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.
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.


CONCLUSIONS
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.
Avarre
Jean-Christophe
JC
Israel Oceanographic and Limnological Research, P.O. Box 8030, Haifa 31080, Israel.
Lubzens
Esther
E
Babin
Patrick J
PJ
D000818:Animals; D001053:Apolipoproteins / Q000235:genetics*; D001055:Apolipoproteins B / Q000235:genetics*; D002352:Carrier Proteins / Q000235:genetics; D033364:Decapoda / Q000235:genetics*; D010802:Phylogeny; D011498:Protein Precursors / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D014819:Vitellogenins / Q000235:genetics*
D001053:Apolipoproteins; D001055:Apolipoproteins B; D002352:Carrier Proteins; D011498:Protein Precursors; D014819:Vitellogenins; C042470:apolipophorin III; C030363:lipid transfer protein; C106092:microsomal triglyceride transfer protein