Vitellogenin of the parasitoid wasp, Encarsia formosa (Hymenoptera: Aphelinidae): gene organization and differential use by members of the genus

Donnell, David M.

doi:10.1016/j.ibmb.2004.06.011

Cited by 24 publications

(28 citation statements)

References 65 publications

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“…Importantly, the Vtg of decapodan Crustacea is not directly related to the Vtg genes of other taxons, as assumed by others (52)(53)(54)(55)(56)(57)(58)(59)(60), but is an apoB-like LLTP. This observation explains previous phylogenetic analyses on Vtgs only (57,62,69,70), in which decapodan Vtg failed to group with other invertebrate Vtgs. Phylogenetic analysis of the aligned vWF-D modules (in total only z100 aa alignable sequence) also supports the grouping of decapodan Vtg with insect apoLp-II/I and ARP, apart from an unresolved group of other LLTPs with a vWF-D module (data not shown), further supporting the notion that decapodan Vtg is an apoB-like LLTP.…”

Section: Three Families Of Lltpssupporting

confidence: 76%

Molecular diversity and evolution of the large lipid transfer protein superfamily

Smolenaars

Madsen

Rodenburg

et al. 2007

Journal of Lipid Research

158

160

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Circulatory lipid transport in animals is mediated to a substantial extent by members of the large lipid transfer (LLT) protein (LLTP) superfamily. These proteins, including apolipoprotein B (apoB), bind lipids and constitute the structural basis for the assembly of lipoproteins. The current analyses of sequence data indicate that LLTPs are unique to animals and that these lipid binding proteins evolved in the earliest multicellular animals. In addition, two novel LLTPs were recognized in insects. Structural and phylogenetic analyses reveal three major families of LLTPs: the apoB-like LLTPs, the vitellogenin-like LLTPs, and the microsomal triglyceride transfer protein (MTP)-like LLTPs, or MTPs. The latter are ubiquitous, whereas the two other families are distributed differentially between animal groups. Besides similarities, remarkable variations are also found among LLTPs in their major lipid-binding sites (i.e., the LLT module as well as the predicted clusters of amphipathic secondary structure): variations such as protein modification and number, size, or occurrence of the clusters. Strikingly, comparative research has also highlighted a multitude of functions for LLTPs in addition to circulatory lipid transport. The integration of LLTP structure, function, and evolution reveals multiple adaptations, which have come about in part upon neofunctionalization of duplicated genes. Moreover, the change, exchange, and expansion of functions illustrate the opportune application of lipid-binding proteins in nature.Accordingly, comparative research exposes the structural and functional adaptations in animal lipid carriers and brings up novel possibilities for the manipulation of lipid transport.

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Section: Three Families Of Lltpssupporting

confidence: 76%

Molecular diversity and evolution of the large lipid transfer protein superfamily

Smolenaars

Madsen

Rodenburg

et al. 2007

Journal of Lipid Research

158

160

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“…As previously demonstrated, using the NJ method [69], insect Vtg sequences available in databases clustered with high confidence in a group separated from other Vtg sequences, including those of crustaceans apoCr. Vtg sequences representative of five insect orders (Lepidoptera, Diptera, Coleoptera, Hemiptera, and Hymenoptera) were therefore selected for analysis and were: UniProt:Q27309 for silkworm ( Bombyx mori ), UniProt:U60186 for gypsy moth ( Lymantria dispar ), UniProt:U02548 for yellow fever mosquito ( Aedes aegypti ), UniProt:Q05808 for boll weevil ( Anthonomus grandis ), UniProt:U97277 for bean bug ( Riptortus clavatus ), GenBank:NP_001011578 for honey bee ( Apis mellifera ), and GenBank:AF026789 for parasitoid wasp ( Pimpla nipponica ).…”

Section: Methodsmentioning

confidence: 68%

Apolipocrustacein, formerly vitellogenin, is the major egg yolk precursor protein in decapod crustaceans and is homologous to insect apolipophorin II/I and vertebrate apolipoprotein B

Avarre

Lubzens

Babin³

2007

BMC Evol Biol

105

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Background: In animals, the biogenesis of some lipoprotein classes requires members of the ancient large lipid transfer protein (LLTP) superfamily, including the cytosolic large subunit of microsomal triglyceride transfer protein (MTP), vertebrate apolipoprotein B (apoB), vitellogenin (Vtg), and insect apolipophorin II/I precursor (apoLp-II/I). In most oviparous species, Vtg, a large glycolipoprotein, is the main egg yolk precursor protein.Results: This report clarifies the phylogenetic relationships of LLTP superfamily members and classifies them into three families and their related subfamilies. This means that the generic term Vtg is no longer a functional term, but is rather based on phylogenetic/structural criteria. In addition, we determined that the main egg yolk precursor protein of decapod crustaceans show an overall greater sequence similarity with apoLp-II/I than other LLTP, including Vtgs. This close association is supported by the phylogenetic analysis, i.e. neighbor-joining, maximum likelihood and Bayesian inference methods, of conserved sequence motifs and the presence of three common conserved domains: an N-terminal large lipid transfer module marker for LLTP, a DUF1081 domain of unknown function in their central region exclusively shared with apoLp-II/I and apoB, and a von Willebrand-factor type D domain at their C-terminal end. Additionally, they share a conserved functional subtilisin-like endoprotease cleavage site with apoLp-II/I, in a similar location. Conclusion:The structural and phylogenetic data presented indicate that the major egg yolk precursor protein of decapod crustaceans is surprisingly closely related to insect apoLp-II/I and vertebrate apoB and should be known as apolipocrustacein (apoCr) rather than Vtg. These LLTP may arise from an ancient duplication event leading to paralogs of Vtg sequences. The presence of LLTP homologs in one genome may facilitate redundancy, e.g. involvement in lipid metabolism and as egg yolk precursor protein, and neofunctionalization and subfunctionalization, e.g. involvement in clotting cascade and immune response, of extracellular LLTP members. These protein-coding nuclear genes may be used to resolve phylogenetic relationships among the major arthropod groups, especially the Pancrustacea-major splits.

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“…The insect mRNAs are large, ranging from 5441 nt for the honey bee, Apis mellifera (Piulachs et al, 2003) to 6654 nt for the wasp, Encarsia formosa (Donnell, 2004). Crustacean vitellogenin mRNAs range from 7782 to 8012 nt for the prawn, Macrobrachium rosenbergii and the sand shrimp, Mentapenaeus ensis (Tsang et al, 2003), respectively.…”

Section: Introductionmentioning

confidence: 99%

Sequence and the developmental and tissue-specific regulation of the first complete vitellogenin messenger RNA from ticks responsible for heme sequestration

Thompson¹,

Khalil²,

Jeffers³

et al. 2007

Insect Biochemistry and Molecular Biology

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Vitellogenin of the parasitoid wasp, Encarsia formosa (Hymenoptera: Aphelinidae): gene organization and differential use by members of the genus

Cited by 24 publications

References 65 publications

Molecular diversity and evolution of the large lipid transfer protein superfamily

Molecular diversity and evolution of the large lipid transfer protein superfamily

Apolipocrustacein, formerly vitellogenin, is the major egg yolk precursor protein in decapod crustaceans and is homologous to insect apolipophorin II/I and vertebrate apolipoprotein B

Sequence and the developmental and tissue-specific regulation of the first complete vitellogenin messenger RNA from ticks responsible for heme sequestration

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