Developmental and comparative immunology最新文献

{"title":"Expression of the receptor for IgM (FcμR) by bovine neutrophils","authors":"","doi":"10.1016/j.dci.2024.105235","DOIUrl":"10.1016/j.dci.2024.105235","url":null,"abstract":"<div><p>Bovine neutrophils possess a particular set of receptors for immunoglobulins. They have been shown to express a distinctive receptor for IgG₂, and it has long been known that they interact poorly with IgG₁ but that they can use IgM antibodies as opsonins. We show that the binding of labeled IgM was inhibited by unlabeled IgM but not by IgA, suggesting that bovine neutrophils express a specific IgM receptor. The binding of non-aggregated IgM is strong at 4 °C, but shedding occurs at 37 °C. We designed anti-peptide antibodies based on the sequence of the FcμR, the newly described receptor for IgM. These antibodies bound to bovine neutrophils at 4 °C. At 37 °C, labeling was lost, but the loss was inhibited by pretreatment with cytochalasin D, indicating internalization of the receptor after cross-linking by antibodies. Neutrophils that had internalized the receptor were no longer able to bind IgM. Eosinophils showed a low level of FcμR expression. FcμR expression by neutrophils was not increased by stimulation with Toll-like receptor agonists or the complement anaphylatoxin C5a, and decreased by TNF-α. Exposure of neutrophils to IFN-γ for 18 h increased FcμR expression without augmenting the binding of IgG₁ or IgG₂. We confirmed that bovine neutrophils can use IgM to phagocytose and kill bacteria without the help of Complement. Neutrophils that have migrated into the lumen of inflamed lactating mammary glands expressed the FcμR<em>.</em> These results indicate that bovine neutrophils express an IgM receptor, the FcμR, which is functional to contribute to the opsonophagocytosis of bacteria at inflammatory sites. Expression of the FcμR by neutrophils gives IgM a particular importance for the immune defense in the bovine species.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0145305X24001071/pdfft?md5=bd82025b5761b960e1d88db3716a747e&pid=1-s2.0-S0145305X24001071-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141862595","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analysis of immunoglobulin organization and complexity in mink (Neovison vison)","authors":"","doi":"10.1016/j.dci.2024.105234","DOIUrl":"10.1016/j.dci.2024.105234","url":null,"abstract":"<div><p>Mink are susceptible to viruses such as SARS-CoV-2, H1N1 and H9N2, so they are considered a potential animal model for studying human viral infections. Therefore, it is important to study the immune system of mink. Immunoglobulin (Ig) is an important component of humoral immunity and plays an important role in the body's immune defense. In this study, we described the gene loci structure of mink Ig germline by genome comparison, and analysed the mechanism of expression diversity of mink antibody library by 5′RACE and next-generation sequencing (NGS). The results were as follows: the IgH, Igκ and Igλ loci of mink were located on chromosome 13, chromosome 8 and chromosome 3, respectively, and they had 25, 36 and 7 V genes, 3, 5 and 7 J genes and 10 DH genes, respectively. Mink Ig heavy chain preferred the IGHV1, IGHD2 and IGHJ4 subgroups, κ chain mainly use the IGKV1, IGKJ1 and IGHL4 subgroups, and λ chain mainly use the IGLV3 and IGLJ3 subgroups. Linkage diversity analysis revealed that N nucleotide insertion was the main factor affecting the linkage diversity of mink Igs. On the mutation types of mink Ig Somatic Hypermutation (SHM), the high mutation types of heavy chain were mainly G &gt; A, C &gt; T, T &gt; C, A &gt; G, C &gt; A, G &gt; T, A &gt; C, and T &gt; G; the high mutation types of κ chain were G &gt; A and T &gt; C; and the high mutation types of λ chain were G &gt; A and A &gt; G. The objective of this study was to analyse the loci structure and expression diversity of Ig in mink. The results contribute to our comprehension of Ig expression patterns in mink and were valuable for advancing knowledge in mink immunogenetics, exploring the evolution of adaptive immune systems across different species, and conducting comparative genomics research.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141784759","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tick-Borne pathogens and defensin genes expression: A closer look at Ixodes ricinus and Dermacentor reticulatus","authors":"","doi":"10.1016/j.dci.2024.105231","DOIUrl":"10.1016/j.dci.2024.105231","url":null,"abstract":"<div><p>The immune system of ticks, along with that of other invertebrates, is comparatively simpler than that of vertebrates, relying solely on innate immune responses. Direct antimicrobial defence is provided by the synthesis of antimicrobial peptides (AMPs), including defensins. The aim of this study was to investigate the differences in defensin genes expression between questing and engorged <em>Ixodes ricinus</em> (<em>def1</em> and <em>def2</em>) and <em>Dermacentor reticulatus</em> (<em>defDr</em>) ticks, in the presence of selected pathogens: <em>Borrelia</em> spp., <em>Rickettsia</em> spp., <em>Babesia</em> spp., <em>Anaplasma phagocytophilum</em>, and <em>Neoehrlichia mikurensis</em> in the natural environment. After pathogen screening by PCR/qPCR, the expression of defensin genes in pathogen positive ticks and ticks without any of the tested pathogens, was analysed by reverse transcription qPCR. The results showed an increased expression of defensin genes in <em>I. ricinus</em> ticks after blood feeding and <em>I. ricinus</em> and <em>D. reticulatus</em> ticks during in cases of co-infection. In particular, the expression of defensins genes was higher in questing <em>D. reticulatus</em> than in questing and engorged <em>I. ricinus</em> ticks, when borreliae were detected. This study contributes to uncovering the expression patterns of defensin genes in the presence of several known tick pathogens, the occurrence of these pathogens and possible regulatory mechanisms of defensins in tick vector competence.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0145305X24001034/pdfft?md5=c37a8a96fd6e6754684f03c3a4de1f6d&pid=1-s2.0-S0145305X24001034-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141745579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lack of signal peptide in insect prophenoloxidase to avoid glycosylation to damage the zymogen activity","authors":"","doi":"10.1016/j.dci.2024.105230","DOIUrl":"10.1016/j.dci.2024.105230","url":null,"abstract":"<div><p>Insect prophenoloxidases (PPOs) are important immunity proteins for defending against the invading pathogens and parasites. As a Type-Ⅲ copper-containing proteins, unlike <em>Homo sapiens</em> tyrosinases, the insect PPOs and most bacterial tyrosinases contain no signal peptides for unknown reason, however they can still be released. To this end, we fused different signal peptides to <em>Drosophila melanogaster</em> PPOs for <em>in vitro</em> and <em>in vivo</em> expression, respectively. We demonstrate that an artificial signal peptide can help PPO secretion <em>in vitro</em>. The secreted PPO appeared larger than wild-type PPO on molecular weight sizes due to glycosylation when expressed in S2 cells. Two asparagine residues for potential glycosylation in PPO1 were identified when a signal peptide was fused. After purification, the glycosylated PPO1 lost zymogen activity. When PPO1 containing a signal peptide was over-expressed in <em>Drosophila</em> larvae, the glycosylation and secretion of PPO1 was detected <em>in vivo</em>. Unlike insect PPO, human tyrosinase needs a signal peptide for protein expression and maintaining enzyme activity. An artificial signal peptide fused to bacterial tyrosinase had no influence on the protein expression and enzyme activity. These Type-Ⅲ copper-containing proteins from different organisms may evolve to perform their specific functions. Intriguingly, our study revealed that the addition of calcium inhibits PPO secretion from the transiently cultured larval hindguts <em>in vitro</em>, indicating that the calcium concentration may regulate PPO secretion. Taken together, insect PPOs can maintain enzyme activities without any signal peptide.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141726961","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Complement system molecules: Expression and regulation at the maternal-conceptus interface during pregnancy in pigs","authors":"","doi":"10.1016/j.dci.2024.105229","DOIUrl":"10.1016/j.dci.2024.105229","url":null,"abstract":"<div><p>The complement system, composed of complement components and complement control proteins, plays an essential role in innate immunity. Complement system molecules are expressed at the maternal-conceptus interface, and inappropriate activation of the complement system is associated with various adverse pregnancy outcomes in humans and rodents. However, the expression, regulation, and function of the complement system at the maternal-conceptus interface in pigs have not been studied. In this study, we investigated the expression, localization, and regulation of complement system molecules at the maternal-conceptus interface in pigs. Complement components and complement control proteins were expressed in the endometrium, early-stage conceptus, and chorioallantoic tissues during pregnancy. The expression of complement components acting on the early stage of complement activation increased in the endometrium on Day 15 of pregnancy, with greater levels on that day compared with the estrous cycle. Localization of several complement components and complement control proteins was cell-type specific in the endometrium. The expression of <em>C1QC</em>, <em>C2</em>, <em>C3</em>, <em>C4A</em>, <em>CFI</em>, <em>ITGB2</em>, <em>MASP1</em>, and <em>SERPING1</em> was increased by IFNG in endometrial explant tissues. Furthermore, cleaved C3 fragments were detected in endometrial tissues and uterine flushings on Day 15 of the estrous cycle and Day 15 of pregnancy, with greater levels on Day 15 of pregnancy. These results suggest that complement system molecules in pigs expressed at the maternal-conceptus interface play important roles in the establishment and maintenance of pregnancy by regulating innate immunity and modulating the maternal immune environment during pregnancy.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141616109","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A leukocyte immune-type receptor specific polyclonal antibody recognizes goldfish kidney leukocytes and activates the MAPK pathway in isolated goldfish kidney neutrophil-like cells","authors":"","doi":"10.1016/j.dci.2024.105228","DOIUrl":"10.1016/j.dci.2024.105228","url":null,"abstract":"<div><p>Leukocyte immune-type receptors (LITRs) belong to a large family of teleost immunoregulatory receptors that share phylogenetic and syntenic relationships with mammalian Fc receptor-like molecules (FCRLs). Recently, several putative stimulatory <em>Carassius auratus</em> (Ca)-LITR transcripts, including CaLITR3, have been identified in goldfish. CaLITR3 has four extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain containing a positively charged histidine residue, and a short cytoplasmic tail region. Additionally, the <em>calitr3</em> transcript is highly expressed by goldfish primary kidney neutrophils (PKNs) and macrophages (PKMs). To further investigate the immunoregulatory potential of CaLITR3 in goldfish myeloid cells, we developed and characterized a CaLITR3-epitope-specific polyclonal antibody (anti-CaL3.D1 pAb). We show that the anti-CaL3.D1 pAb stains various hematopoietic cell types within the goldfish kidney, as well as in PKNs and PKMs. Moreover, cross-linking of the anti-CaL3.D1-pAb on PKN membranes induces phosphorylation of p38 and ERK1/2, critical components of the MAPK pathway involved in controlling a wide variety of innate immune effector responses such as NETosis, respiratory burst, and cytokine release. These findings support the stimulatory potential of CaLITR3 proteins as activators of fish granulocytes and pave the way for a more in-depth examination of the immunoregulatory functions of CaLITRs in goldfish myeloid cells.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141598882","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analyses of the Mx family members in lumpfish: Molecular characterization, phylogeny, and gene expression analyses","authors":"","doi":"10.1016/j.dci.2024.105225","DOIUrl":"10.1016/j.dci.2024.105225","url":null,"abstract":"<div><p>Members of the myxovirus resistance (Mx) protein family play an essential role in antiviral immunity. They are Dynamin-like GTPases, induced by interferons. In the current study, we have characterized two predicted <em>MX</em> genes (<em>MX</em>1 and <em>MX</em>2) from lumpfish (<em>Cyclopterus lumpus</em> L.), having 12 and 13 exons, respectively. Mx2 has two isoforms (Mx2-X1 and Mx2-X2) which differ in exon 1. The lumpfish Mx proteins contain an N-terminal Dynamin-like GTPase domain, the middle domain (MD) and GTPase effector domain (GED) characteristic for Mx proteins. Phylogenetic analyses grouped all the lumpfish Mx sequences in group 1, and synteny analyses showed that both genes were localized at chromosome 5 in proximity to the genes Tohc7, Atxn7 and Psmd6. <em>In vitro</em> stimulation experiment showed that both <em>MX1</em> and <em>MX2</em>-X2 were highly upregulated upon exposure to poly(I:C), but not bacteria, 24 h post exposure, indicating their role in antiviral immunity.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141577866","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The involvement of CgRHIM-containing protein in regulating haemocyte apoptosis after high temperature stress in Pacific oyster Crassostrea gigas","authors":"","doi":"10.1016/j.dci.2024.105226","DOIUrl":"10.1016/j.dci.2024.105226","url":null,"abstract":"<div><p>The interactions induced by RIP homotypic interaction motif (RHIM) are essential for the activation of inflammatory signaling and certain cell death pathways. In the present study, a RHIM-containing protein was identified from Pacific oyster <em>Crassostrea gigas</em>, which harbored a RHIM domain and a Death domain (designated <em>Cg</em>RHIM-containing protein). The mRNA transcripts of <em>Cg</em>RHIM-containing protein were constitutively expressed in all the examined tissues of oysters, with the highest expression level in mantle. The <em>Cg</em>RHIM-containing protein was mainly distributed in the cytoplasm of oyster haemocytes. After high temperature stress, the expression levels of <em>Cg</em>Rel and <em>Cg</em>Bcl-2 increased significantly, and reached the peak level at 12 h, then decreased gradually. The transcripts of <em>Cg</em>RHIM-containing protein, <em>Cg</em>caspase-8 and <em>Cg</em>caspase-3 in haemocytes up-regulated at 12 h after high temperature stress. Moreover, the protein abundance of <em>Cg</em>RHIM-containing protein increased significantly, and the ubiquitination level of <em>Cg</em>RHIM-containing protein in haemocytes showed an increasing trend at first and then decreased. After the expression of <em>Cg</em>RHIM-containing protein was knocked down by siRNA, the mRNA expression levels of <em>Cg</em>Rel and <em>Cg</em>Bcl-2 decreased significantly at 6 h after high temperature stress, and those of <em>Cg</em>FADD-like, <em>Cg</em>caspase-8 and <em>Cg</em>caspase-3, as well as the apoptosis rate of haemocytes also decreased significantly at 24 h. These results indicated that <em>Cg</em>RHIM-containing protein might regulate haemocyte apoptosis in oysters upon high temperature stress via mediating the expression of Rel, Bcl-2 and caspase-8/3.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141588188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The involvement of CaMKKI in activating AMPKα in yesso scallop Patinopecten yessoensis under high temperature stress","authors":"Ziling Tong ,&nbsp;Dongli Jiang ,&nbsp;Chuanyan Yang ,&nbsp;Yinan Li ,&nbsp;Zhaoyu He ,&nbsp;Xiaoxue Ma ,&nbsp;Lingling Wang ,&nbsp;Linsheng Song","doi":"10.1016/j.dci.2024.105227","DOIUrl":"10.1016/j.dci.2024.105227","url":null,"abstract":"<div><p>Calcium/calmodulin dependent protein kinase kinase (CaMKK), a highly conserved protein kinase, is involved in the downstream processes of various biological activities by phosphorylating and activating 5′-AMP-activated protein kinase (AMPK) in response to the increase of cytosolic-free calcium (Ca²⁺). In the present study, a CaMKKI was identified from Yesso scallop <em>Patinopecten yessoensis</em>. Its mRNA was ubiquitously expressed in haemocytes and all tested tissues with the highest expression level in mantle. The expression level of <em>Py</em>CaMKKI mRNA in adductor muscle was significantly upregulated at 1, 3 and 6 h after high temperature treatment (25 °C), which was 3.43-fold (<em>p</em> &lt; 0.05), 5.25-fold (<em>p</em> &lt; 0.05), and 5.70-fold (<em>p</em> &lt; 0.05) of that in blank group, respectively. At 3 h after high temperature treatment (25 °C), the protein level of <em>Py</em>AMPKα, as well as the phosphorylation level of <em>Py</em>AMPKα at Thr170 in adductor muscle, and the positive co-localized fluorescence signals of <em>Py</em>CaMKKI and <em>Py</em>AMPKα in haemocyte all increased significantly (<em>p</em> &lt; 0.05) compared to blank group (18 °C). The pull-down assay showed that r<em>Py</em>CaMKKI and r<em>Py</em>AMPKα could bind each other <em>in vitro</em>. After <em>Py</em>CaMKKI was silenced by siRNA, the mRNA and protein levels of <em>Py</em>CaMKKI and <em>Py</em>AMPKα, and the phosphorylation level of <em>Py</em>AMPKα at Thr170 in adductor muscle were significantly down-regulated (<em>p</em> &lt; 0.05) compared with the negative control group receiving an injection of siRNA-NC. These results collectively suggested that <em>Py</em>CaMKKI was involved in the activation of <em>Py</em>AMPKα in response to high temperature stress and would be helpful for understanding the function of <em>Py</em>CaMKKI-<em>Py</em>AMPKα pathway in maintaining energy homeostasis under high temperature stress in scallops.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141572579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A cryptic homotypic interaction motif of insect STING is required for its antiviral signaling","authors":"Xinyi Wang ,&nbsp;Dongmei Wei ,&nbsp;Yumeng Pan,&nbsp;Jinming Liu,&nbsp;Xiaoyi Xiao,&nbsp;Qingyou Xia,&nbsp;Fei Wang","doi":"10.1016/j.dci.2024.105224","DOIUrl":"10.1016/j.dci.2024.105224","url":null,"abstract":"<div><p>Stimulator of interferon genes (STING) mediates innate immune response upon binding to cyclic GMP-AMP (cGAMP). It recruits tank-binding kinase 1 (TBK1) and transcription factor interferon regulatory factor 3 (IRF3) through its C-terminal tail and facilitates TBK1-dependent phosphorylation of IRF3 via forming STING polymers in mammalian cells. However, the mechanism behind STING-mediated activation of NF-κB transcription factor, Relish, in insect cells is unknown. Our study revealed that insect STING formed oligomers and the cryptic RIP homotypic interaction motif (cRHIM) was required for its oligomerization and its anti-viral functions. Cells expressing cRHIM-deficient mutants exhibited lower levels of anti-viral molecules, higher viral load after viral infection and weak activation of Relish. Moreover, we observed that under cGAMP stimulation, insect STING interacted with IMD, and deletion of the cRHIM motif on either protein prevented this interaction. Finally, we demonstrated that cGAMP enhanced the amyloid-like property of insect STING aggregates by ThT staining. In summary, our research showed that insect STING employed a homotypic motif to form intermolecular interactions that are essential for its antiviral signaling.</p></div>","PeriodicalId":11228,"journal":{"name":"Developmental and comparative immunology","volume":null,"pages":null},"PeriodicalIF":2.7,"publicationDate":"2024-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141537691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}