Publication: Identification and characterization of a QM protein as a possible peptidoglycan recognition protein (PGRP) from the giant tiger shrimp Penaeus monodon
Issued Date
2014-01-01
Resource Type
ISSN
18790089
0145305X
0145305X
Other identifier(s)
2-s2.0-84900553144
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Developmental and Comparative Immunology. Vol.46, No.2 (2014), 146-154
Suggested Citation
Attasit Udompetcharaporn, Kingkamon Junkunlo, Saengchan Senapin, Sittiruk Roytrakul, Timothy W. Flegel, Kallaya Sritunyalucksana Identification and characterization of a QM protein as a possible peptidoglycan recognition protein (PGRP) from the giant tiger shrimp Penaeus monodon. Developmental and Comparative Immunology. Vol.46, No.2 (2014), 146-154. doi:10.1016/j.dci.2014.04.003 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/33486
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Identification and characterization of a QM protein as a possible peptidoglycan recognition protein (PGRP) from the giant tiger shrimp Penaeus monodon
Abstract
In an attempt to identify a peptidoglycan recognition protein (PGRP) in Penaeus (Penaeus) monodon, in vitro pull-down binding assays were used between shrimp proteins and purified peptidoglycan (PG). By gel electrophoresis and mass spectrometry followed by Mascot program analysis, proteins from shrimp hemocyte peripheral membrane proteins showed significant homology to records for a QM protein, actin and prophenoloxidase 2 precursor (proPO2), while proteins from cell-free plasma showed significant homology to records for a vitellogenin, a fibrinogen related protein (FREP) and a C-type lectin. Due to time and resource limitations, specific binding to PG was examined only for recombinant PmQM protein and PmLec that were synthesized based on sequences reported in the Genbank database (accession numbers FJ766846 and DQ078266, respectively). An in vitro assay revealed that hemocytes would bind with and encapsulate agarose beads coated with recombinant PmQM (rPmQM) or rPmLec and that melanization followed 2. h post-encapsulation. ELISA tests confirmed specific binding of rPmQM protein to PG. This is the first time that PmQM has been reported as a potential PGRP in shrimp or any other crustacean. The two other potential PGRP identified (FREP and the vitellin-like protein present in male P. monodon, unlike other vitellin subunits) should also be expressed heterologously and tested for their ability to activate shrimp hemocytes. © 2014 Elsevier Ltd.