PmTBC1D20, a Rab GTPase-activating protein from the black tiger shrimp, Penaeus monodon, is involved in white spot syndrome virus infection.

TBC (TRE2/BUB2/CDC16) domain proteins contain an ≈ 200-amino-acid motif and function as Rab GTPase-activating proteins that are required for regulating the activity of Rab proteins, and so, in turn, endocytic membrane trafficking in cells. TBC domain family member 20 (TBC1D20) has recently been reported to mediate Hepatitis C virus replication. Herein, PmTBC1D20 identified from the black tiger shrimp, Penaeus monodon, was characterized and evaluated for its role in white spot syndrome virus (WSSV) infection.

Genomic structure, expression pattern and functional characterization of crustinPm5, a unique isoform of crustin from Penaeus monodon.

A unique isoform of crustin, crustinPm5, was identified from a gill-epipodite cDNA library of the tiger shrimp, Penaeus monodon. The crustinPm5 cDNA contains an open reading frame (ORF) of 510 bp encoding a 169 amino acid protein. The deduced amino acid sequence of crustinPm5 showed 38% and 37% overall sequence identity with those of crustinPm1 and crustin-likePm, respectively, two crustin isoforms previously reported.