MBV infection in various stages of black tiger shrimp (Penaeus monodon)

MBV infection in various stages of Penaeus monodon were studied. In hatcheries, MBV infection was detected early in nauplii stage using PCR technique, whereas rates of infection of 11.15-49.50% were observed in PL1 using histological technique, rising up to 15.26-100% in PL 10. In earthen ponds, the infection in PL15 was initially in the range of 68.68-96.00%. The infection was decreased toward the end of the first, second and third month of rearing period ranging between 13.63-54.83%. The laboratory trial showed that types of feed might affect the rate of MBV infection of larvae. Postlarva fed with artemia showed lowest infection rate at 29.41±7.98%, whereas the infection rates of shrimp fed with minced cockle flesh and commercial feed were 39.09±12.08% and 52.81±11.91, respectively. In stress test trial, a significant MBV infection was detected in the group of larvae that were raised with 25ºC and 34ºC and the salinity at 6 ppt and 18 ppt for 12 hours then rearing in normal condition for 3 days. In the 24 hour-stress trial, and transferred to normal condition for 7 day, the groups that were exposed to stress conditions had significantly higher rates of infection than the control group (p<0.05). The 24 hour - transportationcondition resulted in highest MBV infection rate (73.61±1.25%). From the present study, it was concluded that MBV infection in larvae from hatcheries increases with period of rearing and stress exposure, but the infection tended to decreased with rearing period in earthen pond condition. Proper feeding management and prevention of stress conditions could reduce of MBV infection in black tiger shrimp

Characterization of a Novel Binding Protein for Fortilin/TCTP — Component of a Defense Mechanism against Viral Infection in Penaeus monodon

The Fortilin (also known as TCTP) in Penaeus monodon (PmFortilin) and Fortilin Binding Protein 1 (FBP1) have recently been shown to interact and to offer protection against the widespread White Spot Syndrome Virus infection. However, the mechanism is yet unknown. We investigated this interaction in detail by a number of in silico and in vitro analyses, including prediction of a binding site between PmFortilin/FBP1 and docking simulations. The basis of the modeling analyses was well-conserved PmFortilin orthologs, containing a Ca2+-binding domain at residues 76–110 representing a section of the helical domain, the translationally controlled tumor protein signature 1 and 2 (TCTP_1, TCTP_2) at residues 45–55 and 123–145, respectively. We found the pairs Cys59 and Cys76 formed a disulfide bond in the C-terminus of FBP1, which is a common structural feature in many exported proteins and the “x–G–K–K” pattern of the amidation site at the end of the C-terminus. This coincided with our previous work, where we found the “x–P–P–x” patterns of an antiviral peptide also to be located in the C-terminus of FBP1. The combined bioinformatics and in vitro results indicate that FBP1 is a transmembrane protein and FBP1 interact with N-terminal region of PmFortilin

Automatic synchronization and distribution of biological databases and software over low-bandwidth networks among developing countries

10.1093/bioinformatics/btm570Bioinformatics242299-301BOIN