In the present study, a comprehensive computational analysis was employed and identified 109 S-RLKs in 9311 genome and 103 S-RLKs in Nipponbare (Nip) genome. The S-RLKs were unevenly distributed across 12 chromosomes. Bioinformatics analysis indicate large-scale gene duplication and family expansion may be the main driving forces for the expansion of S-RLK family members. Although the S-RLKs are highly conserved between the two subspecies, it remains unknown whether these members have undergone functional differentiation during long-term evolution. Given the differences of roots and nitrogen (N) utilization in 9311 and Nip, we focused on the S-RLKs which exhibit different expressions in roots. OsNRS1 (Nitrogen-responsive Root S-domain kinase 1) was selected due to its expression in the roots of 9311 notably more than that in Nip. Phenotypic analysis showed that OsNRS1 CRISPR/Cas9 mutants in 9311 significantly inhibited the length of primary root and total root, and N accumulation, whereas OsNRS1 CRISPR/Cas9 mutants in Nip showed significant functional divergence. In-depth research revealed that these functional divergence of OsNRS1 may be caused by the sequence variation of an auxin response element AuxRR in its promoter. Collectively, this study not only provides novel insights into the evolution of the S-RLK gene family, but also identifies OsNRS1 as a potential key target for the genetic improvement of root and N utilization in rice.
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SiTRAF3 is identified as a pivotal scaffold protein in the echinoid innate immune system, as it significantly drove the promoter activities of nuclear factor kappa-B, activator protein-1, signal transducer and activator of transcription 3, along with multiple inflammatory cytokines and interferon-related elements.
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Ribosomal protein L11 (RPL11) plays important roles in ribosome biogenesis and stress responses, yet its antiviral function remains poorly understood. This study characterized BmRPL11 and its role in Bombyx mori nucleopolyhedrovirus (BmNPV) infection. BmRPL11 is evolutionarily conserved and shares high sequence homology and protein structure with RPL11 from other species. Tissue expression profiling showed predominant BmRPL11 expression in silk glands and the fat body, with upregulation after BmNPV infection. Functional assays demonstrated that BmRPL11 knockdown enhanced, whereas overexpression suppressed, BmNPV proliferation in BmN cells and silkworm larvae. Mechanistically, BmNPV infection induced nuclear export of BmRPL11 and was associated with enhanced apoptosis, while autophagy-related genes were not markedly affected by BmRPL11 knockdown. IP-MS identified candidate BmRPL11-interacting proteins during infection, including RPL5, whereas a canonical murine double minute 2 (MDM2) homologue was not detected. These findings identify BmRPL11 as an antiviral factor in silkworms, potentially acting through an apoptotic rather than an autophagic pathway.
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As an initiating molecule of the classical complement pathway, C1q performs diverse biological functions. In this study, eight C1q genes were identified in Takifugu obscurus and designated as ToC1q1-ToC1q8. Bioinformatics analysis revealed that the proteins encoded by these cDNAs consist of 197-261 amino acids, with varying molecular weights and isoelectric points. SMART domain analysis indicated that all ToC1q proteins contain a signal peptide and a C1q domain, one of which also contains a collagen-like domain. Sequence alignment and phylogenetic analysis showed low sequence similarity among the eight genes, although they exhibited high similarity with their orthologs in T. rubripes and T. flavidus. Pathway analysis revealed that they may be involved in complement-related pathways and may play a role in defense against pathogens. Tissue distribution profiling revealed distinct expression patterns for each gene across different tissues, suggesting potential tissue-specific immune roles. Furthermore, expression pattern analysis following bacterial challenge indicated that the eight genes responded differentially depending on the infection time and bacterial species, with most of them showing significant upregulation upon infection. Collectively, these findings suggest that ToC1q1-ToC1q8 may play important roles in the innate immunity of T. obscurus, participating in the host response to pathogens and sustaining immune function post-infection.
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