Changes in composition and levels of hemolymph proteins during metamorphosis of Manduca sexta

Cao, Xiaolong; Wang, Yan; Rogers, Janet; Hartson, Steve; Kanost, Michael R.; Jiang, Haobo

doi:10.1016/j.ibmb.2020.103489

Cited by 13 publications

(7 citation statements)

References 76 publications

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“…AE4, AE17, and IE1 proteins are present constitutively in hemolymph of larvae, pupae, and adults (Cao et al. , 2020). In contrast, M. sexta FE4‐9, 12, 16, AE(H) 17–19, 36, and IE1, 2 mRNA levels are upregulated in fat body and/or hemocytes after immune challenge (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The enlisted esterases include 61 lipases, 83 COEs, 26 phospholipases, and 13 thioesterases. Proteome verification is based on the previous data (He et al, 2016;Cao et al, 2020). Proteins shaded red were identified in the cell-free hemolymph from larvae 24 h after an immune challenge (He et al, 2016).…”

Section: Disclosurementioning

confidence: 99%

“…Proteins shaded red were identified in the cell-free hemolymph from larvae 24 h after an immune challenge (He et al, 2016). Similarly, those shaded cyan were found in the proteomes of hemolymph at different developmental stages (Cao et al, 2020). Yellow means noncatalytic homolog; green represents lack of the GXSXG motif.…”

Section: Disclosurementioning

confidence: 99%

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Genome‐wide identification, classification, and expression profiling of serine esterases and other esterase‐related proteins in the tobacco hornworm, Manduca sexta

et al. 2022

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Serine esterases (SEs) are hydrolases that catalyze the conversion of carboxylic esters into acids and alcohols. Lipases and carboxylesterases constitute two major groups of SEs. Although over a hundred of insect genomes are known, systematic identification and classification of SEs are rarely performed, likely due to large size and complex composition of the gene family in each species. Considering their key roles in lipid metabolism and other physiological processes, we have categorized 144 M. sexta SEs and SE homologs (SEHs), 114 of which contain a motif of GXSXG. Multiple sequence alignment and phylogenetic tree analysis have revealed 39 neutral lipases (NLs), 3 neutral lipase homologs (NLHs), 11 acidic lipases (ALs), 3 acidic lipase homologs (ALHs), a lipase-3, a triglyceride lipase, a monoglyceride lipase, a hormone-sensitive lipase, and a GDSL lipase. Eighty-three carboxylesterase genes encode 29 α-esterases (AEs), 12 AEHs (e.g., SEH4-1-3), 20 feruloyl esterases (FEs), 2 FEHs, 2 β-esterases (BEs), 2 integument esterases (IEs), 1 IEH, 4 juvenile hormone esterases, 2 acetylcholinesterases, gliotactin, 6 neuroligins, neurotactin, and an uncharacteristic esterase homolog. In addition to these GXSXG proteins, we have identified 26 phospholipases and 13 thioesterases. Expression profiling of these genes in specific tissues and stages has provided insights into their functions including digestion, detoxification, hormone processing, neurotransmission, reproduction, and developmental regulation. In summary, we have established a framework of information on SEs and related proteins in M. sexta to stimulate their research in the model species and comparative investigations in agricultural pests or disease vectors.

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Section: Resultsmentioning

confidence: 99%

Section: Disclosurementioning

confidence: 99%

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Genome‐wide identification, classification, and expression profiling of serine esterases and other esterase‐related proteins in the tobacco hornworm, Manduca sexta

et al. 2022

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“…The resulting peptides were desalted using Omix C18 affinity media, dried, and dissolved in mobile phase A (0.1% formic acid in H 2 O). The samples were loaded onto an Acclaim PepMap RSLC C18 column (75 μm × 50 cm, Thermo Fisher) for data-dependent LC-MS/MS analysis as described previously ( 39 ). Peptides in each sample were separated via a gradient of 0–35% mobile phase B (0.1% formic acid in 80% AcCN) developed over 120 min ( 12 ).…”

Section: Methodsmentioning

confidence: 99%

Two clip-domain serine protease homologs, cSPH35 and cSPH242, act as a cofactor for prophenoloxidase-1 activation in Drosophila melanogaster

Jin,

Wang,

Yin

et al. 2023

Front. Immunol.

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Insect phenoloxidases (POs) catalyze phenol oxygenation and o-diphenol oxidation to form reactive intermediates that kill invading pathogens and form melanin polymers. To reduce their toxicity to host cells, POs are produced as prophenoloxidases (PPOs) and activated by a serine protease cascade as required. In most insects studied so far, PPO activating proteases (PAPs) generate active POs in the presence of a high Mr cofactor, comprising two serine protease homologs (SPHs) each with a Gly residue replacing the catalytic Ser of an S1A serine protease (SP). These SPHs have a regulatory clip domain at the N-terminus, like most of the SP cascade members including PAPs. In Drosophila, PPO activation and PO-catalyzed melanization have been examined in genetic analyses but it is unclear if a cofactor is required for PPO activation. In this study, we produced the recombinant cSPH35 and cSPH242 precursors, activated them with Manduca sexta PAP3, and confirmed their predicted role as a cofactor for Drosophila PPO1 activation by MP2 (i.e., Sp7). The cleavage sites and mechanisms for complex formation and cofactor function are highly similar to those reported in M. sexta. In the presence of high Mr complexes of the cSPHs, PO at a high specific activity of 260 U/μg was generated in vitro. To complement the in vitro analysis, we measured hemolymph PO activity levels in wild-type flies, cSPH35, and cSPH242 RNAi lines. Compared with the wild-type flies, only 4.4% and 18% of the control PO level (26 U/μl) was detected in the cSPH35 and cSPH242 knockdowns, respectively. Consistently, percentages of adults with a melanin spot at the site of septic pricking were 82% in wild-type, 30% in cSPH35 RNAi, and 53% in cSPH242 RNAi lines; the survival rate of the control (45%) was significantly higher than those (30% and 15%) of the two RNAi lines. These data suggest that Drosophila cSPH35 and cSPH242 are components of a cofactor for MP2-mediated PPO1 activation, which are indispensable for early melanization in adults.

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“…Consequently, it plays a crucial role in different physiological processes, including immunity, − clotting, , regulation of diapause, , and reproduction . Furthermore, it has been shown that hemolymph composition can change in different life stages, as observed in Manduca sexta, or nutritional status such as characterized in Drosophila larvae . However, despite its importance to insect physiology, hemolymph and its composition are yet an understudied subject, especially in small insects such as mosquitoes.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes

Alvarenga,

Alves e Silva,

Suzuki

et al. 2024

J. Proteome Res.

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In arthropods, hemolymph carries immune cells and solubilizes and transports nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism, and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label-free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1403 proteins were identified, out of which 447 of them were predicted to be extracellular. In both sexes, almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundances (based on their intensity-based absolute quantification, iBAQ) were 37.9 and 33.2%, respectively. Interestingly, among them, 102 serine proteases/serine protease-homologues were identified, with almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, such as odorantbinding proteins (OBPs) and chemosensory proteins (CSPs), were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of A. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on hemolymph composition.

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Changes in composition and levels of hemolymph proteins during metamorphosis of Manduca sexta

Cited by 13 publications

References 76 publications

Genome‐wide identification, classification, and expression profiling of serine esterases and other esterase‐related proteins in the tobacco hornworm, Manduca sexta

Genome‐wide identification, classification, and expression profiling of serine esterases and other esterase‐related proteins in the tobacco hornworm, Manduca sexta

Two clip-domain serine protease homologs, cSPH35 and cSPH242, act as a cofactor for prophenoloxidase-1 activation in Drosophila melanogaster

Comprehensive Proteomics Analysis of the Hemolymph Composition of Sugar-Fed Aedes aegypti Female and Male Mosquitoes

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