Cloning and characterization of an insect apolipoprotein (apolipophorin-II/I) involved in the host immune response of Antheraea pernyi

Di, Wen; Luo, Hao; Li, Tienan; Wu, Chunfu; Zhang, Jinghai; Wang, Xialu; Zhang, Rong

doi:10.1016/j.dci.2017.08.010

Cited by 17 publications

(9 citation statements)

References 42 publications

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“…ApoLps were characterized for their roles in lipid transportation between organs such as fat body, guts, wing discs, and oocytes ( Benoit et al, 2011 ; Palm et al, 2012 ). They have also been implicated in innate immune responses ( Zdybicka-Barabas and Cytryńska, 2013 ; Wen et al, 2017 ). ApoLp-II/I arise from a common precursor protein apoLp, which are invariably present in a 1:1 molar ratio ( Weers et al, 1993 ).…”

Section: Discussionmentioning

confidence: 99%

“…Many apoLp-II/I proteins have been identified from different insect species including ApapoLp-II/I, BmapoLp-II/I, DmapoLp-II/I, and LmapoLp-II/I. They all contain LPD_N, DUF1943, DUF1081, and VWD domains ( Bogerd et al, 2000 ; Hanada et al, 2011 ; Wen et al, 2017 ), indicating that apoLp-II/I proteins are conserved among insect species. As reported by Bogerd et al (2000) , the transcript of LmapoLp-II/I was mainly detected in the fat body and in the brain.…”

Section: Discussionmentioning

confidence: 99%

“…In our work, besides in the fat body, we also found that LmapoLp-II/I was predominantly expressed in the integument, but showed low expression levels in the other tested tissues. Similarly, the transcript of apoLp-II/I in Antheraea pernyi was mainly expressed in the fat body and the integument, but weakly in other tissues ( Wen et al, 2017 ). Thus, the fat body and the integument might be the main tissues expressing apoLp-II/I in insects.…”

Section: Discussionmentioning

confidence: 99%

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Apolipophorin-II/I Contributes to Cuticular Hydrocarbon Transport and Cuticle Barrier Construction in Locusta migratoria

et al. 2020

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Apolipophorins are carrier proteins that bind lipids and mediate their transport from tissue to tissue in animals. Apolipophorin I and II (apoLp-II/I) are the major apolipophorins in insects. The implication of apoLp-II/I in cuticle lipid-barrier formation in insects has not been addressed to date. In the present study, we investigated the function of apoLp-II/I in the migratory locust Locusta migratoria ( LmapoLp-II/I ). During the development of fifth instar nymphs, LmapoLp-II/I transcript levels increased until mid-instar, and then decreased gradually until molting to the adult stage. We found that LmapoLp-II/I was predominately expressed in the fat body and the integument including oenocytes and epidermal cells. Immunodetection experiments revealed that LmapoLp-I mainly localized in the cytoplasm of oenocytes and epidermal cells. Silencing of LmapoLp-II/I caused molting defects in nymphs. Importantly, RNA interference against LmapoLp-II/I resulted in a significant decrease in the content of cuticle surface lipids including alkanes and methyl alkanes. Cuticular permeability was significantly enhanced in these nymphs in Eosin Y penetration assays. By consequence, desiccation resistance and insecticide tolerance of ds LmapoLp-II/I -treated locusts were reduced. Taken together, our results indicate that LmapoLp-II/I is involved in the transport and deposition of surface-cuticular lipids that are crucial for maintaining normal cuticle barrier function in L. migratoria .

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Apolipophorin-II/I Contributes to Cuticular Hydrocarbon Transport and Cuticle Barrier Construction in Locusta migratoria

et al. 2020

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“…Total RNA extracted from the fat body of 5th‐instar larvae was used to obtain the complete cDNA fragment of hexamerin in A. pernyi (Ap ‐hexamerin) as described by Wen et al (). Then, the cDNA sequence was analyzed with several bioinformatics tools.…”

Section: Methodsmentioning

confidence: 99%

A novel hexamerin with an unexpected contribution to the prophenoloxidase activation system of the Chinese oak silkworm, Antheraea pernyi

Liu

Zhu

et al. 2019

Arch Insect Biochem Physiol

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Hexamerin was originally identified as a storage protein but later confirmed to be involved in many physiological processes. In the present study, we cloned and characterized a novel hexamerin complementary DNA sequence from the Chinese oak silkworm, Antheraea pernyi (Ap‐hexamerin), which shows high homology with reported insect methionine‐rich hexamerins. The tissue distribution and time course of expression demonstrated that Ap‐hexamerin was predominantly synthesized in the fat body and the expression level was significantly increased in response to the microbial challenge, suggesting the relevance of Ap‐hexamerin to immune responses. In further immune functional studies, Ap‐hexamerin was confirmed to take part in the upregulation of prophenoloxidase (PPO) activation in A. pernyi haemolymph triggered by pathogen‐associated molecular patterns (PAMPs). Additional molecular interaction analysis revealed that Ap‐hexamerin is capable of binding the PAMPs used in the phenoloxidase assay, suggesting hexamerin in A. pernyi may positively regulate haemolymph PPO activation, acting as a pattern recognition protein.

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“…Apolipoproteins are dispersed in the hemolymph, and function as lipid shuttles (Ryan & van der Horst, ). In addition, apolipoproteins have been shown to mediate immunity in insects, including facilitating encapsulation and bactericidal activity and activating the prophenoloxidase (PPO) system (Wen et al ., ; Yu et al ., ). Transferrins are glycoproteins that permit effective passage of relatively toxic or hydrated ferric ion through the vertebrate vascular system (Huebers & Finch, ; Geiser et al ., ).…”

Section: Introductionmentioning

confidence: 98%

Clathrin‐dependent endocytosis predominantly mediates protein absorption by fat body from the hemolymph in Bombyx mori

Wang

Zhao

et al. 2019

Insect Science

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During insect larval-pupal metamorphosis, proteins in the hemolymph are absorbed by the fat body for the maintenance of intracellular homeostasis; however, the type of proteins and how these proteins are internalized into the fat body are unclear. In Bombyx mori, the developmental profiles of total proteins in the hemolymph and fat body showed that hemolymph-decreased protein bands (55-100 kDa) were in accordance with those protein bands that increased in the fat body. Inhibition of clathrin-dependent endocytosis predominantly blocked the transportation of 55-100 kDa proteins from the hemolymph into the fat body, which was further verified by RNA interference treatment of Bmclathrin. Six hexamerins were shown to comprise ß90% of the total identified proteins in both the hemolymph and fat body by mass spectrum (MS) analysis. In addition, hemolymphspecific proteins were mainly involved in material transportation, while fat body-specific proteins particularly participated in metabolism. In this paper, four hexamerins were found for the first time, and potential proteins absorbed by the fat body from the hemolymph through clathrin-dependent endocytosis were identified. This study sheds light on the protein absorption mechanism during insect metamorphosis.

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Cloning and characterization of an insect apolipoprotein (apolipophorin-II/I) involved in the host immune response of Antheraea pernyi

Cited by 17 publications

References 42 publications

Apolipophorin-II/I Contributes to Cuticular Hydrocarbon Transport and Cuticle Barrier Construction in Locusta migratoria

Apolipophorin-II/I Contributes to Cuticular Hydrocarbon Transport and Cuticle Barrier Construction in Locusta migratoria

A novel hexamerin with an unexpected contribution to the prophenoloxidase activation system of the Chinese oak silkworm, Antheraea pernyi

Clathrin‐dependent endocytosis predominantly mediates protein absorption by fat body from the hemolymph in Bombyx mori

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